메뉴 건너뛰기




Volumn 35, Issue 6, 2012, Pages 931-941

A process for extracellular thermostable lipase production by a novel Bacillus thermoamylovorans strain

Author keywords

Enzyme; Kinetics; Lipase; Optimisation; Stirred tank; Thermophiles

Indexed keywords

AERATION RATE; BIOLOGICAL PROCESS; DEACTIVATION MODEL; EXTRACELLULAR; EXTRACELLULAR LIPOLYTIC ACTIVITY; GALICIA; INITIAL PH VALUE; LIPASE PRODUCTION; LIPOLYTIC; LIPOLYTIC ENZYMES; LOGISTIC EQUATIONS; LONG-CHAIN FATTY ACIDS; OPTIMISATIONS; SCALING-UP; SERIES-TYPE; SHAKE-FLASK CULTURES; STIRRED TANK; STIRRED TANK BIOREACTORS; THERMOPHILES; THERMOPHILIC MICROORGANISMS;

EID: 84865337994     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-011-0678-9     Document Type: Article
Times cited : (25)

References (41)
  • 2
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • DOI 10.1016/S0167-7799(98)01195-0, PII S0167779998011950
    • Jaeger KE, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396-403 (Pubitemid 28410428)
    • (1998) Trends in Biotechnology , vol.16 , Issue.9 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 3
    • 57749195073 scopus 로고    scopus 로고
    • Lipolytic enzyme production by immobilized Rhizopus oryzae
    • Lopez E, Deive F, Longo MA, Sanromán MA (2008) Lipolytic enzyme production by immobilized Rhizopus oryzae. Chem Eng Technol 31:1555-1560
    • (2008) Chem Eng Technol , vol.31 , pp. 1555-1560
    • Lopez, E.1    Deive, F.2    Longo, M.A.3    Sanromán, M.A.4
  • 4
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: An overview of production, purification and biochemical properties
    • DOI 10.1007/s00253-004-1568-8
    • Gupta R, Gupta N, Rathi P (2004) Bacterial lipase: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64:763-781 (Pubitemid 38918139)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.6 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 5
    • 0014148305 scopus 로고
    • Life at high temperatures
    • Brock TD (1967) Life at high temperatures. Science 158: 1012-1019
    • (1967) Science , vol.158 , pp. 1012-1019
    • Brock, T.D.1
  • 6
    • 79955967117 scopus 로고    scopus 로고
    • On the hyperthermostability of lipolytic enzymes from Thermus aquaticus YT-1: Exploring their application to polymer degradation
    • López E, Alonso B, Deive FJ, Sanromán MA, Longo MA (2011) On the hyperthermostability of lipolytic enzymes from Thermus aquaticus YT-1: exploring their application to polymer degradation. J Chem Technol Biotechnol 86:838-844
    • (2011) J Chem Technol Biotechnol , vol.86 , pp. 838-844
    • López, E.1    Alonso, B.2    Deive, F.J.3    Sanromán, M.A.4    Longo, M.A.5
  • 7
    • 70449403245 scopus 로고    scopus 로고
    • Evaluation of a novel Bacillus strain from a north-western Spain hot spring as a source of extracellular thermostable lipase
    • Deive FJ, Sanromán M, Longo MA (2009) Evaluation of a novel Bacillus strain from a north-western Spain hot spring as a source of extracellular thermostable lipase. J Chem Technol Biotechnol 84:1509-1515
    • (2009) J Chem Technol Biotechnol , vol.84 , pp. 1509-1515
    • Deive, F.J.1    Sanromán, M.2    Longo, M.A.3
  • 9
    • 5044228263 scopus 로고    scopus 로고
    • Identification of extracellular enzyme producing thermophilic bacilli from Balcova (Agamemnon) geothermal site by ITS rDNA RFLP
    • DOI 10.1111/j.1365-2672.2004.02374.x
    • Yavuz E, Gunes H, Harsa H, Yenidunya AF (2004) Identification of extracellular enzyme producing thermophilic bacilli from Balcova (Agamemnon) geothermal site by ITS rDNA RFLP. J Appl Microbiol 97:810-817 (Pubitemid 39334847)
