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Volumn 11, Issue 1, 2014, Pages 119-126

Heterologous expression of thermostable esterase gene from Geobacillus thermoleovorans YN under different expression promoters

Author keywords

BIOFLO III bioreactor; Encoding gene; Escherichia coli; Induction; Six histidines

Indexed keywords

AMINO ACIDS; BIOREACTORS; CLONING; ELECTROPHORESIS; ENCODING (SYMBOLS); ENZYME ACTIVITY; ESCHERICHIA COLI; ESTERS; GENE ENCODING; SIGNAL ENCODING; SULFUR COMPOUNDS;

EID: 84893606133     PISSN: 17351472     EISSN: 17352630     Source Type: Journal    
DOI: 10.1007/s13762-013-0360-7     Document Type: Article
Times cited : (4)

References (31)
  • 1
    • 0000076979 scopus 로고
    • Purification and properties of a thermostable esterase of Bacillus stearothermophilus produced by recombinant Bacillus brevis
    • Amaki Y, Tulin EE, Ueda S, Ohmiya K, Yamane T (1992) Purification and properties of a thermostable esterase of Bacillus stearothermophilus produced by recombinant Bacillus brevis. Biosci Biotechnol Biochem 56(2): 238-241. http://ci. nii. ac. jp/naid/110002680496.
    • (1992) Biosci Biotechnol Biochem , vol.56 , Issue.2 , pp. 238-241
    • Amaki, Y.1    Tulin, E.E.2    Ueda, S.3    Ohmiya, K.4    Yamane, T.5
  • 2
    • 0030824353 scopus 로고    scopus 로고
    • Determination of the kinetic parameters during continuous cultivation of he lipase-producing thermophile Bacillus sp. IHI-91 on olive oil
    • Becker P, Abu-Reesh I, Markossian S, Antranikian G, Markl H (1997) Determination of the kinetic parameters during continuous cultivation of he lipase-producing thermophile Bacillus sp. IHI-91 on olive oil. Appl Microbiol Biotechnol 48: 184-190. www. springerlink. com/index/FWJ6EC1WXW3AQPT2.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 184-190
    • Becker, P.1    Abu-Reesh, I.2    Markossian, S.3    Antranikian, G.4    Markl, H.5
  • 3
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxylesterases: classification, properties and application in biocatalyses
    • Bornscheuer UT (2002) Microbial carboxylesterases: classification, properties and application in biocatalyses. FEMS Microbiol Rev 26: 73-81. http://www. ncbi. nlm. nih. gov/pubmed/12007643.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 4
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution
    • Chung CT, Niemela SL, Miller RH (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86(7): 2172-2175. http://www. ncbi. nlm. nih. gov/pmc/articles/PMC286873/.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.7 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 5
    • 84893581420 scopus 로고
    • Biochemistry and molecular biology of the extremely thermophilic archaeobacteria
    • Cowan DA (1992) Biochemistry and molecular biology of the extremely thermophilic archaeobacteria. Biochem Soc Symp 58: 135-147.
    • (1992) Biochem Soc Symp , vol.58 , pp. 135-147
    • Cowan, D.A.1
  • 6
    • 1642411072 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two thermostable caroxylesterases from Geobacillus stearothermophilus
    • Ewis HE, Abdelal AT, Lu C-D (2004) Molecular cloning and characterization of two thermostable caroxylesterases from Geobacillus stearothermophilus. Gene 329: 187-195. http://www. ncbi. nlm. nih. gov/pubmed/15033540.
    • (2004) Gene , vol.329 , pp. 187-195
    • Ewis, H.E.1    Abdelal, A.T.2    Lu, C.-D.3
  • 7
    • 17644432629 scopus 로고    scopus 로고
    • Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aeropyrum pernix KL
    • abbs. oxfordjournals. org/content/early/2010/03/03/abbs. gmq020. full
    • Gao R, Feng Y, Ishikana K, Ishida H, Ando S, Kosugi Y, Cao S (2003) Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aeropyrum pernix KL. J Mol Catal B 24/25: 1-8. abbs. oxfordjournals. org/content/early/2010/03/03/abbs. gmq020. full.
    • (2003) J Mol Catal B , vol.24-25 , pp. 1-8
    • Gao, R.1    Feng, Y.2    Ishikana, K.3    Ishida, H.4    Ando, S.5    Kosugi, Y.6    Cao, S.7
  • 8
    • 17444408485 scopus 로고    scopus 로고
    • Cloning recombinant expression and biochemical characterization of novel esterases from Bacillus sp. Associated with the marine sponge Aplysina aerophoba
    • Karpushova A, Brummer F, Barth S, Lange S, Schmid RD (2005) Cloning recombinant expression and biochemical characterization of novel esterases from Bacillus sp. Associated with the marine sponge Aplysina aerophoba. Appl Microbiol Biotechnol 67: 59-69. http://www. ncbi. nlm. nih. gov/pubmed/15614567.
