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Volumn 10, Issue 1, 2011, Pages 115-131

Nutritional requirements and physical factors affecting the production of organic solvent-stable lipase by Acinetobacter baylyi

Author keywords

Acinetobacter baylyi; Lipase production; Nutritional requirements; Physical factors

Indexed keywords

ACINETOBACTER; ACINETOBACTER BAYLYI;

EID: 79960528554     PISSN: 16851994     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 0024818825 scopus 로고
    • Industrial enzymology: a look towards the future
    • Arbige, M.V., and W.H. Pitcher. 1989. Industrial enzymology: a look towards the future. Trends in Biotechnology 7: 330-335.
    • (1989) Trends in Biotechnology , vol.7 , pp. 330-335
    • Arbige, M.V.1    Pitcher, W.H.2
  • 2
    • 0035061728 scopus 로고    scopus 로고
    • Effects of low temperature, cold shock, and various carbon sources on esterase and lipase activities and exopolysaccharide production by a psychrotrophic Acinetobacter sp
    • Barbaro, S.E., J.T. Trevors, and W.E. Inniss. 2001. Effects of low temperature, cold shock, and various carbon sources on esterase and lipase activities and exopolysaccharide production by a psychrotrophic Acinetobacter sp. Canadian Journal of Microbiology 47: 194-205.
    • (2001) Canadian Journal of Microbiology , vol.47 , pp. 194-205
    • Barbaro, S.E.1    Trevors, J.T.2    Inniss, W.E.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing, the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing, the principle of protein-dye binding. Analytical Biochemistry 72: 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0037046271 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization
    • Brückner, R., and F. Titgemeyer. 2002. Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiology Letters 209: 141-148.
    • (2002) FEMS Microbiology Letters , vol.209 , pp. 141-148
    • Brückner, R.1    Titgemeyer, F.2
  • 8
    • 0033524798 scopus 로고    scopus 로고
    • Effect of oxygen transfer on lipase production by Acinetobacter radioresistens
    • Chen, J., C.Wen, and T. Chen. 1999. Effect of oxygen transfer on lipase production by Acinetobacter radioresistens. Biotechnology and Bioengineering 62: 311-316.
    • (1999) Biotechnology and Bioengineering , vol.62 , pp. 311-316
    • Chen, J.1    Wen, C.2    Chen, T.3
  • 9
    • 0033016742 scopus 로고    scopus 로고
    • Production and characteristics of the lipase from Yarrowia lipolytica 681
    • Corzo, G., and S. Revah. 1999. Production and characteristics of the lipase from Yarrowia lipolytica 681. Bioresource Technology 70: 173-180.
    • (1999) Bioresource Technology , vol.70 , pp. 173-180
    • Corzo, G.1    Revah, S.2
  • 11
    • 42049092081 scopus 로고    scopus 로고
    • The mechanisms of carbon catabolite repression in bacteria
    • Deutscher, J. 2008. The mechanisms of carbon catabolite repression in bacteria. Current Opinion in Microbiology 11: 87-93.
    • (2008) Current Opinion in Microbiology , vol.11 , pp. 87-93
    • Deutscher, J.1
  • 12
    • 0024655878 scopus 로고
    • Enzymatic catalysis in monophasic organic solvents
    • Dordick, J.S. 1989. Enzymatic catalysis in monophasic organic solvents. Enzyme and Microbial Technology 11: 194-211.
    • (1989) Enzyme and Microbial Technology , vol.11 , pp. 194-211
    • Dordick, J.S.1
  • 13
    • 0033753509 scopus 로고    scopus 로고
    • Influence of oxygen transfer on lipase production by Rhizopus arrhizus
    • Elibol, M., and D. Ozer. 2000. Influence of oxygen transfer on lipase production by Rhizopus arrhizus. Process Biochemistry 36: 325-329.
    • (2000) Process Biochemistry , vol.36 , pp. 325-329
    • Elibol, M.1    Ozer, D.2
  • 14
    • 33751535398 scopus 로고    scopus 로고
    • A newly isolated organic solvent tolerant Staphylococcus saprophyticus M36 produced organic solvent-stable lipase
    • Fang, Y., Z. Lu, F. Lv, X. Bie, S. Liu, Z. Ding, and W. Xu. 2006. A newly isolated organic solvent tolerant Staphylococcus saprophyticus M36 produced organic solvent-stable lipase. Current Microbiology 53: 510-515.