    • (2004) Journal of Applied Microbiology , vol.97 , Issue.4 , pp. 810-817
    • Yavuz, E.1    Gunes, H.2    Harsa, S.3    Yenidunya, A.F.4
  • 10
    • 0035720329 scopus 로고    scopus 로고
    • Identification of thermophilic and marine bacilli from shallow thermal vents by restriction analysis of their amplified 16s rDNA
    • DOI 10.1046/j.1365-2672.2001.01410.x
    • Caccamo D, Maugeri TL, Gugliandolo C (2001) Identification of thermophilic and marine bacilli from shallow thermal vents by restriction analysis of their amplified 16S rDNA. J Appl Microbiol 91:520-524 (Pubitemid 34205765)
    • (2001) Journal of Applied Microbiology , vol.91 , Issue.3 , pp. 520-524
    • Caccamo, D.1    Maugeri, T.L.2    Gugliandolo, C.3
  • 11
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • DOI 10.1016/S0960-8524(03)00033-6
    • Haki GD, Rakshit SK (2003) Developments in industrially important thermostable enzymes: a review. Bioresour Technol 89:17-34 (Pubitemid 36379207)
    • (2003) Bioresource Technology , vol.89 , Issue.1 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 13
    • 0024811833 scopus 로고
    • The effect of Maillard reaction products on zinc metabolism in the rat
    • DOI 10.1079/BJN19890074
    • Furniss DE, Vuichoud J, Finot PA, Hurrell RF (1989) The effect of Maillard reaction products on zinc metabolism in the rat. Br J Nutr 62:739-749 (Pubitemid 20014009)
    • (1989) British Journal of Nutrition , vol.62 , Issue.3 , pp. 739-749
    • Furniss, D.E.1    Vuichoud, J.2    Finot, P.A.3    Hurrell, R.F.4
  • 15
    • 0036890248 scopus 로고    scopus 로고
    • The production of biocatalysts and biomolecules from extremophiles
    • Schiraldi C, De Rosa M (2002) The production of biocatalysts and biomolecules from extremophiles. Trends Biotechnol 20: 515-520
    • (2002) Trends Biotechnol , vol.20 , pp. 515-520
    • Schiraldi, C.1    De Rosa, M.2
  • 16
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • DOI 10.1016/0378-1119(88)90330-7
    • Higgins DG, Sharp PM (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73:237-244 (Pubitemid 19033800)
    • (1988) Gene , vol.73 , Issue.1 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 18
    • 51649149161 scopus 로고
    • Partial purification and characterization of free and immobilized lipase from Mucor miehei
    • Huge-Jensen B, Galluzzo DR, Jensen RG (1987) Partial purification and characterization of free and immobilized lipase from Mucor miehei. Lipids 22:559-656
    • (1987) Lipids , vol.22 , pp. 559-656
    • Huge-Jensen, B.1    Galluzzo, D.R.2    Jensen, R.G.3
  • 20
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M, Giles UA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350-356
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Giles, U.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 21
    • 0028816327 scopus 로고
    • Effect of pH on Bacillus thermoamylovorans growth and glucose fermentation
    • Combet-Blanc Y, Kalamba KK, Kergoat PY (1995) Effect of pH on Bacillus thermoamylovorans growth and glucose fermentation. Appl Environ Microbiol 61:656-659
    • (1995) Appl Environ Microbiol , vol.61 , pp. 656-659
    • Combet-Blanc, Y.1    Kalamba, K.K.2    Kergoat, P.Y.3
  • 23
    • 15744397346 scopus 로고    scopus 로고
    • Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3
    • DOI 10.1016/j.pep.2004.12.010
    • Kumar S, Kikon K, Upadhyay A, Kanwar SS, Gupta R (2005) Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3. Protein Exp Purif 41:38-44 (Pubitemid 40406361)
    • (2005) Protein Expression and Purification , vol.41 , Issue.1 , pp. 38-44
    • Kumar, S.1    Kikon, K.2    Upadhyay, A.3    Kanwar, S.S.4    Gupta, R.5