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 59-69
    • Karpushova, A.1    Brummer, F.2    Barth, S.3    Lange, S.4    Schmid, R.D.5
  • 9
    • 0000868287 scopus 로고
    • Esterification in organic solvents: selection of hydrolases and effect of reaction conditions
    • Kawamoto T, Sonomoto K, Tanaka A (1987) Esterification in organic solvents: selection of hydrolases and effect of reaction conditions. Biocatalysis 1: 137-145. http://informahealthcare. com/doi/abs/10. 3109/10242428709040138.
    • (1987) Biocatalysis , vol.1 , pp. 137-145
    • Kawamoto, T.1    Sonomoto, K.2    Tanaka, A.3
  • 10
    • 0002452053 scopus 로고    scopus 로고
    • Purification and partial characterization of thermostable carboxylesterase from Bacillus stearothermophilus L1
    • Kim H, Park S, Oh T (1997) Purification and partial characterization of thermostable carboxylesterase from Bacillus stearothermophilus L1. J Microbial Biotechnol 7(1): 37-42. http://agris. fao. org/agris-search/search/display. do?f=1997/KR/KR97018. xml;KR9702599.
    • (1997) J Microbial Biotechnol , vol.7 , Issue.1 , pp. 37-42
    • Kim, H.1    Park, S.2    Oh, T.3
  • 11
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409: 241-246. http://www. nature. com/nature/journal/v409/n6817/abs/409241a0. html.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 12
    • 0032524178 scopus 로고    scopus 로고
    • Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens
    • Krebsfanger N, Zocher F, Altenbuchner J, Bornscheuer UT (1998) Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens. Enzyme Microb Technol 22 (7): 641-646. http://www. fstadirect. com/GetRecord. aspx?AN=1998-09-Bg1214.
    • (1998) Enzyme Microb Technol , vol.22 , Issue.7 , pp. 641-646
    • Krebsfanger, N.1    Zocher, F.2    Altenbuchner, J.3    Bornscheuer, U.T.4
  • 13
    • 0027025870 scopus 로고
    • Molecular cloning and structure of the gene for Esterase from Thermophilic Bacterium Bacillus stearothermophilus IFO 12550
    • Kugimiya W, Otani Y, Hashimoto Y (1992) Molecular cloning and structure of the gene for Esterase from Thermophilic Bacterium Bacillus stearothermophilus IFO 12550. Biosci Biotechnol Biochem 56(12): 2074-2075. http://www. ncbi. nlm. nih. gov/pubmed/1369099.
    • (1992) Biosci Biotechnol Biochem , vol.56 , Issue.12 , pp. 2074-2075
    • Kugimiya, W.1    Otani, Y.2    Hashimoto, Y.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685. http://www. nature. com/nature/journal/v227/n5259/abs/227680a0. html.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0001053705 scopus 로고
    • Rapid method for the quantitative estimation of microbial of microbial lipases
    • Lawrence RC, Fryer TF, Reiter B (1967) Rapid method for the quantitative estimation of microbial of microbial lipases. Nature (London) 213: 1264-1265. http://www. nature. com/nature/journal/v213/n5082/abs/2131264a0. html.
    • (1967) Nature (London) , vol.213 , pp. 1264-1265
    • Lawrence, R.C.1    Fryer, T.F.2    Reiter, B.3
  • 17
    • 77956249127 scopus 로고    scopus 로고
    • Biotransformation of the diphenyl ether herbicide lactofen and purification of a Lactofen Esterase from Brevundimonas sp. LY-2
    • Liang B, Zhao YK, Lu P, Li SP, Huang X (2010) Biotransformation of the diphenyl ether herbicide lactofen and purification of a Lactofen Esterase from Brevundimonas sp. LY-2. J Agric Food Chem 58(17): 9711-9715. http://pubs. acs. org/doi/abs/10. 1021/jf101974y.
    • (2010) J Agric Food Chem , vol.58 , Issue.17 , pp. 9711-9715
    • Liang, B.1    Zhao, Y.K.2    Lu, P.3    Li, S.P.4    Huang, X.5
  • 19
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry OH, Rosebrough NJ, Farr LA, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265-275. http://www. jbc. org/content/193/1/265. full. pdf+html.
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, L.A.3    Randall, R.J.4
  • 20
    • 0000258931 scopus 로고
    • Transduction of lactose utilizing ability among strains of E. coli and S. dysentria and the properties of the transducing phage particle
    • Luria SE, Adams JN, Ting RC (1960) Transduction of lactose utilizing ability among strains of E. coli and S. dysentria and the properties of the transducing phage particle. Virology 12: 390-438.
    • (1960) Virology , vol.12 , pp. 390-438
    • Luria, S.E.1    Adams, J.N.2    Ting, R.C.3
  • 21
    • 65549128344 scopus 로고    scopus 로고
    • Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family
