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Volumn 38, Issue 1-2, 2006, Pages 199-208

Acyl transfer strategy for the biocatalytical characterisation of Candida rugosa lipases in organic solvents

Author keywords

Acyl transfer; Candida rugosa lipases; Catalytic performance; Isoenzymes; Organic solvents

Indexed keywords

ALCOHOLS; BIOSYNTHESIS; ENZYME KINETICS; ESTERIFICATION; ORGANIC SOLVENTS; YEAST;

EID: 27844564844     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.06.001     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0032530679 scopus 로고    scopus 로고
    • Candida rugosa lipases: Molecular biology and versatility in biotechnology
    • S. Benjamin, and A. Pandey Candida rugosa lipases: molecular biology and versatility in biotechnology Yeast 14 1998 1069 1197
    • (1998) Yeast , vol.14 , pp. 1069-1197
    • Benjamin, S.1    Pandey, A.2
  • 2
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • R.D. Schmidt, and R. Verger Lipases: interfacial enzymes with attractive applications Angew Chem, Int Ed 37 1998 1609
    • (1998) Angew Chem, Int Ed , vol.37 , pp. 1609
    • Schmidt, R.D.1    Verger, R.2
  • 5
    • 0032825993 scopus 로고    scopus 로고
    • Non-conventional hydrolase chemistry: Amide and carbamate bond formation catalysed by lipases
    • V. Gotor Non-conventional hydrolase chemistry: amide and carbamate bond formation catalysed by lipases Bioorg Med Chem 7 1999 2189
    • (1999) Bioorg Med Chem , vol.7 , pp. 2189
    • Gotor, V.1
  • 6
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • G. Carrea, and S. Riva Properties and synthetic applications of enzymes in organic solvents Angew Chem, Int Ed 39 2000 2226
    • (2000) Angew Chem, Int Ed , vol.39 , pp. 2226
    • Carrea, G.1    Riva, S.2
  • 8
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterisation, and applications of lipases
    • R. Sharma, Y. Chisti, and U.C. Banerjee Production, purification, characterisation, and applications of lipases Biotechnol Adv 19 2001 627
    • (2001) Biotechnol Adv , vol.19 , pp. 627
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 9
    • 0033538660 scopus 로고    scopus 로고
    • Causes of unreproducibility of C. rugosa lipase-catalysed reactions in slightly hydrated organic media
    • P. Domínguez de María, and J.V. Sinisterra Causes of unreproducibility of C. rugosa lipase-catalysed reactions in slightly hydrated organic media Tetrahedron 55 1999 8555 8566
    • (1999) Tetrahedron , vol.55 , pp. 8555-8566
    • Domínguez De María, P.1    Sinisterra, J.V.2
  • 11
    • 0004020909 scopus 로고
    • Enantioselective cleavage of meso-nitrodiol diacetates by an esterase concentrate from fresh pig liver: Preparation of useful nitroaliphatic building blocks for EPC syntheses
    • D. Seebach, and M. Eberle Enantioselective cleavage of meso-nitrodiol diacetates by an esterase concentrate from fresh pig liver: preparation of useful nitroaliphatic building blocks for EPC syntheses Chimia 40 1986 315
    • (1986) Chimia , vol.40 , pp. 315
    • Seebach, D.1    Eberle, M.2
  • 12
    • 0036903280 scopus 로고    scopus 로고
    • Methods to increase enantioselectivity of lipases and esterases
    • U.T. Bornscheuer Methods to increase enantioselectivity of lipases and esterases Curr Opin Biotech 13 2002 543
    • (2002) Curr Opin Biotech , vol.13 , pp. 543
    • Bornscheuer, U.T.1
  • 13
    • 0002425020 scopus 로고
    • Multiple forms and functions of Candida rugosa lipase
    • R.C. Chang, S.J. Chou, and J.F. Shaw Multiple forms and functions of Candida rugosa lipase Biotechnol Appl Biochem 19 1994 93 97
    • (1994) Biotechnol Appl Biochem , vol.19 , pp. 93-97
    • Chang, R.C.1    Chou, S.J.2    Shaw, J.F.3
  • 15
    • 0024727394 scopus 로고
    • Rhizomucor miehei triglyceride lipase is processed and secreted from transformed Aspergillus oryza
    • B. Huge-Jensen, F. Andreasen, T. Christensen, M. Christensen, L. Thim, and E. Boel Rhizomucor miehei triglyceride lipase is processed and secreted from transformed Aspergillus oryza Lipids 24 1989 781
    • (1989) Lipids , vol.24 , pp. 781
    • Huge-Jensen, B.1    Andreasen, F.2    Christensen, T.3    Christensen, M.4    Thim, L.5    Boel, E.6
  • 16
    • 0029123341 scopus 로고
    • Stereoselective production of (+) trans-chrysanthemic acid by a microbial esterase: Cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli
    • M. Nishizawa, M. Shimizu, H. Ohkawa, and M. Kanaoka Stereoselective production of (+) trans-chrysanthemic acid by a microbial esterase: cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli Appl Environ Microbiol 61 1995 3208