    • (2006) Current Microbiology , vol.53 , pp. 510-515
    • Fang, Y.1    Lu, Z.2    Lv, F.3    Bie, X.4    Liu, S.5    Ding, Z.6    Xu, W.7
  • 15
    • 26844486723 scopus 로고    scopus 로고
    • Lipase production by Penicillium restrictum in a bench-scale fermenter: Effect of carbon and nitrogen nutrition, agitation and aeration
    • Freire, D.M.G., E.M.F. Teles, E.P.S. Bon, and G.L. San't Anna Jr. 1997. Lipase production by Penicillium restrictum in a bench-scale fermenter: Effect of carbon and nitrogen nutrition, agitation and aeration. Applied Biochemistry and Biotechnology 63: 409-421.
    • (1997) Applied Biochemistry and Biotechnology , vol.63 , pp. 409-421
    • Freire, D.M.G.1    Teles, E.M.F.2    Bon, E.P.S.3    San't Anna Jr., G.L.4
  • 17
    • 0033813583 scopus 로고    scopus 로고
    • Fermentation and downstream processing on lipase from Aspergillus terreus
    • Gulati, R., R.K. Saxena, and R. Gupta. 2000. Fermentation and downstream processing on lipase from Aspergillus terreus. Process Biochemistry 36: 149-155.
    • (2000) Process Biochemistry , vol.36 , pp. 149-155
    • Gulati, R.1    Saxena, R.K.2    Gupta, R.3
  • 18
    • 3042683021 scopus 로고    scopus 로고
    • Acinetobacter: environmental and biotechnological applications
    • Haleem, D. A. E. 2003. Acinetobacter: environmental and biotechnological applications. African Journal of Biotechnology 2: 71-74.
    • (2003) African Journal of Biotechnology , vol.2 , pp. 71-74
    • Haleem, D.A.E.1
  • 20
    • 0031790622 scopus 로고    scopus 로고
    • Purification and characterization of an alkaline lipase from a newly isolated Acinetobacter radioresistens CMC-1
    • Hong, M., and M. Chang. 1998. Purification and characterization of an alkaline lipase from a newly isolated Acinetobacter radioresistens CMC-1. Biotechnology Letters 20: 1027-1029.
    • (1998) Biotechnology Letters , vol.20 , pp. 1027-1029
    • Hong, M.1    Chang, M.2
  • 21
    • 38249037113 scopus 로고
    • Effect of amino compounds on alkaline amylase production by alkaliphilic Bacillus sp
    • Ikura, Y., and K. Horikoshi. 1987. Effect of amino compounds on alkaline amylase production by alkaliphilic Bacillus sp. Journal of Fermentation Technology 65: 707-709.
    • (1987) Journal of Fermentation Technology , vol.65 , pp. 707-709
    • Ikura, Y.1    Horikoshi, K.2
  • 23
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases from versatile tools for biotechnology
    • Jaeger, K.E., and M.T. Reetz. 1998. Microbial lipases from versatile tools for biotechnology. Trends in Biotechnology 16: 396-403.
    • (1998) Trends in Biotechnology , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 24
    • 0020407541 scopus 로고
    • Exopolysaccharide distribution and bioemusifier production in Acinetobacter BD4 and BD413
    • Kaplan, N., and E. Rosenberg. 1982. Exopolysaccharide distribution and bioemusifier production in Acinetobacter BD4 and BD413. Applied and Environmental Microbiology 44: 1335-1341.
    • (1982) Applied and Environmental Microbiology , vol.44 , pp. 1335-1341
    • Kaplan, N.1    Rosenberg, E.2
  • 25
    • 0024562664 scopus 로고
    • Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102
    • Kimbara, K., T. Hashimoto, M. Fukuda, T. Koana, M. Takagi, M. Oishi, and K. Yano. 1989. Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102. Journal of Bacteriology 171: 2740-2747.
    • (1989) Journal of Bacteriology , vol.171 , pp. 2740-2747
    • Kimbara, K.1    Hashimoto, T.2    Fukuda, M.3    Koana, T.4    Takagi, M.5    Oishi, M.6    Yano, K.7
  • 27
    • 0029815077 scopus 로고    scopus 로고
    • Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: fatty acid repression of lipA expression and degradation of LipA
    • Kok, R.G., C.B. Nudel, R.H. Gonzalez, I.M. Nugteren-Roodzant, and K.J. Hellingwerf. 1996. Physiological factors affecting production of extracellular lipase (LipA) in Acinetobacter calcoaceticus BD413: fatty acid repression of lipA expression and degradation of LipA. Journal of Bacteriology 178: 6025-6035.
    • (1996) Journal of Bacteriology , vol.178 , pp. 6025-6035