  • 24
    • 0020784001 scopus 로고
    • Lipases production by Bacillus circulans under mesophilic and osmophilic conditions. Factors affecting lipases production
    • Elwan SH, el-Hoseiny MM, Ammar MS, Mostafa SA (1993) Lipases production by Bacillus circulans under mesophilic and osmophilic conditions. Factors affecting lipases production. Gen Bacteriol Virol Immunol 76:187-189
    • (1993) Gen Bacteriol Virol Immunol , vol.76 , pp. 187-189
    • Elwan, S.H.1    El-Hoseiny, M.M.2    Ammar, M.S.3    Mostafa, S.A.4
  • 25
    • 0032843146 scopus 로고    scopus 로고
    • Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027
    • DOI 10.1016/S0378-1097(99)00383-3, PII S0378109799003833
    • Dharmsthiti S, Luchai S (1999) Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027. FEMS Microbiol Lett 179:241-246 (Pubitemid 29460684)
    • (1999) FEMS Microbiology Letters , vol.179 , Issue.2 , pp. 241-246
    • Dharmsthiti, S.1    Luchai, S.2
  • 26
    • 0030773417 scopus 로고    scopus 로고
    • Increase in specific growth rate of suspended bacteria through ponds and tanks used in intensive fish farming
    • Bedwell MS, Goulder R (1997) Increase in specific growth rate of suspended bacteria through ponds and tanks used in intensive fish farming. Lett Appl Microbiol 25:212-214 (Pubitemid 27396004)
    • (1997) Letters in Applied Microbiology , vol.25 , Issue.3 , pp. 212-214
    • Bedwell, M.S.1    Goulder, R.2
  • 27
    • 0035286466 scopus 로고    scopus 로고
    • Specific Growth Rate Plays a Critical Role in Hydrogen Peroxide Resistance of the Marine Oligotrophic Ultramicrobacterium Sphingomonas alaskensis Strain RB2256
    • DOI 10.1128/AEM.67.3.1292-1299.2001
    • Ostrowski M, Cavicchioli R, Blaauw M, Gottschal JC (2001) Specific growth rate plays a critical role in hydrogen peroxide resistance of the marine oligotrophic ultramicrobacterium Sphingomonas alaskensis strain RB2256. Appl Environ Microbiol 67:1292-1299 (Pubitemid 33643574)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.3 , pp. 1292-1299
    • Ostrowski, M.1    Cavicchioli, R.2    Blaauw, M.3    Gottschal, J.C.4
  • 28
    • 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
    • DOI 10.1007/s002530051036
    • Becker P, Abu-Rees I, Markossian S, Antranikian G, Märkl H (1997) Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. IHI-91 on olive oil. Appl Microbiol Biotechnol 48:184-190 (Pubitemid 27394748)
    • (1997) Applied Microbiology and Biotechnology , vol.48 , Issue.2 , pp. 184-190
    • Becker, P.1    Abu-Reesh, I.2    Markossian, S.3    Antranikian, G.4    Markl, H.5
  • 30
    • 0001010013 scopus 로고
    • A kinetic study of the lactic acid fermentation. Batch process at controlled pH
    • Luedeking R, Piret EL (1959) A kinetic study of the lactic acid fermentation. Batch process at controlled pH. J Biochem Microbiol Technol Eng 1:393-412
    • (1959) J Biochem Microbiol Technol Eng , vol.1 , pp. 393-412
    • Luedeking, R.1    Piret, E.L.2
  • 31
    • 18144427525 scopus 로고    scopus 로고
    • An unstructured model for the diauxic growth of Penicillium camembertii on glucose and arginine
    • DOI 10.1016/j.bej.2005.02.009
    • Amrane A, Adour L, Couriol C (2005) An unstructured model for the diauxic growth of Penicillium camembertii on glucose and arginine. Biochem Eng J 24:125-133 (Pubitemid 40616124)
    • (2005) Biochemical Engineering Journal , vol.24 , Issue.2 , pp. 125-133
    • Amrane, A.1    Adour, L.2    Couriol, C.3
  • 32
    • 0033524798 scopus 로고    scopus 로고
    • Effect of oxygen transfer on lipase production by Acinetobacter radioresistens
