메뉴 건너뛰기




Volumn 27, Issue 6, 2009, Pages 782-798

Methods for detection and characterization of lipases: A comprehensive review

Author keywords

Characterization; Detection; Lipase; Purification

Indexed keywords

CRITICAL REVIEW; DETECTION; ENANTIO; MICROBIAL LIPASE; NONAQUEOUS MEDIA;

EID: 70350004810     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2009.06.001     Document Type: Review
Times cited : (254)

References (263)
  • 1
    • 53749084765 scopus 로고    scopus 로고
    • Production and characterization of a mesophilic lipase isolated from Bacillus stearothermophilus AB-1
    • Apr 15
    • Abada E.A. Production and characterization of a mesophilic lipase isolated from Bacillus stearothermophilus AB-1. Pak J Biol Sci 11 8 (2008) 1100-1106 Apr 15
    • (2008) Pak J Biol Sci , vol.11 , Issue.8 , pp. 1100-1106
    • Abada, E.A.1
  • 2
    • 0038659569 scopus 로고    scopus 로고
    • Purification and partial characterization of psychrotrophic Serratia marcescens lipase
    • Abdou A.M. Purification and partial characterization of psychrotrophic Serratia marcescens lipase. J Dairy Sci 86 1 (2003) 127-132
    • (2003) J Dairy Sci , vol.86 , Issue.1 , pp. 127-132
    • Abdou, A.M.1
  • 3
    • 84985279778 scopus 로고
    • Factors influencing the heat resistance of a heat resistant lipase of Pseudomonas
    • Adams D.M., and Brawely T.G. Factors influencing the heat resistance of a heat resistant lipase of Pseudomonas. J Food Sci 46 (1981) 673-676
    • (1981) J Food Sci , vol.46 , pp. 673-676
    • Adams, D.M.1    Brawely, T.G.2
  • 4
    • 70350011431 scopus 로고    scopus 로고
    • Adipocyte Lipolysis Colorimetric Assay Kit from Zen-Bio, Inc
    • Adipocyte Lipolysis Colorimetric Assay Kit from Zen-Bio, Inc. http://www.biocompare.com/itemdetails.asp?itemid=493883).
  • 5
    • 47649103512 scopus 로고    scopus 로고
    • Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2
    • Amoozegar M.A., Salehghamari E., Khajeh K., Kabiri M., and Naddaf S. Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2. J Basic Microbiol 48 3 (2008) 160-167
    • (2008) J Basic Microbiol , vol.48 , Issue.3 , pp. 160-167
    • Amoozegar, M.A.1    Salehghamari, E.2    Khajeh, K.3    Kabiri, M.4    Naddaf, S.5
  • 6
    • 0018450235 scopus 로고
    • Thermal inactivation of a heat resistant lipase produced by the psychrotrophic bacterium Pseudomonas fluorescens
    • Andersson R.E., Hedlund C.B., and Jonsson U. Thermal inactivation of a heat resistant lipase produced by the psychrotrophic bacterium Pseudomonas fluorescens. J Dai Sci 62 (1979) 361-367
    • (1979) J Dai Sci , vol.62 , pp. 361-367
    • Andersson, R.E.1    Hedlund, C.B.2    Jonsson, U.3
  • 7
    • 0029781203 scopus 로고    scopus 로고
    • Development and evaluation of an ELISA method for the determination of lipoprotein lipase mass concentration: comparison with a commercial, onestep enzyme immunoassay
    • Antikainen M., Suurinkeroinen L., Jauhiainen M., Ehnholm C., and Taskinen M. Development and evaluation of an ELISA method for the determination of lipoprotein lipase mass concentration: comparison with a commercial, onestep enzyme immunoassay. Eur J Clin Chem Clin Biochem 34 (1996) 547-553
    • (1996) Eur J Clin Chem Clin Biochem , vol.34 , pp. 547-553
    • Antikainen, M.1    Suurinkeroinen, L.2    Jauhiainen, M.3    Ehnholm, C.4    Taskinen, M.5
  • 8
    • 0020031598 scopus 로고
    • Conditions for assay of pancreatic lipase from human plasma using a nephelometric technique
    • Arzoglou P.L., Ferard G., Khalfa F., and Metais P. Conditions for assay of pancreatic lipase from human plasma using a nephelometric technique. Clin Chem Acta 119 (1982) 329-345
    • (1982) Clin Chem Acta , vol.119 , pp. 329-345
    • Arzoglou, P.L.1    Ferard, G.2    Khalfa, F.3    Metais, P.4
  • 9
    • 70350001286 scopus 로고
    • Isolation and characterization of intracellular lipase from Serratia marcescens
    • Bachkatova N.A., and Severina L.O. Isolation and characterization of intracellular lipase from Serratia marcescens. Biochem Soc Trans 28 (1980) 771-773
    • (1980) Biochem Soc Trans , vol.28 , pp. 771-773
    • Bachkatova, N.A.1    Severina, L.O.2
  • 10
    • 0002281241 scopus 로고
    • Evaluation of strains of Geotrichum candidum for lipase production and fatty acid specificity
    • Baillargeon M.W., Bistline Jr. R.G., and Sonnet P.E. Evaluation of strains of Geotrichum candidum for lipase production and fatty acid specificity. Appl Microbiol Biotechnol 30 (1989) 92-96
    • (1989) Appl Microbiol Biotechnol , vol.30 , pp. 92-96
    • Baillargeon, M.W.1    Bistline Jr., R.G.2    Sonnet, P.E.3
  • 11
    • 0035021048 scopus 로고    scopus 로고
    • Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part I. Atomic force microscopy
    • Balasheva K., Jensenb T.R., Kjaerb K., and Bjørnholma T. Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part I. Atomic force microscopy. Biochemistry 8 (2001) 387-397
    • (2001) Biochemistry , vol.8 , pp. 387-397
    • Balasheva, K.1    Jensenb, T.R.2    Kjaerb, K.3    Bjørnholma, T.4
  • 12
    • 84883378772 scopus 로고
    • Conductimetric assay of a bacterial lipase, using triacetin as a substrate
    • Ballot C., Favre-Bonvin G., and Wallach J.M. Conductimetric assay of a bacterial lipase, using triacetin as a substrate. Anal Lett 15 (1982) 119-129
    • (1982) Anal Lett , vol.15 , pp. 119-129
    • Ballot, C.1    Favre-Bonvin, G.2    Wallach, J.M.3
  • 13
    • 0021752095 scopus 로고
    • Lipase assay in duodenal juice using a conductimetric method
    • Ballot C., Favre-Bonvin G., and Wallach J.M. Lipase assay in duodenal juice using a conductimetric method. Clin Chim Acta 143 (1984) 109-114
    • (1984) Clin Chim Acta , vol.143 , pp. 109-114
    • Ballot, C.1    Favre-Bonvin, G.2    Wallach, J.M.3
  • 14
    • 46949087369 scopus 로고    scopus 로고
    • Modeling and optimization I: Usability of response surface methodology
    • Baş D., and Boyaci I.H. Modeling and optimization I: Usability of response surface methodology. J Food Eng 78 (2007) 836-845
    • (2007) J Food Eng , vol.78 , pp. 836-845
    • Baş, D.1    Boyaci, I.H.2
  • 15
    • 70350014535 scopus 로고    scopus 로고
    • Production, purification and characterization of thermoalkalophilic lipase for application in bio-detergent industry
    • Bayoumi R.A., El-louboudey S.S., Sidkey N.M., and Abd-El-Rahman M.A. Production, purification and characterization of thermoalkalophilic lipase for application in bio-detergent industry. J Appl Sci Res 3 12 (2007) 1752-1765
    • (2007) J Appl Sci Res , vol.3 , Issue.12 , pp. 1752-1765
    • Bayoumi, R.A.1    El-louboudey, S.S.2    Sidkey, N.M.3    Abd-El-Rahman, M.A.4
  • 16
    • 0030824353 scopus 로고    scopus 로고
    • Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. IHI-91 on olive oil
    • Becker P., Abu-Reesh I., Markossian S., Antranikian G., and Märkl H. Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. IHI-91 on olive oil. Appl Microbiol Biotechnol 48 (1997) 184-190
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 184-190
    • Becker, P.1    Abu-Reesh, I.2    Markossian, S.3    Antranikian, G.4    Märkl, H.5
  • 18
    • 0025908609 scopus 로고
    • Lipoprotein lipase
    • Bensadoun A. Lipoprotein lipase. Annu Rev Nutr 11 (1991) 217-237
    • (1991) Annu Rev Nutr , vol.11 , pp. 217-237
    • Bensadoun, A.1
  • 19
    • 0029563195 scopus 로고    scopus 로고
    • Sandwich-immunoassay for the measurement of human hepatic lipase
    • Bensadoun A. Sandwich-immunoassay for the measurement of human hepatic lipase. Meth Enzymol 263 (1996) 333-338
    • (1996) Meth Enzymol , vol.263 , pp. 333-338
    • Bensadoun, A.1
  • 20
    • 0026697404 scopus 로고
    • Maturation of lipoprotein lipase: expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment
    • Ben-Zeev O., Doolittle M.H., Davis R.C., Elovson J., and Schotz M.C. Maturation of lipoprotein lipase: expression of full catalytic activity requires glucose trimming but not translocation to the cis-Golgi compartment. J Biol Chem 267 (1992) 6219-6227
    • (1992) J Biol Chem , vol.267 , pp. 6219-6227
    • Ben-Zeev, O.1    Doolittle, M.H.2    Davis, R.C.3    Elovson, J.4    Schotz, M.C.5
  • 21
    • 0027931405 scopus 로고
    • Lipoprotein lipase and hepatic lipase: the role of asparagine-linked glycosylation in the expression of a functional enzyme
    • Ben-Zeev O., Stahnke G., Liu G., Davis R.C., and Doolittle M.H. Lipoprotein lipase and hepatic lipase: the role of asparagine-linked glycosylation in the expression of a functional enzyme. J Lipid Res 35 (1994) 1511-1523
    • (1994) J Lipid Res , vol.35 , pp. 1511-1523
    • Ben-Zeev, O.1    Stahnke, G.2    Liu, G.3    Davis, R.C.4    Doolittle, M.H.5
  • 22
    • 0032510716 scopus 로고    scopus 로고
    • Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid
    • Berg O., Cajal Y., Butterfoss G., Grey R., Alsina M., Yu B., et al. Interfacial activation of triglyceride lipase from Thermomyces (Humicola) lanuginosa: kinetic parameters and a basis for control of the lid. Biochem 37 (1998) 6615-6627
    • (1998) Biochem , vol.37 , pp. 6615-6627
    • Berg, O.1    Cajal, Y.2    Butterfoss, G.3    Grey, R.4    Alsina, M.5    Yu, B.6
  • 23
    • 0025801275 scopus 로고
    • Regioselectivity of lipases in organic solvents
    • Berger M., and Schneider M.P. Regioselectivity of lipases in organic solvents. Biotechnol Lett 13 (1991) 333-338
    • (1991) Biotechnol Lett , vol.13 , pp. 333-338
    • Berger, M.1    Schneider, M.P.2
  • 24
    • 85047685160 scopus 로고    scopus 로고
    • Identification, purification, and characterization of a thermally stable lipase from rice bran: a new member of the (phospho) lipase family
    • Bhardwaj K., Raju A., and Rajasekharan R. Identification, purification, and characterization of a thermally stable lipase from rice bran: a new member of the (phospho) lipase family. Plant Physiol 127 (2001) 1728-1738
    • (2001) Plant Physiol , vol.127 , pp. 1728-1738
    • Bhardwaj, K.1    Raju, A.2    Rajasekharan, R.3
  • 25
    • 0019996715 scopus 로고
    • A simple, fully enzymic bioluminescent assay for triglycerides in serum
    • Bjoerkhem I.K., and Sandelin A.T. A simple, fully enzymic bioluminescent assay for triglycerides in serum. Clin Chem 28 (1982) 1742-1744
    • (1982) Clin Chem , vol.28 , pp. 1742-1744
    • Bjoerkhem, I.K.1    Sandelin, A.T.2
  • 26
    • 1542686207 scopus 로고    scopus 로고
    • A semiautomated reflectance colorimetric method for the determination of lipase activity in milk
    • Blake M.R., Koka R., and Weimer B.C. A semiautomated reflectance colorimetric method for the determination of lipase activity in milk. J Dairy Sci 79 (1996) 1164-1171
    • (1996) J Dairy Sci , vol.79 , pp. 1164-1171
    • Blake, M.R.1    Koka, R.2    Weimer, B.C.3
  • 27
    • 34250817483 scopus 로고    scopus 로고
    • Hexadecane and Tween 80 stimulate lipase production in Burkholderia glumae by different mechanisms
    • Boekema B.K.H.L., Beselin A., Breuer M., Hauer B., Koster M., Rosenau F., et al. Hexadecane and Tween 80 stimulate lipase production in Burkholderia glumae by different mechanisms. Appl Environ Microbiol 73 12 (2007) 3838-3844
    • (2007) Appl Environ Microbiol , vol.73 , Issue.12 , pp. 3838-3844
    • Boekema, B.K.H.L.1    Beselin, A.2    Breuer, M.3    Hauer, B.4    Koster, M.5    Rosenau, F.6
  • 28
    • 0027050786 scopus 로고
    • Continuous fluorescence assay for lecithin:cholesterol acyltransferase using a water-soluble phosphatidylcholine
    • Bonelli F.S., and Jonas A. Continuous fluorescence assay for lecithin:cholesterol acyltransferase using a water-soluble phosphatidylcholine. J Lipid Res 33 (1992) 1863-1869
    • (1992) J Lipid Res , vol.33 , pp. 1863-1869
    • Bonelli, F.S.1    Jonas, A.2
  • 29
    • 47349097451 scopus 로고    scopus 로고
    • Production and optimization of thermostable lipase from a thermophilic Bacillus sp LBN 4
    • Bora L., and Kalita M.C. Production and optimization of thermostable lipase from a thermophilic Bacillus sp LBN 4. The Internet Journal of Microbiology 4 1 (2007)