    • Kok, R.G.1    Nudel, C.B.2    Gonzalez, R.H.3    Nugteren-Roodzant, I.M.4    Hellingwerf, K.J.5
  • 29
    • 23944433931 scopus 로고    scopus 로고
    • Production of Acinetobacter radioresistens lipase with repeated fed-batch culture
    • Li, C.Y., S.J. Chen, C.Y. Cheng, and T.L. Chen. 2005. Production of Acinetobacter radioresistens lipase with repeated fed-batch culture. Biochemical Engineering Journal 25: 195-199.
    • (2005) Biochemical Engineering Journal , vol.25 , pp. 195-199
    • Li, C.Y.1    Chen, S.J.2    Cheng, C.Y.3    Chen, T.L.4
  • 30
    • 0035152950 scopus 로고    scopus 로고
    • Production of Acinetobacter radioresistens lipase with repeated batch culture in presence of nonwoven fabric
    • Lin, Y., J. Wu, and T. Chen. 2001. Production of Acinetobacter radioresistens lipase with repeated batch culture in presence of nonwoven fabric. Biotechnology and Bioengineering 76: 214-218.
    • (2001) Biotechnology and Bioengineering , vol.76 , pp. 214-218
    • Lin, Y.1    Wu, J.2    Chen, T.3
  • 31
    • 0037318405 scopus 로고    scopus 로고
    • Improvements in lipase production and recovery from Acinetobacter radioresistens in presence of polypropylene powders filled with carbon sources
    • Liu, I.L., and S.W. Tsai. 2003. Improvements in lipase production and recovery from Acinetobacter radioresistens in presence of polypropylene powders filled with carbon sources. Applied Biochemistry and Biotechnology 104: 129-140.
    • (2003) Applied Biochemistry and Biotechnology , vol.104 , pp. 129-140
    • Liu, I.L.1    Tsai, S.W.2
  • 32
    • 14544289163 scopus 로고
    • Physiological and nutritional factors affecting synthesis of extracellular metalloproteinase by Clostridium bifermentans
    • Macfarlane, G.T., and S. Macfarlane. 1992. Physiological and nutritional factors affecting synthesis of extracellular metalloproteinase by Clostridium bifermentans. Applied and Environmental Microbiology 58: 1973-1976.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 1973-1976
    • Macfarlane, G.T.1    Macfarlane, S.2
  • 34
    • 0036954191 scopus 로고    scopus 로고
    • The improvement of lipase secretion and stability by addition of inert compounds into Acinetobacter calcoaceticus cultures
    • Martinez, D.A., and B.C. Nudel. 2002. The improvement of lipase secretion and stability by addition of inert compounds into Acinetobacter calcoaceticus cultures. Canadian Journal of Microbiology 48: 1056-1061.
    • (2002) Canadian Journal of Microbiology , vol.48 , pp. 1056-1061
    • Martinez, D.A.1    Nudel, B.C.2
  • 35
    • 0033080656 scopus 로고    scopus 로고
    • The production of alkaline protease by a Bacillus species isolate
    • Mehrotra, S., P.K. Pandey, R. Gaur, and N.S. Darmwal. 1999. The production of alkaline protease by a Bacillus species isolate. Bioresource Technology 67: 201-203.
    • (1999) Bioresource Technology , vol.67 , pp. 201-203
    • Mehrotra, S.1    Pandey, P.K.2    Gaur, R.3    Darmwal, N.S.4
  • 37
    • 0030152430 scopus 로고    scopus 로고
    • Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: A simple test for the determination of lipase activity in organic media
    • Pencreac'h, G., and J.C. Baratti. 1996. Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: A simple test for the determination of lipase activity in organic media. Enzyme and Microbial Technology 18: 417-422.
    • (1996) Enzyme and Microbial Technology , vol.18 , pp. 417-422
    • Pencreac'h, G.1    Baratti, J.C.2
  • 38
    • 0015400912 scopus 로고
    • Microbial degradation of crude oil: factors affecting the dispersion in sea water by mixed and pure cultures
    • Reisfeld, A., E. Rosenberg, and D. Gutnick. 1972. Microbial degradation of crude oil: factors affecting the dispersion in sea water by mixed and pure cultures. Journal of Applied Microbiology 24: 363-368.
    • (1972) Journal of Applied Microbiology , vol.24 , pp. 363-368
    • Reisfeld, A.1    Rosenberg, E.2    Gutnick, D.3
  • 40
  • 41
    • 0036445837 scopus 로고    scopus 로고
    • Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG-1