    • Montoro-García S, Martínez-Martínez I, Navarro-Fernández J, Takami H, García-Carmona F, Sánchez-Ferrer A (2009) Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family. J Bacteriol 19(9): 3076-3085. http://www. ncbi. nlm. nih. gov/pubmed/19304850.
    • (2009) J Bacteriol , vol.19 , Issue.9 , pp. 3076-3085
    • Montoro-García, S.1    Martínez-Martínez, I.2    Navarro-Fernández, J.3    Takami, H.4    García-Carmona, F.5    Sánchez-Ferrer, A.6
  • 22
    • 0037160540 scopus 로고    scopus 로고
    • A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene and characterization of the protein
    • Morana A, Prizito ND, Aurilia V, Rossi M, Cannio R (2002) A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene and characterization of the protein. Gene 283(1-2): 107-115. http://www. ncbi. nlm. nih. gov/pubmed/11867217.
    • (2002) Gene , vol.283 , Issue.1-2 , pp. 107-115
    • Morana, A.1    Prizito, N.D.2    Aurilia, V.3    Rossi, M.4    Cannio, R.5
  • 23
    • 0024726863 scopus 로고
    • Correlation between microbial protein thermostability and resistance to denaturation in aqueous: organic solvent two-phase systems
    • Owusu RK, Cowan DA (1989) Correlation between microbial protein thermostability and resistance to denaturation in aqueous: organic solvent two-phase systems. Enzyme Microb Technol 11(9): 568-574. http://eprints. ulster. ac. uk/14682/.
    • (1989) Enzyme Microb Technol , vol.11 , Issue.9 , pp. 568-574
    • Owusu, R.K.1    Cowan, D.A.2
  • 24
    • 17944374832 scopus 로고    scopus 로고
    • Production and applications of esterases
    • Panda T, Gowrishankar BS (2005) Production and applications of esterases. Appl Microbiol Biotechnol 67(2): 160-169. http://www. springerlink. com/content/xvlvclrkey1whq09/.
    • (2005) Appl Microbiol Biotechnol , vol.67 , Issue.2 , pp. 160-169
    • Panda, T.1    Gowrishankar, B.S.2
  • 25
    • 78651487257 scopus 로고    scopus 로고
    • Biodiesel production using solid metal oxide catalysts
    • Refaat AA (2011) Biodiesel production using solid metal oxide catalysts. Int J Environ Sci Tech 8: 203-221. http://www. ijest. org/jufile?c2hvd1BERj00NzI=&ob=09304388b36cb6d488838c7ddc1b0560&fileName=full_text. pdf.
    • (2011) Int J Environ Sci Tech , vol.8 , pp. 203-221
    • Refaat, A.A.1
  • 26
    • 1642325863 scopus 로고    scopus 로고
    • Genome-wide cloning and characterization of microbial esterases
    • Ro HS, Hong HP, Kho BH, Kim S, Chung BH (2004) Genome-wide cloning and characterization of microbial esterases. FEMS Microbiol Lett 233(1): 97-105. http://onlinelibrary. wiley. com/doi/10. 1016/j. femsle. 2004. 01. 046/full.
    • (2004) FEMS Microbiol Lett , vol.233 , Issue.1 , pp. 97-105
    • Ro, H.S.1    Hong, H.P.2    Kho, B.H.3    Kim, S.4    Chung, B.H.5
  • 28
    • 0029899631 scopus 로고    scopus 로고
    • Thermoalkalophilic lipase of Bacillus thermocatenulatus. 1. Molecular cloning, nucleotide sequence, purification and some properties
    • Schmidt-Dannert C, Rua ML, Atomi H, Schmid RD (1996) Thermoalkalophilic lipase of Bacillus thermocatenulatus. 1. Molecular cloning, nucleotide sequence, purification and some properties. Biochim Biophys Acta 1301: 105-114. http://www. ncbi. nlm. nih. gov/pubmed/8652645.
    • (1996) Biochim Biophys Acta , vol.1301 , pp. 105-114
    • Schmidt-Dannert, C.1    Rua, M.L.2    Atomi, H.3    Schmid, R.D.4
  • 29
    • 34347206354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt
    • Soliman NA, Knoll M, Abdel-Fattah YR, Schmid RD, Lange S (2007) Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt. Process Biochem 42(7): 1090-1100. http://cat. inist. fr/?aModele=afficheN&cpsidt=18911423.
    • (2007) Process Biochem , vol.42 , Issue.7 , pp. 1090-1100
    • Soliman, N.A.1    Knoll, M.2    Abdel-Fattah, Y.R.3    Schmid, R.D.4    Lange, S.5
  • 30
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol 185: 60-89. http://www. ncbi. nlm. nih. gov/pubmed/2199796.
    • (1990) Methods Enzymol , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 31
    • 0029073537 scopus 로고
    • Purification and partial characterization of a novel thermophilic carboxyl esterase with high mesophilic specific activity
    • Wood ANP, Femandez-Lafuente R, Cowan DA (1995) Purification and partial characterization of a novel thermophilic carboxyl esterase with high mesophilic specific activity. Enzyme Microbiol Technol 17: 816-825. http://www. ncbi. nlm. nih. gov/pubmed/7576531.
    • (1995) Enzyme Microbiol Technol , vol.17 , pp. 816-825
    • Wood, A.N.P.1    Femandez-Lafuente, R.2    Cowan, D.A.3


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