    • (2007) The Internet Journal of Microbiology , vol.4 , Issue.1
    • Bora, L.1    Kalita, M.C.2
  • 31
    • 0026672309 scopus 로고
    • Regulation of the synthesis, processing and translocation of lipoprotein lipase
    • Braun J.E.A., and Severson D.L. Regulation of the synthesis, processing and translocation of lipoprotein lipase. Biochem J 287 (1992) 337-347
    • (1992) Biochem J , vol.287 , pp. 337-347
    • Braun, J.E.A.1    Severson, D.L.2
  • 32
  • 33
    • 0016832061 scopus 로고
    • Partial purification and characterization of the lipase of a facultatively psychrophilic bacterium (Acinetobacter O16)
    • Breuil C., and Kushner D.J. Partial purification and characterization of the lipase of a facultatively psychrophilic bacterium (Acinetobacter O16). Can J Microbiol 21 (1975) 434-441
    • (1975) Can J Microbiol , vol.21 , pp. 434-441
    • Breuil, C.1    Kushner, D.J.2
  • 34
    • 0032622210 scopus 로고    scopus 로고
    • Determining lipoprotein lipase and hepatic lipase activity using radiolabelled substrates
    • Doolittle M., and Reue K. (Eds), Humana Press, Totowa, New Jersey, USA
    • Briquet-Laugier V., Ben-Zeev O., and Doolittle M.H. Determining lipoprotein lipase and hepatic lipase activity using radiolabelled substrates. In: Doolittle M., and Reue K. (Eds). Methods in Molecular Biology (1999), Humana Press, Totowa, New Jersey, USA 81-94
    • (1999) Methods in Molecular Biology , pp. 81-94
    • Briquet-Laugier, V.1    Ben-Zeev, O.2    Doolittle, M.H.3
  • 35
    • 0025221733 scopus 로고
    • Longitudinal study of the biotypes of Gardnerella vaginalis
    • Briselden A.M., and Hillier S.L. Longitudinal study of the biotypes of Gardnerella vaginalis. J Clin Microbiol 28 12 (1990) 2761-2764
    • (1990) J Clin Microbiol , vol.28 , Issue.12 , pp. 2761-2764
    • Briselden, A.M.1    Hillier, S.L.2
  • 36
    • 0019345682 scopus 로고
    • Triglyceride lipase from porcine pancreas
    • Brockman H.L. Triglyceride lipase from porcine pancreas. Methods Enzymol 71 (1981) 619-627
    • (1981) Methods Enzymol , vol.71 , pp. 619-627
    • Brockman, H.L.1
  • 37
    • 0032608440 scopus 로고    scopus 로고
    • Immunological characterization of digestive lipases
    • Doolittle M., and Reue K. (Eds), Humana Press, Totowa, New Jersey
    • Caro A.D., Bezzine S., Lopez V., Aoubala M., Daniel C., Verger R., et al. Immunological characterization of digestive lipases. In: Doolittle M., and Reue K. (Eds). Methods Mol Biol (1999), Humana Press, Totowa, New Jersey 239-256
    • (1999) Methods Mol Biol , pp. 239-256
    • Caro, A.D.1    Bezzine, S.2    Lopez, V.3    Aoubala, M.4    Daniel, C.5    Verger, R.6
  • 39
    • 0024144461 scopus 로고
    • Reversed micelles in biotechnological processes
    • Castro M.J.M., and Cabral J.M.S. Reversed micelles in biotechnological processes. Biotechnol Adv 6 (1988) 151-167
    • (1988) Biotechnol Adv , vol.6 , pp. 151-167
    • Castro, M.J.M.1    Cabral, J.M.S.2
  • 40
    • 0034133889 scopus 로고    scopus 로고
    • Production of extracellular lipases by Penicillium cyclopium purification and characterization of a partial acylglycerol lipase
    • Chahinian H., Vanot G., Ibrik A., Rugani N., Sarda L., and Comeau L.C. Production of extracellular lipases by Penicillium cyclopium purification and characterization of a partial acylglycerol lipase. Biosci Biotechnol Biochem 64 (2000) 215-222
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 215-222
    • Chahinian, H.1    Vanot, G.2    Ibrik, A.3    Rugani, N.4    Sarda, L.5    Comeau, L.C.6
  • 41
    • 84985209726 scopus 로고
    • Purification and some properties of lipase from Streptococcus faecalis
    • Chander H., Ranganathan B., and Singh J. Purification and some properties of lipase from Streptococcus faecalis. J Food Sci 44 (1979) 1747-1751
    • (1979) J Food Sci , vol.44 , pp. 1747-1751
    • Chander, H.1    Ranganathan, B.2    Singh, J.3
  • 42
    • 84985278847 scopus 로고
    • Role of some fatty acids on the growth and lipase production by Streptococcus faecalis
    • Chander H., Ranganathan B., and Singh J. Role of some fatty acids on the growth and lipase production by Streptococcus faecalis. J Food Sci 44 (1979) 1566-1567
    • (1979) J Food Sci , vol.44 , pp. 1566-1567
    • Chander, H.1    Ranganathan, B.2    Singh, J.3
  • 43
    • 70350024660 scopus 로고    scopus 로고
    • Production of a novel lipase from Pichia lynferdii Nrrl Y-7723
    • http://www.ars.usda.gov/research/publications/publications.htm?seq_no_115=145134&pf=1.
    • Chang-Ho C., Jong-Wook H In-Hwan K., Ki-Taek L., Tae-Yol H., and Hou C. Production of a novel lipase from Pichia lynferdii Nrrl Y-7723. Annual Meeting and Expo of the American Oil Chemists' Society May 9 (2003). http://www.ars.usda.gov/research/publications/publications.htm?seq_no_11 5=145134&pf=1 http://www.ars.usda.gov/research/publications/publications.htm?seq_no_115=145134&pf=1.
    • (2003) Annual Meeting and Expo of the American Oil Chemists' Society May 9
    • Chang-Ho, C.1    Jong-Wook H In-Hwan, K.2    Ki-Taek, L.3    Tae-Yol, H.4    Hou, C.5
  • 44
    • 0017114559 scopus 로고
    • Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase
    • Chapus C., Sémériva M., Bovier-Lapierre C., and Desnuelle P. Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase. Biochemistry 15 (1976) 4980-4987
    • (1976) Biochemistry , vol.15 , pp. 4980-4987
    • Chapus, C.1    Sémériva, M.2    Bovier-Lapierre, C.3    Desnuelle, P.4
  • 45
    • 0026580351 scopus 로고
    • Substrate specificities of lipases A and B from Geotrichum candidum CMICC 335426
    • Charton E., and MacRae A.R. Substrate specificities of lipases A and B from Geotrichum candidum CMICC 335426. Biochim Biophys Acta 1123 (1992) 59-64
    • (1992) Biochim Biophys Acta , vol.1123 , pp. 59-64
    • Charton, E.1    MacRae, A.R.2
  • 46
    • 0027624255 scopus 로고
    • Purification and characterization of a novel bioconverting lipase from Pseudomonas aeruginosa MB 5001
    • Chartrain M., Katz L., Marcin C., Thien M., Smith S., Fisher E., et al. Purification and characterization of a novel bioconverting lipase from Pseudomonas aeruginosa MB 5001. Enz Microb Technol 15 (1993) 575-580
    • (1993) Enz Microb Technol , vol.15 , pp. 575-580
    • Chartrain, M.1    Katz, L.2    Marcin, C.3    Thien, M.4    Smith, S.5    Fisher, E.6
  • 47
    • 0031657603 scopus 로고    scopus 로고
    • Production of an alkaline lipase by Acinetobacter radioresistens
    • Chen S.J., Cheng C.Y., and Chen T.L. Production of an alkaline lipase by Acinetobacter radioresistens. J Ferment Bioeng 86 (1998) 308-312
    • (1998) J Ferment Bioeng , vol.86 , pp. 308-312
    • Chen, S.J.1    Cheng, C.Y.2    Chen, T.L.3
  • 48
    • 0031889267 scopus 로고    scopus 로고
    • A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization
    • Choo D.W., Kurihara T., Suzuki T., Soda K., and Esaki N. A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl Environ Microbiol 64 2 (1998) 486-491
    • (1998) Appl Environ Microbiol , vol.64 , Issue.2 , pp. 486-491
    • Choo, D.W.1    Kurihara, T.2    Suzuki, T.3    Soda, K.4    Esaki, N.5
  • 51
    • 0028943623 scopus 로고
    • Purification and properties of an extracellular lipase from the fungus Botrytis cinerea
    • Commenil P., Belingheri L., Sancholle M., and Dehorter B. Purification and properties of an extracellular lipase from the fungus Botrytis cinerea. Lipids 30 (1995) 351-356
    • (1995) Lipids , vol.30 , pp. 351-356
    • Commenil, P.1    Belingheri, L.2    Sancholle, M.3    Dehorter, B.4
  • 52
    • 0033012528 scopus 로고    scopus 로고
    • Production of lipase by soil fungi and partial characterization of lipase from a selected strain (Penicillium wortmanii)
    • Costa M.A., and Peralta R.M. Production of lipase by soil fungi and partial characterization of lipase from a selected strain (Penicillium wortmanii). J Basic Microbiol 39 (1999) 11-15
    • (1999) J Basic Microbiol , vol.39 , pp. 11-15
    • Costa, M.A.1    Peralta, R.M.2
  • 53
    • 0027172476 scopus 로고
    • Medium optimization by a fractional factorial design for lipase production by Rhizopus-delemar
    • Cruz P.M., Christen P., and Farres A. Medium optimization by a fractional factorial design for lipase production by Rhizopus-delemar. J Ferment Bioeng 76 (1993) 94-97
    • (1993) J Ferment Bioeng , vol.76 , pp. 94-97
    • Cruz, P.M.1    Christen, P.2    Farres, A.3
  • 54
    • 0032499653 scopus 로고    scopus 로고
    • How colipase-fatty acid interactions mediate adsorption of pancreatic lipase to interfaces
    • Dahim M., and Brockman H. How colipase-fatty acid interactions mediate adsorption of pancreatic lipase to interfaces. Biochemistry 37 (1998) 8369-8377
    • (1998) Biochemistry , vol.37 , pp. 8369-8377
    • Dahim, M.1    Brockman, H.2
  • 55
    • 0021465162 scopus 로고
    • A new approach to the diagnosis of pancreatic diseases by immunochemical lipase quantitation
    • Jul-Sep
    • Dati F., and Grenner G. A new approach to the diagnosis of pancreatic diseases by immunochemical lipase quantitation. Ric Clin Lab 14 3 (1984) 399-407 Jul-Sep
    • (1984) Ric Clin Lab , vol.14 , Issue.3 , pp. 399-407
    • Dati, F.1    Grenner, G.2
  • 58
    • 0001611648 scopus 로고
    • Potentiometric technic for the measurement of pancreatic lipase activity
    • Desnuelle P., Constantin M.J., and Baldy J. Potentiometric technic for the measurement of pancreatic lipase activity. Bull Soc Chim Biol (Paris) 37 2-3 (1955) 285-290
    • (1955) Bull Soc Chim Biol (Paris) , vol.37 , Issue.2-3 , pp. 285-290
    • Desnuelle, P.1    Constantin, M.J.2    Baldy, J.3
  • 59
    • 0030802019 scopus 로고    scopus 로고
    • Purification and characterization of lipase from a raw-milk yeast (Trichosporon asteroides)
    • Dharmsthiti S., and Ammaranond P. Purification and characterization of lipase from a raw-milk yeast (Trichosporon asteroides). Biotechnol Appl Biochem 26 (1997) 111-116
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 111-116
    • Dharmsthiti, S.1    Ammaranond, P.2
  • 60
    • 0031774033 scopus 로고    scopus 로고
    • Lipase from Pseudomonas aeruginosa LP602: biochemical properties and application for wastewater treatment
    • Dharmsthiti S., and Kuhasuntisuk B. Lipase from Pseudomonas aeruginosa LP602: biochemical properties and application for wastewater treatment. J Industr Microbiol Biotechnol 21 (1998) 75-80
    • (1998) J Industr Microbiol Biotechnol , vol.21 , pp. 75-80
    • Dharmsthiti, S.1    Kuhasuntisuk, B.2
  • 61
    • 0032843146 scopus 로고    scopus 로고
    • Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027
    • Dharmsthiti S., and Luchai S. Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027. FEMS Microbiol Lett 179 (1999) 241-246
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 241-246
    • Dharmsthiti, S.1    Luchai, S.2
  • 62
    • 0033380198 scopus 로고    scopus 로고
    • Purification and characterization of a Pseudomonas sp. lipase and its properties in non-aqueous media
    • Dong H., Gao S., Han S.p., and Cao S.g. Purification and characterization of a Pseudomonas sp. lipase and its properties in non-aqueous media. Biotechnol Appl Biochem 30 (1999) 251-256
    • (1999) Biotechnol Appl Biochem , vol.30 , pp. 251-256
    • Dong, H.1    Gao, S.2    Han, S.p.3    Cao, S.g.4
  • 63
    • 0031977244 scopus 로고    scopus 로고
    • Enhanced detection of lipoprotein lipase by combining immunoprecipitation with Western blot analysis
    • Doolittle M.H., Ben-Zeev O., and Briquet-Laugier V. Enhanced detection of lipoprotein lipase by combining immunoprecipitation with Western blot analysis. J Lipid Res 39 (1998) 934-942
    • (1998) J Lipid Res , vol.39 , pp. 934-942
    • Doolittle, M.H.1    Ben-Zeev, O.2    Briquet-Laugier, V.3
  • 64
    • 0002322351 scopus 로고
    • The colorimetric determination of long- chain fatty acids in the 0.05-0.5 μmol range
    • Duncombe W.G. The colorimetric determination of long- chain fatty acids in the 0.05-0.5 μmol range. Biochem J 88 (1963) 7