    • Snellman, E.A., E.R. Sullivan, and R.R. Colwell. 2002. Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG-1. European Journal of Biochemistry 269: 5771-5779.
    • (2002) European Journal of Biochemistry , vol.269 , pp. 5771-5779
    • Snellman, E.A.1    Sullivan, E.R.2    Colwell, R.R.3
  • 42
    • 10944270620 scopus 로고    scopus 로고
    • Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential
    • Snellman, E.A., and R.R. Colwell. 2004. Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential. Journal of Industrial Microbiology and Biotechnology 31: 391-400.
    • (2004) Journal of Industrial Microbiology and Biotechnology , vol.31 , pp. 391-400
    • Snellman, E.A.1    Colwell, R.R.2
  • 43
    • 0026553652 scopus 로고
    • Regulation of proteolytic activity in the hyperthermophiles Pyrococcus furisosus
    • Snowden, L.Y., I.I. Blumentals, and R.M. Kelly. 1992. Regulation of proteolytic activity in the hyperthermophiles Pyrococcus furisosus. Applied and Environmental Microbiology 58: 1134-1141.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 1134-1141
    • Snowden, L.Y.1    Blumentals, I.I.2    Kelly, R.M.3
  • 44
    • 0342489742 scopus 로고
    • Principles of isolation and conservation of bacteria
    • M. P. Starr, H. Stolp, H. G. Truper, A. Balows, and H. P. Schlegel (eds), Springer-Verlag, Heidelberg
    • Stolp, H., and M. P. Starr. 1981. Principles of isolation and conservation of bacteria, p. 135-175. In M. P. Starr, H. Stolp, H. G. Truper, A. Balows, and H. P. Schlegel (eds) The prokaryotes. Springer-Verlag, Heidelberg.
    • (1981) The prokaryotes , pp. 135-175
    • Stolp, H.1    Starr, M.P.2
  • 46
    • 0026026966 scopus 로고
    • Purification and characterization of a novel thermostable lipase from Bacillus sp
    • Sugihara, A., T. Tani, and Y. Tominaga. 1991. Purification and characterization of a novel thermostable lipase from Bacillus sp. Journal of Biochemistry 109: 211-216.
    • (1991) Journal of Biochemistry , vol.109 , pp. 211-216
    • Sugihara, A.1    Tani, T.2    Tominaga, Y.3
  • 48
    • 77955926979 scopus 로고    scopus 로고
    • Isolation and characterization of a novel thermophilic-organic solvent stable lipase from Acinetobacter baylyi
    • DOI:10.1007/s12010-010-8928-x
    • Uttatree, S., P. Winayanuwattikun, and J. Charoenpanich. 2010. Isolation and characterization of a novel thermophilic-organic solvent stable lipase from Acinetobacter baylyi. Applied Biochemistry and Biotechnology DOI:10.1007/s12010-010-8928-x.
    • (2010) Applied Biochemistry and Biotechnology
    • Uttatree, S.1    Winayanuwattikun, P.2    Charoenpanich, J.3
  • 49
    • 0031720054 scopus 로고    scopus 로고
    • Lipase production by Acinetobacter radioresistens in a batch fill-and-draw culture
    • Wang, T., and T. Chen. 1998. Lipase production by Acinetobacter radioresistens in a batch fill-and-draw culture. Applied Biochemistry and Biotechnology 73: 185-194.
    • (1998) Applied Biochemistry and Biotechnology , vol.73 , pp. 185-194
    • Wang, T.1    Chen, T.2
  • 50
    • 0018399632 scopus 로고
    • Glycogen, hyaluronidate and some other polysaccharides greatly enhance the formation of exocellular lipase by Serratia marcescens
    • Winkler, U.K., and M. Stuckmann. 1979. Glycogen, hyaluronidate and some other polysaccharides greatly enhance the formation of exocellular lipase by Serratia marcescens. Journal of Bacteriology 138: 663-670.
    • (1979) Journal of Bacteriology , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 51
    • 27144480292 scopus 로고    scopus 로고
    • Opportunities for genetic investigation afforded by Acinetobacter baylyi, a nutritionally versatile bacterial species that is highly competent for natural transformation
    • Young, D.M., D. Parke, and L.N. Ornston. 2005. Opportunities for genetic investigation afforded by Acinetobacter baylyi, a nutritionally versatile bacterial species that is highly competent for natural transformation. Annual Review of Microbiology 59: 519-551.
    • (2005) Annual Review of Microbiology , vol.59 , pp. 519-551
    • Young, D.M.1    Parke, D.2    Ornston, L.N.3


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