    • Chen JY, Wen CM, Chen TL (1999) Effect of oxygen transfer on lipase production by Acinetobacter radioresistens. Biotechnol Bioeng 62:311-316
    • (1999) Biotechnol Bioeng , vol.62 , pp. 311-316
    • Chen, J.Y.1    Wen, C.M.2    Chen, T.L.3
  • 33
    • 0020504842 scopus 로고
    • Factors affecting lipase production in Syncephalastrum racemosum
    • Chopra AK, Chander H (1983) Factors affecting lipase production in Syncephalastrum racemosum. J Appl Bacteriol 54:163-169 (Pubitemid 13098024)
    • (1983) Journal of Applied Bacteriology , vol.54 , Issue.2 , pp. 163-169
    • Chopra, A.K.1    Chander, H.2
  • 34
    • 3342883774 scopus 로고    scopus 로고
    • Quantification of intra- and extra-cellular thermophilic lipase/esterase production by Thermus sp
    • DOI 10.1023/B:BILE.0000024092.27943.75
    • Domínguez A, Sanromán MA, Fuciños P, Rúa ML, Pastrana L, Longo MA (2004) Quantification of intra- and extra-cellular thermophilic lipase/esterase production by Thermus spp. Biotechnol Lett 26:705-708 (Pubitemid 38982873)
    • (2004) Biotechnology Letters , vol.26 , Issue.9 , pp. 705-708
    • Dominguez, A.1    Sanroman, A.2    Fucinos, P.3    Rua, M.L.4    Pastrana, L.5    Longo, M.A.6
  • 35
    • 31044448437 scopus 로고    scopus 로고
    • A novel esterase from Bacillus subtilis (RRL 1789): Purification and characterization of the enzyme
    • DOI 10.1016/j.pep.2005.08.030, PII S1046592805002962
    • Kaiser P, Raina C, Parshad R, Johri S, Verma V, Andrabi KI, Qazi GN (2006) A novel esterase from Bacillus subtilis (RRL 1789): Purification and characterization of the enzyme. Protein Exp Purif 45:262-268 (Pubitemid 43120430)
    • (2006) Protein Expression and Purification , vol.45 , Issue.2 , pp. 262-268
    • Kaiser, P.1    Raina, C.2    Parshad, R.3    Johri, S.4    Verma, V.5    Andrabi, K.I.6    Qazi, G.N.7
  • 36
    • 0037009167 scopus 로고    scopus 로고
    • Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity
    • DOI 10.1016/S0141-0229(02)00133-3, PII S0141022902001333
    • Sunna A, Hunter L, Hutton CA, Bergquist PL (2002) Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity. Enzym Microb Technol 31:472-476 (Pubitemid 34874826)
    • (2002) Enzyme and Microbial Technology , vol.31 , Issue.4 , pp. 472-476
    • Sunna, A.1    Hunter, L.2    Hutton, C.A.3    Bergquist, P.L.4
  • 38
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • DOI 10.1016/0141-0229(85)90013-4
    • Henley JP, Sadana A (1985) Categorization of enzyme deactivations using a series-type mechanism. Enzym Microb Technol 7:50-60 (Pubitemid 15066619)
    • (1985) Enzyme and Microbial Technology , vol.7 , Issue.2 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 39
    • 0033003960 scopus 로고    scopus 로고
    • Thermostability of modified enzymes: A detailed study
    • DOI 10.1002/(SICI)1097-4660(199901)74:1<25::AID-JCTB978>3.0.CO;2-B
    • Longo MA, Combes D (1999) Thermostability of modified enzymes: a detailed study. J Chem Technol Biotechnol 74:25-32 (Pubitemid 29084259)
    • (1999) Journal of Chemical Technology and Biotechnology , vol.74 , Issue.1 , pp. 25-32
    • Longo, M.A.1    Combes, D.2
  • 40
    • 0042694726 scopus 로고    scopus 로고
    • Production of a thermostable extracellular lipase by Kluyveromyces marxianus
    • DOI 10.1023/A:1025049825720
    • Deive FJ, Costas M, Longo MA (2003) Production of thermostable extracellular lipase by Kluyveromyces marxianus. Biotechnol Lett 25:1403-1406 (Pubitemid 37065288)
    • (2003) Biotechnology Letters , vol.25 , Issue.17 , pp. 1403-1406
    • Deive, F.J.1    Costas, M.2    Longo, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.