    • (1963) Biochem J , vol.88 , pp. 7
    • Duncombe, W.G.1
  • 65
    • 70350564289 scopus 로고    scopus 로고
    • Production and characterization of an alkaline thermostable crude lipase from an isolated strain of Bacillus cereus C(7)
    • Feb. 06 (Electronic publication a head of print)
    • Dutta S., and Ray L. Production and characterization of an alkaline thermostable crude lipase from an isolated strain of Bacillus cereus C(7). Appl Biochem Biotechnol (2009) Feb. 06 (Electronic publication a head of print)
    • (2009) Appl Biochem Biotechnol
    • Dutta, S.1    Ray, L.2
  • 66
    • 60249084620 scopus 로고    scopus 로고
    • A modeling study by response surface methodology and artificial neural network on culture parameters optimization for thermostable lipase production from a newly isolated thermophilic Geobacillus sp. strain ARM
    • Ebrahimpour A., Abd Rahman R.N., Ean Ch'ng D.H., Basri M., and Salleh A.B. A modeling study by response surface methodology and artificial neural network on culture parameters optimization for thermostable lipase production from a newly isolated thermophilic Geobacillus sp. strain ARM. BMC Biotechnol 8 (2008) 96
    • (2008) BMC Biotechnol , vol.8 , pp. 96
    • Ebrahimpour, A.1    Abd Rahman, R.N.2    Ean Ch'ng, D.H.3    Basri, M.4    Salleh, A.B.5
  • 67
    • 0029044979 scopus 로고
    • Enzymatic properties of lipase and characteristics production by Lactobacillus delbrueckii subsp. bulgaricus
    • El-Sawah M.M., Sherief A.A., and Bayoumy S.M. Enzymatic properties of lipase and characteristics production by Lactobacillus delbrueckii subsp. bulgaricus. Antonie Van Leeuwenhoek 67 (1995) 357-362
    • (1995) Antonie Van Leeuwenhoek , vol.67 , pp. 357-362
    • El-Sawah, M.M.1    Sherief, A.A.2    Bayoumy, S.M.3
  • 68
    • 0031194286 scopus 로고    scopus 로고
    • Production, purification and characterization of Bacillus lipase
    • El-Shafei H.A., and Rezkallah L.A. Production, purification and characterization of Bacillus lipase. Microbiol Res 152 (1997) 199-208
    • (1997) Microbiol Res , vol.152 , pp. 199-208
    • El-Shafei, H.A.1    Rezkallah, L.A.2
  • 69
    • 1842309224 scopus 로고
    • Characteristics of lipases in the growth filtrate dialysate of Bacillus stearothermophilus grown at 55 °C using a tributyrin cup-plate assay
    • Elwan S.H., El-Nagger M.R., and Ammar M.B. Characteristics of lipases in the growth filtrate dialysate of Bacillus stearothermophilus grown at 55 °C using a tributyrin cup-plate assay. Bull Fac Sci 8 (1977) 105-119
    • (1977) Bull Fac Sci , vol.8 , pp. 105-119
    • Elwan, S.H.1    El-Nagger, M.R.2    Ammar, M.B.3
  • 71
    • 0020784001 scopus 로고
    • Lipases production by Bacillus circulans under mesophilic and osmophilic conditions. Factors affecting lipases production
    • Elwan S.H., el-Hoseiny M.M., Ammar M.S., and Mostafa S.A. Lipases production by Bacillus circulans under mesophilic and osmophilic conditions. Factors affecting lipases production. G Bacteriol Virol Immunol 76 (1983) 187-199
    • (1983) G Bacteriol Virol Immunol , vol.76 , pp. 187-199
    • Elwan, S.H.1    el-Hoseiny, M.M.2    Ammar, M.S.3    Mostafa, S.A.4
  • 72
    • 0027419914 scopus 로고
    • Thermoalkalophilic lipase-producing Bacillus selected by continuous cultivation
    • Emanuilova E., Kambourova M., Dekovska M., and Manolov R. Thermoalkalophilic lipase-producing Bacillus selected by continuous cultivation. FEMS Microbiol Lett 108 (1993) 247-250
    • (1993) FEMS Microbiol Lett , vol.108 , pp. 247-250
    • Emanuilova, E.1    Kambourova, M.2    Dekovska, M.3    Manolov, R.4
  • 73
    • 0024532911 scopus 로고
    • Simple high performance liquid chromatography methods for monitoring lipase reactions
    • Ergan F., and Andre G. Simple high performance liquid chromatography methods for monitoring lipase reactions. Lipids 24 (1989) 76-78
    • (1989) Lipids , vol.24 , pp. 76-78
    • Ergan, F.1    Andre, G.2
  • 74
    • 35548970149 scopus 로고    scopus 로고
    • Isolation of lipase producing Bacillus sp. from olive mill wastewater and improving its enzyme activity
    • Ertuǧrul S., Dönmez G., and Takaç S. Isolation of lipase producing Bacillus sp. from olive mill wastewater and improving its enzyme activity. J Hazard Mater 149 3 (2007) 720-724
    • (2007) J Hazard Mater , vol.149 , Issue.3 , pp. 720-724
    • Ertuǧrul, S.1    Dönmez, G.2    Takaç, S.3
  • 75
    • 0025308037 scopus 로고
    • Nutritional factors affecting lipase production by Rhizopus delemar CDBB H313
    • Espinosa E., Sanchez S., and Farres A. Nutritional factors affecting lipase production by Rhizopus delemar CDBB H313. Biotechnol Lett 12 (1990) 209-214
    • (1990) Biotechnol Lett , vol.12 , pp. 209-214
    • Espinosa, E.1    Sanchez, S.2    Farres, A.3
  • 76
    • 0015921543 scopus 로고
    • Effects of surface pressure on the hydrolysis of ester monolayers by pancreatic lipase
    • Espostio S., Semeriva M., and Desnuelle P. Effects of surface pressure on the hydrolysis of ester monolayers by pancreatic lipase. Biochim Biophys Acta 302 (1973) 293-304
    • (1973) Biochim Biophys Acta , vol.302 , pp. 293-304
    • Espostio, S.1    Semeriva, M.2    Desnuelle, P.3
  • 77
    • 0036234329 scopus 로고    scopus 로고
    • Effects of carbon and nitrogen sources on lipase production by Candida rugosa
    • Fadiloglu S., and Erkmen O.s.m.a.n. Effects of carbon and nitrogen sources on lipase production by Candida rugosa. Turkish J Eng Env Sci 26 (2002) 249-254
    • (2002) Turkish J Eng Env Sci , vol.26 , pp. 249-254
    • Fadiloglu, S.1    Erkmen, O.s.m.a.n.2
  • 78
    • 0031670591 scopus 로고    scopus 로고
    • Microbial growth and lipolytic activities of moderate thermophilic bacterial strains
    • Fakhreddine L., Kademi A., Ait-Abdelkader N., and Baratti J.C. Microbial growth and lipolytic activities of moderate thermophilic bacterial strains. Biotechnol Lett 20 (1998) 879-883
    • (1998) Biotechnol Lett , vol.20 , pp. 879-883
    • Fakhreddine, L.1    Kademi, A.2    Ait-Abdelkader, N.3    Baratti, J.C.4
  • 79
    • 0025752822 scopus 로고
    • Studies on the production of lipase from recombinant Staphylococcus carnosus
    • Falk M.P.F., Sanders E.A., and Deckwer W.D. Studies on the production of lipase from recombinant Staphylococcus carnosus. Appl Microbiol Biotechnol 35 (1991) 10-13
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 10-13
    • Falk, M.P.F.1    Sanders, E.A.2    Deckwer, W.D.3
  • 80
    • 0030928763 scopus 로고    scopus 로고
    • A critical re-evaluation of the phenomenon of "interfacial activation"
    • Dennis E., and Rubin B. (Eds), Academic Press, New York
    • Ferrato F., Carriere F., Sarda L., and Verger R. A critical re-evaluation of the phenomenon of "interfacial activation". In: Dennis E., and Rubin B. (Eds). Methods Enzymol. (1997), Academic Press, New York 327-347
    • (1997) Methods Enzymol. , pp. 327-347
    • Ferrato, F.1    Carriere, F.2    Sarda, L.3    Verger, R.4
  • 81
    • 0020713292 scopus 로고
    • Isolation and some properties of extracellular heat-stable lipases from Pseudomonas fluorescens strain AFT 36
    • Fox P.F., and Stepaniak L. Isolation and some properties of extracellular heat-stable lipases from Pseudomonas fluorescens strain AFT 36. J Dairy Res 50 (1983) 77-89
    • (1983) J Dairy Res , vol.50 , pp. 77-89
    • Fox, P.F.1    Stepaniak, L.2
  • 82
    • 0037450983 scopus 로고    scopus 로고
    • Highly sensitive active-site titration of lipase in microscale culture media using fluorescent organophosphorus ester
    • Fujii R., Utsunomiya Y., Hiratake J., Sogabe A., and Sakata K. Highly sensitive active-site titration of lipase in microscale culture media using fluorescent organophosphorus ester. Biochim Biophys Acta 1631 2 (2003) 197-205
    • (2003) Biochim Biophys Acta , vol.1631 , Issue.2 , pp. 197-205
    • Fujii, R.1    Utsunomiya, Y.2    Hiratake, J.3    Sogabe, A.4    Sakata, K.5
  • 83
    • 0022448659 scopus 로고
    • Inhibition of lipases by proteins: a binding study using dicaprin monolayers
    • Gargouri Y., Piéroni G., Rivière C., Sarda L., and Verger R. Inhibition of lipases by proteins: a binding study using dicaprin monolayers. Biochemistry 25 (1986) 1733-1738
    • (1986) Biochemistry , vol.25 , pp. 1733-1738
    • Gargouri, Y.1    Piéroni, G.2    Rivière, C.3    Sarda, L.4    Verger, R.5
  • 84
    • 0028949624 scopus 로고
    • Assay of pancreatic lipase with the surface acoustic wave sensor system
    • Ge K., Liu D.H., Chen K., Nie L.H., and Yao S.Z. Assay of pancreatic lipase with the surface acoustic wave sensor system. Anal Biochem 226 (1995) 207-211
    • (1995) Anal Biochem , vol.226 , pp. 207-211
    • Ge, K.1    Liu, D.H.2    Chen, K.3    Nie, L.H.4    Yao, S.Z.5
  • 85
    • 0025807532 scopus 로고
    • Physiological regulation and optimization of lipase activity in Pseudomonas aeruginosa EF2
    • Gilbert E.J., Drozd J.W., and Jones C.W.J. Physiological regulation and optimization of lipase activity in Pseudomonas aeruginosa EF2. J Gen Microbiol 137 (1991) 2215-2221
    • (1991) J Gen Microbiol , vol.137 , pp. 2215-2221
    • Gilbert, E.J.1    Drozd, J.W.2    Jones, C.W.J.3
  • 86
    • 0025926043 scopus 로고
    • Mechanical studies of proteases and lipases for detergent industry
    • Gormsen E., Aaslyng D., and Malmos H. Mechanical studies of proteases and lipases for detergent industry. J Chem Tech Biotechnol 50 (1991) 321-330
    • (1991) J Chem Tech Biotechnol , vol.50 , pp. 321-330
    • Gormsen, E.1    Aaslyng, D.2    Malmos, H.3
  • 87
  • 88
    • 0019128983 scopus 로고
    • Effect of taurodeoxycholate, colipase and temperature on the interfacial inactivation of porcine pancreatic lipase
    • Granon S., and Semeriva M. Effect of taurodeoxycholate, colipase and temperature on the interfacial inactivation of porcine pancreatic lipase. Eur J Biochem 111 (1980) 117-124
    • (1980) Eur J Biochem , vol.111 , pp. 117-124
    • Granon, S.1    Semeriva, M.2
  • 89
    • 0003072046 scopus 로고
    • Analyse de la forme du profil d'une goutte pendante par traitement d'images numériques. (Mesure en temps réel de la tension interfaciale)
    • Grimaldi M., Bois A., Nury S., Rivière C., Verger R., and Richou J. Analyse de la forme du profil d'une goutte pendante par traitement d'images numériques. (Mesure en temps réel de la tension interfaciale). Opto 91 (1991) 104-110
    • (1991) Opto , vol.91 , pp. 104-110
    • Grimaldi, M.1    Bois, A.2    Nury, S.3    Rivière, C.4    Verger, R.5    Richou, J.6
  • 91
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: an overview of production, purification and biochemical properties
    • Gupta R., Gupta N., and Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64 (2004) 763-781
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 92
    • 0025809090 scopus 로고
    • Production of lipase by Yarrowia lipolytica. I. Lipases from yeasts
    • Hadeball W. Production of lipase by Yarrowia lipolytica. I. Lipases from yeasts. Acta Biotechnol 11 (1991) 159-167
    • (1991) Acta Biotechnol , vol.11 , pp. 159-167
    • Hadeball, W.1
  • 93
    • 0028577588 scopus 로고
    • Production and characterization of an extracellular thermostable lipase from a thermophilic Bacillus sp
    • Handelsman T., and Shoham Y. Production and characterization of an extracellular thermostable lipase from a thermophilic Bacillus sp. J Gen Appl Microbiol 40 (1994) 435-443
    • (1994) J Gen Appl Microbiol , vol.40 , pp. 435-443
    • Handelsman, T.1    Shoham, Y.2
  • 94
    • 33750182423 scopus 로고    scopus 로고
    • Influence of culture conditions on lipase production by Bacillus sp.FH5
    • Hasan F., Shah A.A., and Abul-Hameed A. Influence of culture conditions on lipase production by Bacillus sp.FH5. Ann Microbiol 56 3 (2006) 247-252
    • (2006) Ann Microbiol , vol.56 , Issue.3 , pp. 247-252
    • Hasan, F.1    Shah, A.A.2    Abul-Hameed, A.3
  • 95
    • 0002227983 scopus 로고
    • Scamehorn J.F., and Harwell J.H. (Eds), Marcel Dekker Press, New York,U.S.A.
    • Hatton T.A. In: Scamehorn J.F., and Harwell J.H. (Eds). In Surfactant-Based Separation Processes (1989), Marcel Dekker Press, New York,U.S.A. 55-90
    • (1989) In Surfactant-Based Separation Processes , pp. 55-90
    • Hatton, T.A.1
  • 96
    • 0028229720 scopus 로고
    • Fluorescence-based assays of lipases, phospholipases, and other lipolytic enzymes
    • Hendrickson H.S. Fluorescence-based assays of lipases, phospholipases, and other lipolytic enzymes. Anal Biochem 219 (1994) 1-8
    • (1994) Anal Biochem , vol.219 , pp. 1-8
    • Hendrickson, H.S.1
  • 97
    • 0019812636 scopus 로고
    • Continuous assay of phospholipase A2 with pyrene-labeled lecithin as a substrate
    • Hendrickson H.S., and Rauk P.N. Continuous assay of phospholipase A2 with pyrene-labeled lecithin as a substrate. Anal Biochem 116 (1981) 553-558
    • (1981) Anal Biochem , vol.116 , pp. 553-558
    • Hendrickson, H.S.1    Rauk, P.N.2
  • 98
    • 53749083429 scopus 로고    scopus 로고
    • Isolation and identification of a lipase producing Bacillus sp. from soil
    • Heravi K.M., Eftekhar F., Yakhchali B., and Tabandeh F. Isolation and identification of a lipase producing Bacillus sp. from soil. Pak J Biol Sci 11 (2008) 740-745
    • (2008) Pak J Biol Sci , vol.11 , pp. 740-745
    • Heravi, K.M.1    Eftekhar, F.2    Yakhchali, B.3    Tabandeh, F.4
  • 99
    • 0034000128 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit
    • Hiol A., Jonzo M.D., Rugani N., Druet D., Sarda L., and Comeau L.C. Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit. Enzyme Microb Technol 26 (2000) 421-430
    • (2000) Enzyme Microb Technol , vol.26 , pp. 421-430
    • Hiol, A.1    Jonzo, M.D.2    Rugani, N.3    Druet, D.4    Sarda, L.5    Comeau, L.C.6
  • 100
    • 70350014438 scopus 로고    scopus 로고
    • http://www.markergene.com/kits.php. MarkerGene™ Fluorescent Lipase Assay Kit. Product ID M0612.
    • http://www.markergene.com/kits.php. MarkerGene™ Fluorescent Lipase Assay Kit. Product ID M0612).
  • 101
    • 70350014441 scopus 로고    scopus 로고
    • Http://Www.Diaglab.Vet.Cornell.Edu/Clinpath/Modules/Chem/Lipase.Htm).
  • 102
    • 70350019805 scopus 로고    scopus 로고
    • http://probes.invitrogen.com/handbook/sections/1006.html).
  • 103
    • 0024376181 scopus 로고
    • A sensitive, inexpensive method for determining minute quantities of lipase activity
    • Huang J., Roheim P.S., Sloop C.H., and Wong L. A sensitive, inexpensive method for determining minute quantities of lipase activity. Anal Biochem 179 (1989) 413-417
    • (1989) Anal Biochem , vol.179 , pp. 413-417
    • Huang, J.1    Roheim, P.S.2    Sloop, C.H.3    Wong, L.4
  • 104
    • 0031968917 scopus 로고    scopus 로고
    • Biochemical and structural characterization of triacylglycerol lipase from Penicillium cyclopium
    • Ibrik A., Chahinian H., Rugani N., Sarda L., and Comeau L.C. Biochemical and structural characterization of triacylglycerol lipase from Penicillium cyclopium. Lipids 33 (1998) 377-384
    • (1998) Lipids , vol.33 , pp. 377-384
    • Ibrik, A.1    Chahinian, H.2    Rugani, N.3    Sarda, L.4    Comeau, L.C.5
  • 105
    • 0025894836 scopus 로고
    • Purification of human pancreatic lipase and the influence of bicarbonate on lipase activity
    • Iizuka K., Higurashi H., Fujimoto J., Hayashi Y., Yamamoto K., and Hiura H. Purification of human pancreatic lipase and the influence of bicarbonate on lipase activity. Ann Clin Biochem 28 (1991) 373-378
    • (1991) Ann Clin Biochem , vol.28 , pp. 373-378
    • Iizuka, K.1    Higurashi, H.2    Fujimoto, J.3    Hayashi, Y.4    Yamamoto, K.5    Hiura, H.6
  • 106
    • 0343457387 scopus 로고
    • Purification and characterization of a thermostable lipase from newly isolated Pseudomonas sp. KWI-56
    • Iizumi T., Nakamura K., and Fukase T. Purification and characterization of a thermostable lipase from newly isolated Pseudomonas sp. KWI-56. Agric Biol Chem 54 (1990) 1253-1258
    • (1990) Agric Biol Chem , vol.54 , pp. 1253-1258
    • Iizumi, T.1    Nakamura, K.2    Fukase, T.3
  • 107
    • 0026472502 scopus 로고
    • Clinical evaluation of a pancreatic lipase mass concentration assay
    • Ingen H.E.V., and Sanders G.T.B. Clinical evaluation of a pancreatic lipase mass concentration assay. Clin Chem 38 (1992) 2310-2313
    • (1992) Clin Chem , vol.38 , pp. 2310-2313
    • Ingen, H.E.V.1    Sanders, G.T.B.2
  • 108
    • 64549144156 scopus 로고    scopus 로고
    • Deactivation and unfolding are uncoupled in a bacterial lipase exposed to heat, low pH and organic solvents
    • Invernizzi G., Casiraghi L., Grandori R., and Lotti M. Deactivation and unfolding are uncoupled in a bacterial lipase exposed to heat, low pH and organic solvents. J Biotechnol 141 (2009) 42-46
    • (2009) J Biotechnol , vol.141 , pp. 42-46
    • Invernizzi, G.1    Casiraghi, L.2    Grandori, R.3    Lotti, M.4
  • 109
    • 0029934060 scopus 로고    scopus 로고
    • Hydrolysis of monomolecular films of long chain phosphatidylcholine by phospholipase A2 in the presence of β-cyclodextrin
    • Ivanova M.G., Ivanova T., Verger R., and Panaiotov I. Hydrolysis of monomolecular films of long chain phosphatidylcholine by phospholipase A2 in the presence of β-cyclodextrin. Colloids Surfaces B: Biointerface 6 (1996) 9-17
    • (1996) Colloids Surfaces B: Biointerface , vol.6 , pp. 9-17
    • Ivanova, M.G.1    Ivanova, T.2    Verger, R.3    Panaiotov, I.4
  • 112
    • 0029092045 scopus 로고
    • Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: bacterial lipases hydrolyze poly (omega-hydroxyalkanoates)
    • Jaeger K.E., Steinbuchel A., and Jendrossek D. Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: bacterial lipases hydrolyze poly (omega-hydroxyalkanoates). Appl Environ Microbiol 61 (1995) 3113-3118
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3113-3118
    • Jaeger, K.E.1    Steinbuchel, A.2    Jendrossek, D.3
  • 113
    • 0028241550 scopus 로고
    • Determination of lipase activity by a rhodamine-triglyceride-agarose assay
    • Jette J.F., and Ziomek E. Determination of lipase activity by a rhodamine-triglyceride-agarose assay. Anal Biochem 219 (1994) 256-260
    • (1994) Anal Biochem , vol.219 , pp. 256-260
    • Jette, J.F.1    Ziomek, E.2
  • 114
    • 0019310867 scopus 로고
    • On the mechanism of the lipoprotein lipase-induced fluorescence changes in dansyl phosphatidylethanolamine-labeled very low density lipoproteins
    • Johnson J.D., Taskinen M.R., Matsuoka N., and Jackson R.L. On the mechanism of the lipoprotein lipase-induced fluorescence changes in dansyl phosphatidylethanolamine-labeled very low density lipoproteins. J Biol Chem 255 (1980) 3466-3471
    • (1980) J Biol Chem , vol.255 , pp. 3466-3471
    • Johnson, J.D.1    Taskinen, M.R.2    Matsuoka, N.3    Jackson, R.L.4
  • 115
    • 46849092215 scopus 로고    scopus 로고
    • Cold active microbial lipases: some hot issues and recent developments
    • Joseph B., Ramteke P.W., and Thomas G. Cold active microbial lipases: some hot issues and recent developments. Biotechnol Adv 26 (2008) 457-470
    • (2008) Biotechnol Adv , vol.26 , pp. 457-470
    • Joseph, B.1    Ramteke, P.W.2    Thomas, G.3
  • 117
    • 0000112343 scopus 로고
    • Production and properties of alkaline lipase from Alcaligenes sp. strain No. 679
    • Kakusho Y., Machida H., and Iwasaki S. Production and properties of alkaline lipase from Alcaligenes sp. strain No. 679. Agric Biol Chem 46 (1982) 1743-1750
    • (1982) Agric Biol Chem , vol.46 , pp. 1743-1750
    • Kakusho, Y.1    Machida, H.2    Iwasaki, S.3
  • 118
    • 0038371433 scopus 로고    scopus 로고
    • Influence of culture conditions on thermostable lipase production by a thermophilic alkalitolerant strain of Bacillus sp
    • Kambourova M., Emanuilova E., and Dimitrov P. Influence of culture conditions on thermostable lipase production by a thermophilic alkalitolerant strain of Bacillus sp. Folia Microbiol 41 (1996) 146-148
    • (1996) Folia Microbiol , vol.41 , pp. 146-148
    • Kambourova, M.1    Emanuilova, E.2    Dimitrov, P.3
  • 119
    • 0033752932 scopus 로고    scopus 로고
    • Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2
    • Kamini N.R., Fujii T., Kurosu T., and Iefuji H. Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2. Process Biochem 36 (2000) 317-324
    • (2000) Process Biochem , vol.36 , pp. 317-324
    • Kamini, N.R.1    Fujii, T.2    Kurosu, T.3    Iefuji, H.4
  • 120
    • 0030162373 scopus 로고    scopus 로고
    • Isolation and identification of alkaline thermostable lipase producing microorganism and some properties of crude enzyme
    • Kar M.K., Ray L., and Chattopadhyay P. Isolation and identification of alkaline thermostable lipase producing microorganism and some properties of crude enzyme. Indian J Exp Biol 34 (1996) 535-538
    • (1996) Indian J Exp Biol , vol.34 , pp. 535-538
    • Kar, M.K.1    Ray, L.2    Chattopadhyay, P.3
  • 121
    • 47649097612 scopus 로고    scopus 로고
    • Isolation and identification of a psychrotrophic Acinetobacter sp. CR9 and characterization of its alkaline lipase
    • Kasana R.C., Kaur B., and Yadav S.K. Isolation and identification of a psychrotrophic Acinetobacter sp. CR9 and characterization of its alkaline lipase. J Basic Microbiol 48 3 (2008) 207-212
    • (2008) J Basic Microbiol , vol.48 , Issue.3 , pp. 207-212
    • Kasana, R.C.1    Kaur, B.2    Yadav, S.K.3
  • 122
    • 33646941674 scopus 로고    scopus 로고
    • Production, purification and partial characterization of lipase from Trichoderma viride
    • Kashmiri M.A., Ahmad A., and Butt B.W. Production, purification and partial characterization of lipase from Trichoderma viride. Afr J Biotechnol 5 10 (2006) 878-882
    • (2006) Afr J Biotechnol , vol.5 , Issue.10 , pp. 878-882
    • Kashmiri, M.A.1    Ahmad, A.2    Butt, B.W.3
  • 123
    • 0035663814 scopus 로고    scopus 로고
    • Conversion of Bacillus thermocatenulatus lipase into an efficient phospholipase with increased activity towards long-chain fatty acyl substrates by directed evolution and rational design
    • Kauffmann I., and Schmidt-Dannert C. Conversion of Bacillus thermocatenulatus lipase into an efficient phospholipase with increased activity towards long-chain fatty acyl substrates by directed evolution and rational design. Protein Eng 14 11 (2001) 919-928
    • (2001) Protein Eng , vol.14 , Issue.11 , pp. 919-928
    • Kauffmann, I.1    Schmidt-Dannert, C.2
  • 124
    • 0027953729 scopus 로고
    • Establishment of enzyme-linked immunosorbent assays for lipoprotein lipase with newly developed antibodies
    • Kawamura M., Gotoda T., Mori N., Shimano H., Kozaki K., Harada K., et al. Establishment of enzyme-linked immunosorbent assays for lipoprotein lipase with newly developed antibodies. J Lipid Res 35 (1994) 1688-1697
    • (1994) J Lipid Res , vol.35 , pp. 1688-1697
    • Kawamura, M.1    Gotoda, T.2    Mori, N.3    Shimano, H.4    Kozaki, K.5    Harada, K.6
  • 125
    • 0031613603 scopus 로고    scopus 로고
    • Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1
    • Kim H.K., Park S.Y., Lee J.K., and Oh T.K. Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Biosci Biotechnol Biochem 62 (1998) 66-71
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 66-71
    • Kim, H.K.1    Park, S.Y.2    Lee, J.K.3    Oh, T.K.4
  • 126
    • 0034134257 scopus 로고    scopus 로고
    • Thermostable lipase of Bacillus stearothermophilus: high-level production, purification and calcium dependent thermostability
    • Kim M.H., Kim H.K., Lee J.K., Park S.Y., and Oh T.K. Thermostable lipase of Bacillus stearothermophilus: high-level production, purification and calcium dependent thermostability. Biosci Biotechnol Biochem 64 (2000) 280-286
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 280-286
    • Kim, M.H.1    Kim, H.K.2    Lee, J.K.3    Park, S.Y.4    Oh, T.K.5
  • 127
    • 0034811043 scopus 로고    scopus 로고
    • Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator
    • Kim E.K., Jang W.H., Ko J.H., Kang J.S., Noh M.J., and Yoo O.J. Lipase and its modulator from Pseudomonas sp. strain KFCC 10818: proline-to-glutamine substitution at position 112 induces formation of enzymatically active lipase in the absence of the modulator. J Bacteriol 183 20 (2001) 5937-5941
    • (2001) J Bacteriol , vol.183 , Issue.20 , pp. 5937-5941
    • Kim, E.K.1    Jang, W.H.2    Ko, J.H.3    Kang, J.S.4    Noh, M.J.5    Yoo, O.J.6
  • 128
    • 0032972915 scopus 로고    scopus 로고
    • Development and evaluation of a direct sandwich enzyme-linked immunosorbent assay for the quantification of lipoprotein lipase mass in human plasma
    • Kimura H., Ohkaru Y., Katoh K., Ishii H., Sunahara N., Takagi A., et al. Development and evaluation of a direct sandwich enzyme-linked immunosorbent assay for the quantification of lipoprotein lipase mass in human plasma. Clin Biochem 32 (1999) 15-23
    • (1999) Clin Biochem , vol.32 , pp. 15-23
    • Kimura, H.1    Ohkaru, Y.2    Katoh, K.3    Ishii, H.4    Sunahara, N.5    Takagi, A.6
  • 129
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker G., and Jaeger K.E. Specific and sensitive plate assay for bacterial lipases. Appl Environ Microbiol 53 (1987) 211-213
    • (1987) Appl Environ Microbiol , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.E.2
  • 130
    • 0027413273 scopus 로고
    • Detection of hormone-sensitive lipase in various tissues. I. Expression of an HSL/bacterial fusion protein and generation of anti-HSL antibodies
    • Kraemer F.B., Patel S., Saedi M.S., and Sztalryd C. Detection of hormone-sensitive lipase in various tissues. I. Expression of an HSL/bacterial fusion protein and generation of anti-HSL antibodies. J Lipid Res 34 (1993) 663-671
    • (1993) J Lipid Res , vol.34 , pp. 663-671
    • Kraemer, F.B.1    Patel, S.2    Saedi, M.S.3    Sztalryd, C.4
  • 131
    • 15744397346 scopus 로고    scopus 로고
    • Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3
    • Kumar S., Kikon K., Upadhyay A., Kanwar S.S., and Gupta R. Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3. Protein Expr Purif 41 1 (2005) 38-44
    • (2005) Protein Expr Purif , vol.41 , Issue.1 , pp. 38-44
    • Kumar, S.1    Kikon, K.2    Upadhyay, A.3    Kanwar, S.S.4    Gupta, R.5
  • 132
    • 21144480197 scopus 로고
    • Purification and characterization of lipase from Pseudomonas fluorescens No 33
    • Kumura H., Mikawa K., and Saito Z. Purification and characterization of lipase from Pseudomonas fluorescens No 33. Milchwissenschaft-Milk Sci Int 48 (1993) 431-434
    • (1993) Milchwissenschaft-Milk Sci Int , vol.48 , pp. 431-434
    • Kumura, H.1    Mikawa, K.2    Saito, Z.3
  • 133
    • 0017336351 scopus 로고
    • A novel and simple colorimetric assay for human serum lipase
    • Kurooka S., and Okamoto S Hashimoto M. A novel and simple colorimetric assay for human serum lipase. J Biochem 81 (1977) 361-369
    • (1977) J Biochem , vol.81 , pp. 361-369
    • Kurooka, S.1    Okamoto S Hashimoto, M.2
  • 135
    • 0033514417 scopus 로고    scopus 로고
    • The effects of environmental conditions on the lipolytic activity of strains of Penicillium roqueforti
    • Larsen M.D., and Jensen K. The effects of environmental conditions on the lipolytic activity of strains of Penicillium roqueforti. Int J Food Microbiol 46 (1999) 159-166
    • (1999) Int J Food Microbiol , vol.46 , pp. 159-166
    • Larsen, M.D.1    Jensen, K.2
  • 136
    • 67651021326 scopus 로고    scopus 로고
    • An alkaliphilic bacterium isolation and physiological characterization of Bacillus clausii SKAL-16 isolated from wastewater
    • Lee S.H., and Park D.H. An alkaliphilic bacterium isolation and physiological characterization of Bacillus clausii SKAL-16 isolated from wastewater. J Microbiol Biotechnol 18 (2008) 1908-1914
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1908-1914
    • Lee, S.H.1    Park, D.H.2
  • 137
    • 0027627474 scopus 로고
    • Production and partial purification of a lipase from Pseudomonas-putida 3SK
    • Lee S.Y., and Rhee J.S. Production and partial purification of a lipase from Pseudomonas-putida 3SK. Enz Microbial Technol 15 (1993) 617-623
    • (1993) Enz Microbial Technol , vol.15 , pp. 617-623
    • Lee, S.Y.1    Rhee, J.S.2
  • 138
    • 0032872147 scopus 로고    scopus 로고
    • Isolation and characterization of a thermophilic lipase from Bacillus thermoleovorans ID-1
    • Lee D.W., Koh Y.S., Kim K.J., Kim B.C., Choi H.J., Kim D.S., et al. Isolation and characterization of a thermophilic lipase from Bacillus thermoleovorans ID-1. FEMS Microbiol Lett 179 (1999) 393-400
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 393-400
    • Lee, D.W.1    Koh, Y.S.2    Kim, K.J.3    Kim, B.C.4    Choi, H.J.5    Kim, D.S.6
  • 139
    • 4644247440 scopus 로고    scopus 로고
    • Display of bacterial lipase on the Escherichia coli cell surface by using fadl as an anchoring motif and use of the enzyme in enantioselective biocatalysis
    • Lee S.H., Choi J.I., Park S.J., Lee S.Y., and Park B.C. Display of bacterial lipase on the Escherichia coli cell surface by using fadl as an anchoring motif and use of the enzyme in enantioselective biocatalysis. Appl Environ Microbiol 70 (2004) 5074-5080
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5074-5080
    • Lee, S.H.1    Choi, J.I.2    Park, S.J.3    Lee, S.Y.4    Park, B.C.5
  • 140
    • 0033559817 scopus 로고    scopus 로고
    • Subcellular localization, developmental expression and characterization of a liver triacylglycerol hydrolase
    • Lehner R., Cui Z., and Vance D. Subcellular localization, developmental expression and characterization of a liver triacylglycerol hydrolase. Biochem J 338 (1999) 761-768
    • (1999) Biochem J , vol.338 , pp. 761-768
    • Lehner, R.1    Cui, Z.2    Vance, D.3
  • 141
    • 0027279621 scopus 로고
    • Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme
    • Lesuisse E., Schanck K., and Colson C. Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur J Biochem 216 (1993) 155-160
    • (1993) Eur J Biochem , vol.216 , pp. 155-160
    • Lesuisse, E.1    Schanck, K.2    Colson, C.3
  • 142
    • 0035150139 scopus 로고    scopus 로고
    • Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase
    • Liebeton K., Zacharias A., and Jaeger K.E. Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase. J Bacteriol 183 2 (2001) 597-603
    • (2001) J Bacteriol , vol.183 , Issue.2 , pp. 597-603
    • Liebeton, K.1    Zacharias, A.2    Jaeger, K.E.3
  • 143
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J Am Chem Soc 56 (1934) 658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 144
    • 0018307995 scopus 로고
    • Effect of emulsifiers on the hydrolysis of solid fats by microorganism lipases
    • Lobyreva L.B., and Marchenkova A.I. Effect of emulsifiers on the hydrolysis of solid fats by microorganism lipases. Mikrobiologiia 48 (1979) 53-56
    • (1979) Mikrobiologiia , vol.48 , pp. 53-56
    • Lobyreva, L.B.1    Marchenkova, A.I.2
  • 145
    • 0019159032 scopus 로고
    • Isolation and characteristics of Penicillium roqueforti lipases
    • Lobyreva L.B., and Marchenkova A.I. Isolation and characteristics of Penicillium roqueforti lipases. Mikrobiologiia 49 (1980) 924-930
    • (1980) Mikrobiologiia , vol.49 , pp. 924-930
    • Lobyreva, L.B.1    Marchenkova, A.I.2
  • 147
    • 0030911253 scopus 로고    scopus 로고
    • Purification and characterization of lipase from Aeromonas sobria LP004
    • Lotrakul P., and Dharmsthiti S. Purification and characterization of lipase from Aeromonas sobria LP004. J Biotechnol 54 (1997) 113-120
    • (1997) J Biotechnol , vol.54 , pp. 113-120
    • Lotrakul, P.1    Dharmsthiti, S.2
  • 148
    • 0030570083 scopus 로고    scopus 로고
    • On the issue of interfacial activation of lipase in nonaqueous media
    • Louwrier A., Drtin G.J., and Klibanov A.M. On the issue of interfacial activation of lipase in nonaqueous media. Biotechnol Bioeng 50 (1996) 1-5
    • (1996) Biotechnol Bioeng , vol.50 , pp. 1-5
    • Louwrier, A.1    Drtin, G.J.2    Klibanov, A.M.3
  • 149
    • 0016979036 scopus 로고
    • Rapid colorimetric determination of free fatty acids
    • Lowry R.L., and Tinsley I.J. Rapid colorimetric determination of free fatty acids. J Am Oil Chem Soc 53 (1976) 470-472
    • (1976) J Am Oil Chem Soc , vol.53 , pp. 470-472
    • Lowry, R.L.1    Tinsley, I.J.2
  • 150
    • 0002650750 scopus 로고    scopus 로고
    • Partial purification and characterization of an extracellular lipase from a newly isolated strain of Geotrichum sp
    • Macedo G.A., Park Y.K., and Pastore G.M. Partial purification and characterization of an extracellular lipase from a newly isolated strain of Geotrichum sp. Rev Microbiol 28 2 (1997) 90-95
    • (1997) Rev Microbiol , vol.28 , Issue.2 , pp. 90-95
    • Macedo, G.A.1    Park, Y.K.2    Pastore, G.M.3
  • 152
    • 0034566882 scopus 로고    scopus 로고
    • Isolation and characterization of lipid degrading Bacillus thermoleovorans IHI-91 from an Icelandic hot spring
    • Markossian S., Becker P., Markl H., and Antranikian G. Isolation and characterization of lipid degrading Bacillus thermoleovorans IHI-91 from an Icelandic hot spring. Extremophiles 4 (2000) 365-371
    • (2000) Extremophiles , vol.4 , pp. 365-371
    • Markossian, S.1    Becker, P.2    Markl, H.3    Antranikian, G.4
  • 153
    • 0025765937 scopus 로고
    • p-nitrophenyllaurate: a substrate for the high-performance liquid chromatographic determination of lipase activity
    • Maurich V., Zacchigna M., and Pitotti A. p-nitrophenyllaurate: a substrate for the high-performance liquid chromatographic determination of lipase activity. J Chromatogr 566 2 (1991) 453-459
    • (1991) J Chromatogr , vol.566 , Issue.2 , pp. 453-459
    • Maurich, V.1    Zacchigna, M.2    Pitotti, A.3
  • 154
    • 84907422227 scopus 로고
    • The egg yolk plate reaction for the presumptive diagnosis of Clostridium sporogenes and certain species of the gangrene and Botulinum Groups
    • McClung L.S., and Toabe R. The egg yolk plate reaction for the presumptive diagnosis of Clostridium sporogenes and certain species of the gangrene and Botulinum Groups. J Bacteriol 53 2 (1947) 139-147
    • (1947) J Bacteriol , vol.53 , Issue.2 , pp. 139-147
    • McClung, L.S.1    Toabe, R.2
  • 155
    • 0026524412 scopus 로고
    • Lamellar bodies as delivery systems of hydrolytic enzymes: implications for normal and abnormal desquamation
    • Menon G., Ghadially R., Williams M., and Elias P. Lamellar bodies as delivery systems of hydrolytic enzymes: implications for normal and abnormal desquamation. Br J Dermatol 126 (1992) 337-345
    • (1992) Br J Dermatol , vol.126 , pp. 337-345
    • Menon, G.1    Ghadially, R.2    Williams, M.3    Elias, P.4
  • 157
    • 0033217160 scopus 로고    scopus 로고
    • Purification and characterization of a novel extracellular lipase catalyzing hydrolysis of oleyl benzoate from Acinetobacter nov. sp. strain KM109
    • Mitsuhashi K., Yamashita M., Hwan Y.S., Ihara F., Nihira T., and Yamada Y. Purification and characterization of a novel extracellular lipase catalyzing hydrolysis of oleyl benzoate from Acinetobacter nov. sp. strain KM109. Biosci Biotechnol Biochem 63 (1999) 1959-1964
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1959-1964
    • Mitsuhashi, K.1    Yamashita, M.2    Hwan, Y.S.3    Ihara, F.4    Nihira, T.5    Yamada, Y.6
  • 158
    • 0030627885 scopus 로고    scopus 로고
    • Recovery of monomolecular films in studies of lipolysis
    • Momsen W.E., and Brockman H.L. Recovery of monomolecular films in studies of lipolysis. Methods Enzymol 286 (1997) 292-305
    • (1997) Methods Enzymol , vol.286 , pp. 292-305
    • Momsen, W.E.1    Brockman, H.L.2
  • 159
    • 65549136697 scopus 로고    scopus 로고
    • Oleate lipase activity in Gardnerella vaginalis and reconsideration of existing biotype schemes
    • Moncla B.J., and Pryke K.M. Oleate lipase activity in Gardnerella vaginalis and reconsideration of existing biotype schemes. BMC Microbiol 9 (2009) 78
    • (2009) BMC Microbiol , vol.9 , pp. 78
    • Moncla, B.J.1    Pryke, K.M.2
  • 160
    • 0025164808 scopus 로고
    • Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria
    • Moncla B.J., Braham P., and Hillier S.L. Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria. J Clin Microbiol 28 3 (1990) 422-425
    • (1990) J Clin Microbiol , vol.28 , Issue.3 , pp. 422-425
    • Moncla, B.J.1    Braham, P.2    Hillier, S.L.3
  • 162
    • 84889853728 scopus 로고
    • A new spectrophotometric method for the detection of lipase activity using 2,4-dinitrophenyl butyrate as a substrate
    • Mosmuller E.W.J., Van Heemst J.D.H., Van Delden C.J., Franssen M.C.R., and Engbersen J.F.J. A new spectrophotometric method for the detection of lipase activity using 2,4-dinitrophenyl butyrate as a substrate. Biocatalysis 5 (1992) 279-287
    • (1992) Biocatalysis , vol.5 , pp. 279-287
    • Mosmuller, E.W.J.1    Van Heemst, J.D.H.2    Van Delden, C.J.3    Franssen, M.C.R.4    Engbersen, J.F.J.5
  • 163
    • 0018586593 scopus 로고
    • Identity and lipase productivity of a mesophilic actinomycete isolated from Egyptian soil
    • Mostafa S.A., and Ali O.A. Identity and lipase productivity of a mesophilic actinomycete isolated from Egyptian soil. Zentralbl Bakteriol [Naturwiss] 134 (1979) 316-324
    • (1979) Zentralbl Bakteriol [Naturwiss] , vol.134 , pp. 316-324
    • Mostafa, S.A.1    Ali, O.A.2
  • 164
    • 0027221594 scopus 로고
    • Purification and properties of an extracellular lipase from Pythium ultimum
    • Mozaffar Z., and Weete J. Purification and properties of an extracellular lipase from Pythium ultimum. Lipids 28 (1993) 377-382
    • (1993) Lipids , vol.28 , pp. 377-382
    • Mozaffar, Z.1    Weete, J.2
  • 165
    • 0020436764 scopus 로고
    • Purification and properties of a novel lipase from Staphylococcus aureus 226
    • Muraoka T., Ando T., and Okuda H.J. Purification and properties of a novel lipase from Staphylococcus aureus 226. Biochem (Tokyo) 92 (1982) 1933-1939
    • (1982) Biochem (Tokyo) , vol.92 , pp. 1933-1939
    • Muraoka, T.1    Ando, T.2    Okuda, H.J.3
  • 166
    • 0027058143 scopus 로고
    • Hyperproduction of thermostable lipase by genetically engineered Pseudomonas species
    • of the Annals of the New York Academy of Sciences
    • Nakamura K., Iizumi T., and Fukase T. Hyperproduction of thermostable lipase by genetically engineered Pseudomonas species. of the Annals of the New York Academy of Sciences. Enzyme Eng. XI. vol. 672 (1992) 100-102
    • (1992) Enzyme Eng. XI. , vol.672 , pp. 100-102
    • Nakamura, K.1    Iizumi, T.2    Fukase, T.3
  • 167
    • 0021813223 scopus 로고
    • New fluorometric assay of lysosomal acid lipase and its application to the diagnosis of Wolman and chleseryl ester storage disease
    • Negre A.E., Salvayre R.S., Dagan A., and Gatt S. New fluorometric assay of lysosomal acid lipase and its application to the diagnosis of Wolman and chleseryl ester storage disease. Clin Chim Acta 149 (1985) 81-88
    • (1985) Clin Chim Acta , vol.149 , pp. 81-88
    • Negre, A.E.1    Salvayre, R.S.2    Dagan, A.3    Gatt, S.4
  • 168
    • 0024412982 scopus 로고
    • Pyrenemethyl laurate, a new fluorescent substrate for continuous kinetic determination of lipase activity
    • Nègre A., Salvayre R., Dagna A., and Gatt S. Pyrenemethyl laurate, a new fluorescent substrate for continuous kinetic determination of lipase activity. Biochim Biophys Acta 1006 (1989) 84-88
    • (1989) Biochim Biophys Acta , vol.1006 , pp. 84-88
    • Nègre, A.1    Salvayre, R.2    Dagna, A.3    Gatt, S.4
  • 169
    • 0032794188 scopus 로고    scopus 로고
    • Lag-burst kinetics in phospholipase A2 hydrolysis of DPPC bilayers visualized by atomic force microscopy
    • Nielsen L., Risbo C.T., and Bjornholm T. Lag-burst kinetics in phospholipase A2 hydrolysis of DPPC bilayers visualized by atomic force microscopy. Biochim Biophys Acta 1420 (1999) 266-271
    • (1999) Biochim Biophys Acta , vol.1420 , pp. 266-271
    • Nielsen, L.1    Risbo, C.T.2    Bjornholm, T.3
  • 170
    • 84954905402 scopus 로고
    • Purification and some properties of lipase produced by Pseudomonas fragi 22. 39 B
    • Nishio T., Chikano T., and Kamimura M. Purification and some properties of lipase produced by Pseudomonas fragi 22. 39 B. Agric Biol Chem 51 (1987) 181-187
    • (1987) Agric Biol Chem , vol.51 , pp. 181-187
    • Nishio, T.1    Chikano, T.2    Kamimura, M.3
  • 171
    • 0023427532 scopus 로고
    • Lipase kinetics at the triacylglycerol-water interface using surface tension measurements
    • Nury S., Pieroni G., Riviere C., Gargouri Y., Bois A., and Verger R. Lipase kinetics at the triacylglycerol-water interface using surface tension measurements. Chem Phys Lipids 45 (1987) 27-37
    • (1987) Chem Phys Lipids , vol.45 , pp. 27-37
    • Nury, S.1    Pieroni, G.2    Riviere, C.3    Gargouri, Y.4    Bois, A.5    Verger, R.6
  • 173
    • 70350016423 scopus 로고
    • Environmental Monitoring Systems Laboratory Office of Research and Development U.S. Environmental Protection Agency Cincinnati, Ohio 45268
    • O'Dell JW. Determination of turbidity by Nephelometry, http://www.epa.gov/safewater/mdbp/pdf/turbidity/appb.pdf. Environmental Monitoring Systems Laboratory Office of Research and Development U.S. Environmental Protection Agency Cincinnati, Ohio 45268,1993.
    • (1993) Determination of turbidity by Nephelometry
    • O'Dell, J.W.1
  • 174
    • 0032844672 scopus 로고    scopus 로고
    • Staphylococcus haemolyticus lipase: biochemical properties, substrate specificity and gene cloning
    • Oh B., Kim H., Lee J., Kang S., and Oh T. Staphylococcus haemolyticus lipase: biochemical properties, substrate specificity and gene cloning. FEMS Microbiol Lett 179 (1999) 385-392
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 385-392
    • Oh, B.1    Kim, H.2    Lee, J.3    Kang, S.4    Oh, T.5
  • 175
    • 70350013347 scopus 로고
    • Influence of NaCl on colonies and lipase of Natto bacilli
    • Ohkuro I., Komatsuzaki T., Kawashima M., and Kuriyama S. Influence of NaCl on colonies and lipase of Natto bacilli. Med Biol 97 (1978) 171-174
    • (1978) Med Biol , vol.97 , pp. 171-174
    • Ohkuro, I.1    Komatsuzaki, T.2    Kawashima, M.3    Kuriyama, S.4
  • 176
    • 0002536480 scopus 로고    scopus 로고
    • Enzymatic reactions at interfaces: interfacial and temporal organization of enzymatic lipolysis
    • Baszkin A., and Norde W. (Eds), Marcel Dekker, Inc, New York, Basel (Switzerland)
    • Panaitov I., and Verger R. Enzymatic reactions at interfaces: interfacial and temporal organization of enzymatic lipolysis. In: Baszkin A., and Norde W. (Eds). Physical Chemistry of Biological Interfaces (2000), Marcel Dekker, Inc, New York, Basel (Switzerland) 359-400
    • (2000) Physical Chemistry of Biological Interfaces , pp. 359-400
    • Panaitov, I.1    Verger, R.2
  • 177
    • 0034941347 scopus 로고    scopus 로고
    • Measurement of pancreatic lipase activity in serum by a kinetic colorimetric assay using a new chromogenic substrate
    • Panteghini M., Bonora R., and Pagani F. Measurement of pancreatic lipase activity in serum by a kinetic colorimetric assay using a new chromogenic substrate. Ann Clin Biochem 38 (2001) 365-370
    • (2001) Ann Clin Biochem , vol.38 , pp. 365-370
    • Panteghini, M.1    Bonora, R.2    Pagani, F.3
  • 178
    • 0023957639 scopus 로고
    • Factors affecting growth and lipase production by meat lactobacilli strains and Brochothrix thermosphaota
    • Papon M., and Talon R. Factors affecting growth and lipase production by meat lactobacilli strains and Brochothrix thermosphaota. J Appl Bacteriol 64 (1988) 107-115
    • (1988) J Appl Bacteriol , vol.64 , pp. 107-115
    • Papon, M.1    Talon, R.2
  • 179
    • 64549111395 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5
    • Park I.H., Kim S.H., Lee Y.S., Lee S.C., Zhou Y., Kim C.M., et al. Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5. J Microbiol Biotechnol 19 2 (2009) 128-135
    • (2009) J Microbiol Biotechnol , vol.19 , Issue.2 , pp. 128-135
    • Park, I.H.1    Kim, S.H.2    Lee, Y.S.3    Lee, S.C.4    Zhou, Y.5    Kim, C.M.6
  • 181
    • 26844479299 scopus 로고    scopus 로고
    • A stable lipase from Candida lipolytica: cultivation conditions and crude enzyme characteristics
    • Pereira-Meirelles F.V., Rocha-Leão M.H., and Sant Anna Jr. G.L. A stable lipase from Candida lipolytica: cultivation conditions and crude enzyme characteristics. Appl Biochem Biotechnol 65 (1997) 73-85
    • (1997) Appl Biochem Biotechnol , vol.65 , pp. 73-85
    • Pereira-Meirelles, F.V.1    Rocha-Leão, M.H.2    Sant Anna Jr., G.L.3
  • 183
    • 0025195435 scopus 로고
    • Lipases catalyze hydrolysis of fatty acid anhydrides
    • Pieroni G., and Fourneron J.D. Lipases catalyze hydrolysis of fatty acid anhydrides. Eur J Biochem 193 (1990) 249-253
    • (1990) Eur J Biochem , vol.193 , pp. 249-253
    • Pieroni, G.1    Fourneron, J.D.2
  • 184
    • 0342803577 scopus 로고    scopus 로고
    • Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica
    • Pignède G., Wang H., Fudalej F., Gaillardin C., Seman M., and Nicaud J.M. Characterization of an extracellular lipase encoded by LIP2 in Yarrowia lipolytica. J Bacteriol 182 (2000) 2802-2810
    • (2000) J Bacteriol , vol.182 , pp. 2802-2810
    • Pignède, G.1    Wang, H.2    Fudalej, F.3    Gaillardin, C.4    Seman, M.5    Nicaud, J.M.6
  • 187
    • 0033907241 scopus 로고    scopus 로고
    • Purification and characterization of lipase from psychrophilic Acinetobacter calcoaceticus LP009
    • Pratuangdejkul J., and Dharmsthiti S. Purification and characterization of lipase from psychrophilic Acinetobacter calcoaceticus LP009. Microbiol Res 155 (2000) 95-100
    • (2000) Microbiol Res , vol.155 , pp. 95-100
    • Pratuangdejkul, J.1    Dharmsthiti, S.2
  • 188
    • 34948830172 scopus 로고    scopus 로고
    • Geobacillus zalihae sp. nov., a thermophilic lipolytic bacterium isolated from palm oil mill effluent in Malaysia
    • Rahman R.N.Z.R.A., Leow T.C., Salleh A.B., and Basri M. Geobacillus zalihae sp. nov., a thermophilic lipolytic bacterium isolated from palm oil mill effluent in Malaysia. Microbiology 7 (2007) 77
    • (2007) Microbiology , vol.7 , pp. 77
    • Rahman, R.N.Z.R.A.1    Leow, T.C.2    Salleh, A.B.3    Basri, M.4
  • 189
    • 0024399931 scopus 로고
    • Multi-competitive enzymic reactions in organic media: a simple test for the determination of lipase fatty acid specificity
    • Rangheard M.S., Langrand G., Triantaphylides C., and Baratti J. Multi-competitive enzymic reactions in organic media: a simple test for the determination of lipase fatty acid specificity. Biochim Biophys Acta 1004 (1989) 20-28
    • (1989) Biochim Biophys Acta , vol.1004 , pp. 20-28
    • Rangheard, M.S.1    Langrand, G.2    Triantaphylides, C.3    Baratti, J.4
  • 190
    • 0032614764 scopus 로고    scopus 로고
    • Monolayer techniques for studying lipase kinetics
    • Doolittle M., and Reue K. (Eds), Humana Press, Totowa, New Jersey
    • Ransac S., Ivanova M., Panaiotov I., and Verger R. Monolayer techniques for studying lipase kinetics. In: Doolittle M., and Reue K. (Eds). Methods Mol. Biol. (1999), Humana Press, Totowa, New Jersey 279-302
    • (1999) Methods Mol. Biol. , pp. 279-302
    • Ransac, S.1    Ivanova, M.2    Panaiotov, I.3    Verger, R.4
  • 191
    • 0001175580 scopus 로고
    • Production of lipase by Candida rugosa in solid state fermentation. 2. Medium optimization and effect of aeration
    • Rao P.V., Jayaraman K., and Lakshmanan C.M. Production of lipase by Candida rugosa in solid state fermentation. 2. Medium optimization and effect of aeration. Proc Biochem 28 (1993) 391-395
    • (1993) Proc Biochem , vol.28 , pp. 391-395
    • Rao, P.V.1    Jayaraman, K.2    Lakshmanan, C.M.3
  • 192
    • 0035461361 scopus 로고    scopus 로고
    • Low-temperature lipase from psychrotrophic Pseudomonas sp. strain KB700A
    • Rashid N., Shimada Y., Ezaki S., Atomi H., and Imanaka T. Low-temperature lipase from psychrotrophic Pseudomonas sp. strain KB700A. Appl Environ Microbiol 67 9 (2001) 4064-4069
    • (2001) Appl Environ Microbiol , vol.67 , Issue.9 , pp. 4064-4069
    • Rashid, N.1    Shimada, Y.2    Ezaki, S.3    Atomi, H.4    Imanaka, T.5
  • 193
    • 0024452172 scopus 로고
    • A single and continuous spectrophotometric assay for various lipolytic enzymes, using natural, non-labeled lipid substrates
    • Rawyler A., and Siegenthaler P.A. A single and continuous spectrophotometric assay for various lipolytic enzymes, using natural, non-labeled lipid substrates. Biochim Biophys Acta 1004 (1989) 337-344
    • (1989) Biochim Biophys Acta , vol.1004 , pp. 337-344
    • Rawyler, A.1    Siegenthaler, P.A.2
  • 194
    • 0035074323 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular lipase from Penicillium candidum
    • Ruiz B., Farres A., Langley E., Masso F., and Sanchez S. Purification and characterization of an extracellular lipase from Penicillium candidum. Lipids 36 (2001) 283-289
    • (2001) Lipids , vol.36 , pp. 283-289
    • Ruiz, B.1    Farres, A.2    Langley, E.3    Masso, F.4    Sanchez, S.5
  • 195
    • 0037056938 scopus 로고    scopus 로고
    • Optical resolution of racemic 2-hydroxy octanoic acid using biphasic enzyme membrane reactor
    • Sakaki K., Hara S., and Itoh N. Optical resolution of racemic 2-hydroxy octanoic acid using biphasic enzyme membrane reactor. Desalination 149 (2002) 247-252
    • (2002) Desalination , vol.149 , pp. 247-252
    • Sakaki, K.1    Hara, S.2    Itoh, N.3
  • 196
    • 38449094836 scopus 로고    scopus 로고
    • Purification and characterization of two highly thermophilic alkaline lipases from Thermosyntropha lipolytica
    • Dec
    • Salameh M.A., and Wiegel J. Purification and characterization of two highly thermophilic alkaline lipases from Thermosyntropha lipolytica. Appl Environ Microbiol 73 23 (2007) 7725-7731 Dec
    • (2007) Appl Environ Microbiol , vol.73 , Issue.23 , pp. 7725-7731
    • Salameh, M.A.1    Wiegel, J.2
  • 197
    • 0027135561 scopus 로고
    • Extra-cellular and intra-cellular lipases from a thermophilic Rhizopus oryzae and factors affecting their production
    • Salleh A.B., Musani R., Basri M., Ampon K., Yunus W.M.Z., and Razak C.N.A. Extra-cellular and intra-cellular lipases from a thermophilic Rhizopus oryzae and factors affecting their production. Can J Microbiol 39 (1993) 978-981
    • (1993) Can J Microbiol , vol.39 , pp. 978-981
    • Salleh, A.B.1    Musani, R.2    Basri, M.3    Ampon, K.4    Yunus, W.M.Z.5    Razak, C.N.A.6
  • 199
    • 79957635953 scopus 로고    scopus 로고
    • Optimization of protease and lipase production by Bacillus pumilus SG 2 isolated from an industrial effluent
    • ISSN 1937-8289, Chennai, India
    • Sangeetha R., Geetha A., and Arulpandi I. Optimization of protease and lipase production by Bacillus pumilus SG 2 isolated from an industrial effluent. Internet J Microbiol 03 27 (2009) 13-0500 ISSN 1937-8289, Chennai, India
    • (2009) Internet J Microbiol , vol.3 , Issue.27 , pp. 13-0500
    • Sangeetha, R.1    Geetha, A.2    Arulpandi, I.3
  • 201
    • 0028025693 scopus 로고
    • Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
    • Schmidt-Dannert C., Sztajer H., Stocklein W., Menge U., and Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim Biophys Acta 1214 (1994) 43-53
    • (1994) Biochim Biophys Acta , vol.1214 , pp. 43-53
    • Schmidt-Dannert, C.1    Sztajer, H.2    Stocklein, W.3    Menge, U.4    Schmid, R.D.5
  • 202
    • 0029899631 scopus 로고    scopus 로고
    • Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. molecular cloning, nucleotide sequence, purification and some properties
    • Schmidt-Danert C., Rua M.L., Atomi H., and Schmid R.D. Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. molecular cloning, nucleotide sequence, purification and some properties. Biochim Biophys Acta 1301 (1996) 105-114
    • (1996) Biochim Biophys Acta , vol.1301 , pp. 105-114
    • Schmidt-Danert, C.1    Rua, M.L.2    Atomi, H.3    Schmid, R.D.4
  • 203
    • 0344577852 scopus 로고    scopus 로고
    • Fluorescent inhibitors for the qualitative and quantitative analysis of lipolytic enzymes
    • Scholze H., Stütz H., Paltauf F., and Hermetter A. Fluorescent inhibitors for the qualitative and quantitative analysis of lipolytic enzymes. Anal Biochem 276 1 (1999) 72-80
    • (1999) Anal Biochem , vol.276 , Issue.1 , pp. 72-80
    • Scholze, H.1    Stütz, H.2    Paltauf, F.3    Hermetter, A.4
  • 204
    • 0032895646 scopus 로고    scopus 로고
    • Bioreactor operated production of lipase: castor oil hydrolysis using partially-purified lipase
    • Sharon C., Nakazato M., Ogawa H.I., and Kato Y. Bioreactor operated production of lipase: castor oil hydrolysis using partially-purified lipase. Indian J Exp Biol 5 (1999) 481-486
    • (1999) Indian J Exp Biol , vol.5 , pp. 481-486
    • Sharon, C.1    Nakazato, M.2    Ogawa, H.I.3    Kato, Y.4
  • 205
    • 0023304214 scopus 로고
    • A numerical taxonomic study of psychrotrophic bacteria associated with lipolytic spoilage of raw milk
    • Shelley A.W., Deeth H.C., and MacRae I.C. A numerical taxonomic study of psychrotrophic bacteria associated with lipolytic spoilage of raw milk. J Appl Bacteriol 62 (1987) 197-207
    • (1987) J Appl Bacteriol , vol.62 , pp. 197-207
    • Shelley, A.W.1    Deeth, H.C.2    MacRae, I.C.3
  • 206
    • 0023144607 scopus 로고
    • Review of methods of enumeration, detection and isolation of lipolytic microorganisms with special reference to dairy applications
    • Shelley A.W., Deeth H.C., and MacRae I.C. Review of methods of enumeration, detection and isolation of lipolytic microorganisms with special reference to dairy applications. J Microbiol Meth 6 (1987) 123-137
    • (1987) J Microbiol Meth , vol.6 , pp. 123-137
    • Shelley, A.W.1    Deeth, H.C.2    MacRae, I.C.3
  • 207
    • 0027278512 scopus 로고
    • Purification and characterization of a novel solvent-tolerant lipase from Fusarium heterosporum
    • Shimada Y., Koga C., Sugihara A., Nagao T., Takada N., and Tsunasawa S. Purification and characterization of a novel solvent-tolerant lipase from Fusarium heterosporum. J Ferment Bioeng 75 (1993) 349-352
    • (1993) J Ferment Bioeng , vol.75 , pp. 349-352
    • Shimada, Y.1    Koga, C.2    Sugihara, A.3    Nagao, T.4    Takada, N.5    Tsunasawa, S.6
  • 208
    • 35748936435 scopus 로고    scopus 로고
    • Aspergillus niger lipase: gene cloning, over-expression in Escherichia coli and in vitro refolding
    • Shu Z.Y., Yan Y.J., Yang J.K., and Xu L. Aspergillus niger lipase: gene cloning, over-expression in Escherichia coli and in vitro refolding. Biotechnol Lett 29 12 (2007) 1875-1879
    • (2007) Biotechnol Lett , vol.29 , Issue.12 , pp. 1875-1879
    • Shu, Z.Y.1    Yan, Y.J.2    Yang, J.K.3    Xu, L.4
  • 209
    • 70350001196 scopus 로고    scopus 로고
    • Ecological screening for lipolytic molds and process optimization for lipase production from Rhizopus oryzae KG-5
    • Shukla P., and Gupta K. Ecological screening for lipolytic molds and process optimization for lipase production from Rhizopus oryzae KG-5. J Appl Sci Environ Sanit 2 2 (2007) 35-42
    • (2007) J Appl Sci Environ Sanit , vol.2 , Issue.2 , pp. 35-42
    • Shukla, P.1    Gupta, K.2
  • 210
    • 0348195651 scopus 로고    scopus 로고
    • Production of extracellular alkaline lipase by a new thermophilic Bacillus sp
    • Sidhu P., Sharma R., Soni S.K., and Gupta J.K. Production of extracellular alkaline lipase by a new thermophilic Bacillus sp. Folia Microbiol (Praha) 43 (1998) 51-54
    • (1998) Folia Microbiol (Praha) , vol.43 , pp. 51-54
    • Sidhu, P.1    Sharma, R.2    Soni, S.K.3    Gupta, J.K.4
  • 212
    • 0032079361 scopus 로고    scopus 로고
    • Cloning, purification and characterization of the lipase from Staphylococcus epidermidis-comparison of the substrate selectivity with those of other microbial lipases
    • Simons J.W., van Kampen M.D., Riel S., Götz F., Egmond M.R., and Verheij H.M. Cloning, purification and characterization of the lipase from Staphylococcus epidermidis-comparison of the substrate selectivity with those of other microbial lipases. Eur J Biochem 253 (1998) 675-683
    • (1998) Eur J Biochem , vol.253 , pp. 675-683
    • Simons, J.W.1    van Kampen, M.D.2    Riel, S.3    Götz, F.4    Egmond, M.R.5    Verheij, H.M.6
  • 213
    • 0030886660 scopus 로고    scopus 로고
    • Physical behavior of lipase substrate
    • Small D.M. Physical behavior of lipase substrate. Methods Enzymol 286 (1997) 153-167
    • (1997) Methods Enzymol , vol.286 , pp. 153-167
    • Small, D.M.1
  • 214
    • 0026758653 scopus 로고
    • Quantitative spectrophotometric assay for Staphylococcal lipase
    • Smeltzer M.S., Hart M.E., and Iandolo J.J. Quantitative spectrophotometric assay for Staphylococcal lipase. Appl Environ Microbiol 58 (1992) 2815-2819
    • (1992) Appl Environ Microbiol , vol.58 , pp. 2815-2819
    • Smeltzer, M.S.1    Hart, M.E.2    Iandolo, J.J.3
  • 215
    • 53349178725 scopus 로고    scopus 로고
    • Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1
    • Snellman E.A., and Colwell R.R. Transesterification activity of a novel lipase from Acinetobacter venetianus RAG-1. Antonie Van Leeuwenhoek 94 4 (2008) 621-625
    • (2008) Antonie Van Leeuwenhoek , vol.94 , Issue.4 , pp. 621-625
    • Snellman, E.A.1    Colwell, R.R.2
  • 217
    • 4444314047 scopus 로고    scopus 로고
    • Development and analytical validation of an enzyme linked immunosorbent assay for the measurement of canine gastric lipase immunoreactivity in serum
    • Steiner J.M., and Williams D.A. Development and analytical validation of an enzyme linked immunosorbent assay for the measurement of canine gastric lipase immunoreactivity in serum. Can J Vet Res 68 3 (2004) 161-168
    • (2004) Can J Vet Res , vol.68 , Issue.3 , pp. 161-168
    • Steiner, J.M.1    Williams, D.A.2
  • 218
    • 0021181446 scopus 로고
    • Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals
    • Sternby B., and Akerstrom B. Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals. Biochim Biophys Acta 789 (1984) 164-169
    • (1984) Biochim Biophys Acta , vol.789 , pp. 164-169
    • Sternby, B.1    Akerstrom, B.2
  • 219
    • 0025766884 scopus 로고
    • Pancreatic lipolytic enzymes in human duodenal contents: radioimmunoassay compared with enzyme activity
    • Sternby B., Nilsson A., Melin T., and Borgström B. Pancreatic lipolytic enzymes in human duodenal contents: radioimmunoassay compared with enzyme activity. Scand J Gastroenterol 26 (1991) 859-866
    • (1991) Scand J Gastroenterol , vol.26 , pp. 859-866
    • Sternby, B.1    Nilsson, A.2    Melin, T.3    Borgström, B.4
  • 220
    • 0022913002 scopus 로고
    • Purification of extracellular lipase from Pseudomonas aeruginosa
    • Stuer W., Jaeger K.E., and Winkler U.K. Purification of extracellular lipase from Pseudomonas aeruginosa. J Bacteriol 168 (1986) 1070-1074
    • (1986) J Bacteriol , vol.168 , pp. 1070-1074
    • Stuer, W.1    Jaeger, K.E.2    Winkler, U.K.3
  • 221
    • 0026026966 scopus 로고
    • Purification and characterization of a novel thermostable lipase from Bacillus sp
    • Sugihara A., Tani T., and Tominaga Y. Purification and characterization of a novel thermostable lipase from Bacillus sp. J Biochem 109 (1991) 211-216
    • (1991) J Biochem , vol.109 , pp. 211-216
    • Sugihara, A.1    Tani, T.2    Tominaga, Y.3
  • 222
    • 0001951183 scopus 로고
    • Bacterial lipases
    • Borgstrom B., and Brockman H.L. (Eds), Elsevier, Amsterdam
    • Sugiura M. Bacterial lipases. In: Borgstrom B., and Brockman H.L. (Eds). Lipases (1984), Elsevier, Amsterdam 505-524
    • (1984) Lipases , pp. 505-524
    • Sugiura, M.1
  • 223
    • 0015953506 scopus 로고
    • Studies on the lipase of Chromobacterium visurum. III. Purification of a low molecular weight lipase and its enzymatic properties
    • Sugiura M., and Isobe M. Studies on the lipase of Chromobacterium visurum. III. Purification of a low molecular weight lipase and its enzymatic properties. Biochim Biophysics Acta 341 (1974) 195-200
    • (1974) Biochim Biophysics Acta , vol.341 , pp. 195-200
    • Sugiura, M.1    Isobe, M.2
  • 224
    • 0016730839 scopus 로고
    • Effects on temperature and state of substrate on rate of hydrolysis of glycerides by lipase
    • Sugiura M., and Isobe M. Effects on temperature and state of substrate on rate of hydrolysis of glycerides by lipase. Chem Pharm Bull 23 (1975) 681-682
    • (1975) Chem Pharm Bull , vol.23 , pp. 681-682
    • Sugiura, M.1    Isobe, M.2
  • 225
    • 0016185111 scopus 로고
    • Purification and properties of a Chromobacterium lipase with a high molecular weight
    • Sugiura M., Isobe M., Muroya N., and Yamaguchi T. Purification and properties of a Chromobacterium lipase with a high molecular weight. Agri Biol Chem 38 (1974) 947-952
    • (1974) Agri Biol Chem , vol.38 , pp. 947-952
    • Sugiura, M.1    Isobe, M.2    Muroya, N.3    Yamaguchi, T.4
  • 226
    • 0016529478 scopus 로고
    • Application of lipoprotein lipase for the assay of serum triglyceride
    • Sugiura M., Isobe M., Hirata F., and Inagawa T. Application of lipoprotein lipase for the assay of serum triglyceride. Chem Pharm Bull 23 7 (1975) 1417-1420
    • (1975) Chem Pharm Bull , vol.23 , Issue.7 , pp. 1417-1420
    • Sugiura, M.1    Isobe, M.2    Hirata, F.3    Inagawa, T.4
  • 227
    • 0017669295 scopus 로고
    • Purification, crystallization and properties of triacyglycerol lipase from Pseudomonas fluorescens
    • Sugiura M., Oikawa T., Hirano K., and Inukai T. Purification, crystallization and properties of triacyglycerol lipase from Pseudomonas fluorescens. Biochim Biophysics Acta 488 (1977) 353-358
    • (1977) Biochim Biophysics Acta , vol.488 , pp. 353-358
    • Sugiura, M.1    Oikawa, T.2    Hirano, K.3    Inukai, T.4
  • 229
    • 34249907264 scopus 로고    scopus 로고
    • Rivoflavin may interfere with on-line monitoring of secreted green fluorescence protein fusion proteins in Pichia pastoris
    • Surribas A., Resina D., Ferrer P., and Valero F. Rivoflavin may interfere with on-line monitoring of secreted green fluorescence protein fusion proteins in Pichia pastoris. Microb Cell Fact 6 (2007) 15
    • (2007) Microb Cell Fact , vol.6 , pp. 15
    • Surribas, A.1    Resina, D.2    Ferrer, P.3    Valero, F.4
  • 230
    • 0022816957 scopus 로고
    • Purification and general properties of a metal-insensitive lipase from
    • Suzuki M., Yamamoto H., and Mizugaki M. Purification and general properties of a metal-insensitive lipase from. J Biochem (Tokyo) 100 (1986) 1207-1213
    • (1986) J Biochem (Tokyo) , vol.100 , pp. 1207-1213
    • Suzuki, M.1    Yamamoto, H.2    Mizugaki, M.3
  • 232
    • 0028910051 scopus 로고
    • Purification and characterization of extracellular Staphylococcus warneri lipase
    • Talon R., Dublet N., Montel M.C., and Cantonnet M. Purification and characterization of extracellular Staphylococcus warneri lipase. Curr Microbiol 30 (1995) 11-16
    • (1995) Curr Microbiol , vol.30 , pp. 11-16
    • Talon, R.1    Dublet, N.2    Montel, M.C.3    Cantonnet, M.4
  • 233
    • 0025768447 scopus 로고
    • A continuous fluorimetric assay for phospholipase C from Clostridium perfringens
    • Thuren T., and Kinnunen P.K.J. A continuous fluorimetric assay for phospholipase C from Clostridium perfringens. Chem Phys Lipids 59 (1991) 69-74
    • (1991) Chem Phys Lipids , vol.59 , pp. 69-74
    • Thuren, T.1    Kinnunen, P.K.J.2
  • 234
    • 0023882714 scopus 로고
    • Phospholipase A2 assay using an intramolecularly quenched pyren-labeled phospholipid analog as a substrate
    • Thuren T., Virtanen J.A., Somerharju P.J., and Kunnunen P.K.J. Phospholipase A2 assay using an intramolecularly quenched pyren-labeled phospholipid analog as a substrate. Anal Biochem 170 (1988) 248-255
    • (1988) Anal Biochem , vol.170 , pp. 248-255
    • Thuren, T.1    Virtanen, J.A.2    Somerharju, P.J.3    Kunnunen, P.K.J.4
  • 235
    • 0032038256 scopus 로고    scopus 로고
    • Purification and characterization of triacylglycerol lipase from Aspergillus oryzae
    • Toida J., Arikawa Y., Kondou K., Fukuzawa M., and Sekiguchi J. Purification and characterization of triacylglycerol lipase from Aspergillus oryzae. Biosci Biotechnol Biochem 62 (1998) 759-763
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 759-763
    • Toida, J.1    Arikawa, Y.2    Kondou, K.3    Fukuzawa, M.4    Sekiguchi, J.5
  • 236
    • 0027319112 scopus 로고
    • Reverse-phase high-performance liquid chromatographic assay of phospholipases: application of spectrophotometric detection to rat phospholipase A2 isozymes
    • Tojo H., Ono T., and Okamoto M. Reverse-phase high-performance liquid chromatographic assay of phospholipases: application of spectrophotometric detection to rat phospholipase A2 isozymes. J Lipid Res 34 (1993) 837-844
    • (1993) J Lipid Res , vol.34 , pp. 837-844
    • Tojo, H.1    Ono, T.2    Okamoto, M.3
  • 237
    • 37649003923 scopus 로고    scopus 로고
    • Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography
    • Trodler P., Nieveler J., Rusnak M., Schmid R.D., and Pleiss J. Rational design of a new one-step purification strategy for Candida antarctica lipase B by ion-exchange chromatography. J Chromatogr A 1179 2 (2008) 161-167
    • (2008) J Chromatogr A , vol.1179 , Issue.2 , pp. 161-167
    • Trodler, P.1    Nieveler, J.2    Rusnak, M.3    Schmid, R.D.4    Pleiss, J.5
  • 238
    • 0021114598 scopus 로고
    • Purification and some properties of the staphylococcal extracellular lipase
    • Tyski S., Hryniewicz W., and Jeljaszewicz J. Purification and some properties of the staphylococcal extracellular lipase. Biochim Biophys Acta 749 (1983) 312-317
    • (1983) Biochim Biophys Acta , vol.749 , pp. 312-317
    • Tyski, S.1    Hryniewicz, W.2    Jeljaszewicz, J.3
  • 239
    • 0035150136 scopus 로고    scopus 로고
    • DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa
    • Urban A., Leipelt M., Eggert T., and Jaeger K.E. DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa. J Bacteriol 183 2 (2001) 587-596
    • (2001) J Bacteriol , vol.183 , Issue.2 , pp. 587-596
    • Urban, A.1    Leipelt, M.2    Eggert, T.3    Jaeger, K.E.4
  • 241
    • 0026635877 scopus 로고
    • Lipases from different sources vary widely in dependence of catalytic activity on water activity
    • Valivety R.H., Halling P.J., Peilow A.D., and MacRae A.R. Lipases from different sources vary widely in dependence of catalytic activity on water activity. Biochim Biophys Acta 1122 (1992) 143-146
    • (1992) Biochim Biophys Acta , vol.1122 , pp. 143-146
    • Valivety, R.H.1    Halling, P.J.2    Peilow, A.D.3    MacRae, A.R.4
  • 242
    • 0025309695 scopus 로고
    • Purification and characterization of two distinct lipases from Geotrichum candidum
    • Veeraragavan K., Colpitts T., and Gibbs B.F. Purification and characterization of two distinct lipases from Geotrichum candidum. Biochim Biophys Acta 1044 (1990) 26-33
    • (1990) Biochim Biophys Acta , vol.1044 , pp. 26-33
    • Veeraragavan, K.1    Colpitts, T.2    Gibbs, B.F.3
  • 243
    • 0018890516 scopus 로고
    • Enzyme kinetics of lipolysis
    • Verger R. Enzyme kinetics of lipolysis. Methods Enzymol 64 (1980) 341-392
    • (1980) Methods Enzymol , vol.64 , pp. 341-392
    • Verger, R.1
  • 244
    • 0031023666 scopus 로고    scopus 로고
    • Interfacial activation of lipases: facts and artifacts
    • Verger R. Interfacial activation of lipases: facts and artifacts. Trends Biotechnol 15 (1997) 32-38
    • (1997) Trends Biotechnol , vol.15 , pp. 32-38
    • Verger, R.1
  • 245
    • 0020382687 scopus 로고
    • Lipid-protein interactions in monolayers
    • Verger R., and Pattus F. Lipid-protein interactions in monolayers. Chem Phys Lipids 30 (1982) 189-227
    • (1982) Chem Phys Lipids , vol.30 , pp. 189-227
    • Verger, R.1    Pattus, F.2
  • 246
    • 0032254070 scopus 로고    scopus 로고
    • In vitro measurement of lipoprotein and hepatic lipases
    • Villela E., and Joven J. In vitro measurement of lipoprotein and hepatic lipases. Methods Mol Biol 110 (1998) 243-251
    • (1998) Methods Mol Biol , vol.110 , pp. 243-251
    • Villela, E.1    Joven, J.2
  • 248
    • 0024517405 scopus 로고
    • A continuous assay for lipases in reverse micelles based on Fourier transform infrared spectroscopy
    • Walde P., and Luisi P.L. A continuous assay for lipases in reverse micelles based on Fourier transform infrared spectroscopy. Biochemistry 28 (1989) 3353-3360
    • (1989) Biochemistry , vol.28 , pp. 3353-3360
    • Walde, P.1    Luisi, P.L.2
  • 249
    • 57649224365 scopus 로고    scopus 로고
    • Purification and characterization of extracellular lipases from Pseudomonas monteilii TKU009 by the use of soybeans as the substrate
    • Wang S.L., Lin Y.T., Liang T.W., Chio S.H., Ming L.J., and Wu P.C. Purification and characterization of extracellular lipases from Pseudomonas monteilii TKU009 by the use of soybeans as the substrate. J Ind Microbiol Biotechnol 36 1 (2009) 65-73
    • (2009) J Ind Microbiol Biotechnol , vol.36 , Issue.1 , pp. 65-73
    • Wang, S.L.1    Lin, Y.T.2    Liang, T.W.3    Chio, S.H.4    Ming, L.J.5    Wu, P.C.6
  • 250
    • 0017655156 scopus 로고
    • Studies on alkaline lipases from Pseudomonas species. Part I: Isolation and identification of alkaline lipase producing microorganisms, cultural conditions and some properties of the crude enzymes
    • Watanabe N., Ota Y., Minoda Y., and Yamada K. Studies on alkaline lipases from Pseudomonas species. Part I: Isolation and identification of alkaline lipase producing microorganisms, cultural conditions and some properties of the crude enzymes. Agric Biol Chem 41 (1977) 1353-1358
    • (1977) Agric Biol Chem , vol.41 , pp. 1353-1358
    • Watanabe, N.1    Ota, Y.2    Minoda, Y.3    Yamada, K.4
  • 251
    • 0015937861 scopus 로고
    • A rapid and specific method for the determination of pancreatic lipase in serum and urine
    • Whitaker J. A rapid and specific method for the determination of pancreatic lipase in serum and urine. Clin Chim Acta 44 (1973) 133-138
    • (1973) Clin Chim Acta , vol.44 , pp. 133-138
    • Whitaker, J.1
  • 253
    • 84921078455 scopus 로고
    • Lipases
    • Desnuelle P. (Ed), Macmillan (Pergamon), New York
    • Wills E.D. Lipases. In: Desnuelle P. (Ed). The enzymes of lipid metabolism (1961), Macmillan (Pergamon), New York 13-402
    • (1961) The enzymes of lipid metabolism , pp. 13-402
    • Wills, E.D.1
  • 254
    • 0025911613 scopus 로고
    • A continuous fluorescence-displacement assay for triacylglycerol lipase and phospholipase C that also allows the measurement of acylglycerols
    • Wilton D.C. A continuous fluorescence-displacement assay for triacylglycerol lipase and phospholipase C that also allows the measurement of acylglycerols. Biochem J 276 (1991) 129-133
    • (1991) Biochem J , vol.276 , pp. 129-133
    • Wilton, D.C.1
  • 255
    • 0018999368 scopus 로고
    • Fluorometric and colorimetric enzymic determination of triglycerides (triacylglycerols) in serum
    • Winartasaputra H., Mallet V.N., Kuan S.S., and Guilbault G.G. Fluorometric and colorimetric enzymic determination of triglycerides (triacylglycerols) in serum. Clin Chem 26 (1980) 613-617
    • (1980) Clin Chem , vol.26 , pp. 613-617
    • Winartasaputra, H.1    Mallet, V.N.2    Kuan, S.S.3    Guilbault, G.G.4
  • 256
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens
    • Winkler U.K., and Stuckmann M. Glycogen, hyaluronate and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J Bacteriol 138 (1979) 663-670
    • (1979) J Bacteriol , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 257
    • 0017887641 scopus 로고
    • Pleiotropic consequences of mutations towards antibiotic hypersensitivity in Serratia marcescens
    • Winkler U.K., Heller B., and Folle B. Pleiotropic consequences of mutations towards antibiotic hypersensitivity in Serratia marcescens. Arch Microbiol 116 (1978) 259-268
    • (1978) Arch Microbiol , vol.116 , pp. 259-268
    • Winkler, U.K.1    Heller, B.2    Folle, B.3
  • 259
    • 0021352650 scopus 로고
    • Hydrolysis of a fluorescent phospholipid substrate by phospholipase A2 and lipoprotein lipase
    • Wittenauer L., Shirai A.K., Jackson R.L., and Johnson J.D. Hydrolysis of a fluorescent phospholipid substrate by phospholipase A2 and lipoprotein lipase. Biochem Biophys Res Commun 118 (1984) 894-901
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 894-901
    • Wittenauer, L.1    Shirai, A.K.2    Jackson, R.L.3    Johnson, J.D.4
  • 260
    • 0031701836 scopus 로고    scopus 로고
    • Purification and characterization of a regiospecific lipase from Aspergillus terreus
    • Yadav R.P., Saxena R.K., Gupta R., and Davidson W.S. Purification and characterization of a regiospecific lipase from Aspergillus terreus. Biotechnol Appl Biochem 28 (1998) 243-249
    • (1998) Biotechnol Appl Biochem , vol.28 , pp. 243-249
    • Yadav, R.P.1    Saxena, R.K.2    Gupta, R.3    Davidson, W.S.4
  • 261
    • 49349093802 scopus 로고    scopus 로고
    • Molecular cloning and expression of a cold-adapted lipase gene from an Antarctic deep sea psychrotrophic bacterium Pseudomonas sp. 7323
    • Zhang J.W., and Zeng R.Y. Molecular cloning and expression of a cold-adapted lipase gene from an Antarctic deep sea psychrotrophic bacterium Pseudomonas sp. 7323. Mar Biotechnol (NY) 10 5 (2008) 612-621
    • (2008) Mar Biotechnol (NY) , vol.10 , Issue.5 , pp. 612-621
    • Zhang, J.W.1    Zeng, R.Y.2
  • 262
    • 66749094353 scopus 로고    scopus 로고
    • Screening for lipase-producing Enterobacter agglomerans for biodiesel catalyzation
    • Zhen-qian Z., and Chun-yun G. Screening for lipase-producing Enterobacter agglomerans for biodiesel catalyzation. Afr J Biotechnol 8 7 (2009) 1273-1279
    • (2009) Afr J Biotechnol , vol.8 , Issue.7 , pp. 1273-1279
    • Zhen-qian, Z.1    Chun-yun, G.2
  • 263
    • 0015922751 scopus 로고
    • Nephelometric determination of pancreatic enzymes. II. Lipase
    • Zinterhofer L., Wardlaw S., Jatlow P., and Seligson D. Nephelometric determination of pancreatic enzymes. II. Lipase. Clin Chim Acta 44 (1973) 173-178
    • (1973) Clin Chim Acta , vol.44 , pp. 173-178
    • Zinterhofer, L.1    Wardlaw, S.2    Jatlow, P.3    Seligson, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.