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3208
    • Nishizawa, M.1    Shimizu, M.2    Ohkawa, H.3    Kanaoka, M.4
  • 17
    • 0030801251 scopus 로고    scopus 로고
    • Overexpression of lipase a and B of Geotrichum candidum in Pichia pastoris: High-level production and some properties of functional expressed lipase B
    • E. Catoni, C. Schmidt-Dannert, S. Brocca, and R.D. Schmid Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: high-level production and some properties of functional expressed lipase B Biotechnol Tech 11 1997 689
    • (1997) Biotechnol Tech , vol.11 , pp. 689
    • Catoni, E.1    Schmidt-Dannert, C.2    Brocca, S.3    Schmid, R.D.4
  • 18
    • 0000646394 scopus 로고    scopus 로고
    • Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens towards alcohols and carboxylic acids
    • N. Krebsfanger, K. Schierholz, and U.T. Bornscheuer Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens towards alcohols and carboxylic acids J Bioetchnol 5 1998 105
    • (1998) J Bioetchnol , vol.5 , pp. 105
    • Krebsfanger, N.1    Schierholz, K.2    Bornscheuer, U.T.3
  • 19
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence and biochemical characterisation of an esterase from Pseudomonas fuorescens with high activity toward lactones
    • V. Khalameyzer, I. Fischer, U.T. Bornscheuer, and J. Altenbuchner Screening, nucleotide sequence and biochemical characterisation of an esterase from Pseudomonas fuorescens with high activity toward lactones Appl Environ Microbiol 65 1999 477
    • (1999) Appl Environ Microbiol , vol.65 , pp. 477
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 20
    • 0000934321 scopus 로고    scopus 로고
    • High-level formation of active Pseudomonas cepacia lipase after heterologous expression of its gene and its modified chaperone in E. coli and rapid in vitro refolding
    • D.T. Quyen, C. Schmidt-Dannert, and R.D. Schmid High-level formation of active Pseudomonas cepacia lipase after heterologous expression of its gene and its modified chaperone in E. coli and rapid in vitro refolding Appl Environ Microbiol 65 1999 787
    • (1999) Appl Environ Microbiol , vol.65 , pp. 787
    • Quyen, D.T.1    Schmidt-Dannert, C.2    Schmid, R.D.3
  • 21
    • 0032955788 scopus 로고    scopus 로고
    • Overexpression and characterisation of an esterase from Streptomyces diastatochromogenes
    • V. Khalameyzer, and U.T. Bornscheuer Overexpression and characterisation of an esterase from Streptomyces diastatochromogenes Biotechnol Lett 21 1999 101
    • (1999) Biotechnol Lett , vol.21 , pp. 101
    • Khalameyzer, V.1    Bornscheuer, U.T.2
  • 22
    • 0035800379 scopus 로고    scopus 로고
    • By overexpression in the yeast pichia pastoris to enhanced enantioselectivity: New aspects in the application of pig liver esterase
    • A. Musidlowska, S. Lange, and U.T. Bornscheuer By overexpression in the yeast pichia pastoris to enhanced enantioselectivity: new aspects in the application of pig liver esterase Angew Chem Int Ed 40 2001 2851
    • (2001) Angew Chem Int Ed , vol.40 , pp. 2851
    • Musidlowska, A.1    Lange, S.2    Bornscheuer, U.T.3
  • 23
    • 0036714663 scopus 로고    scopus 로고
    • Multiple mutagenesis of non-universal serine codons of the Candida rugosa LIP2 gene and biochemical characterisation of purified recombinant LIP2 lipase overexpressed in Pichia pastoris
    • G.Ch. Lee, L.Ch. Lee, V. Sava, and J.F. Shaw Multiple mutagenesis of non-universal serine codons of the Candida rugosa LIP2 gene and biochemical characterisation of purified recombinant LIP2 lipase overexpressed in Pichia pastoris Biochem J 366 2002 603
    • (2002) Biochem J , vol.366 , pp. 603
    • Lee, G.Ch.1    Lee, L.Ch.2    Sava, V.3    Shaw, J.F.4
  • 24
    • 0038448247 scopus 로고    scopus 로고
    • Site directed mutagenesis of recombinant pig liver esterase yields mutants with altered enantioselectivity
    • A. Musidlowska-Persson, and U.T. Bornscheuer Site directed mutagenesis of recombinant pig liver esterase yields mutants with altered enantioselectivity Tetrahedron: Asymmetry 14 2003 1341
    • (2003) Tetrahedron: Asymmetry , vol.14 , pp. 1341
    • Musidlowska-Persson, A.1    Bornscheuer, U.T.2
  • 26
    • 0032552811 scopus 로고    scopus 로고
    • Enhancement of Candida rugosa lipase production by using different control fed-batch operational strategies
    • M.A. Gordillo, A. Sanz, A. Sánchez, F. Valero, J.L. Lafuente, and C. Solá Enhancement of Candida rugosa lipase production by using different control fed-batch operational strategies Biotechnol Bioeng 60 1998 156
    • (1998) Biotechnol Bioeng , vol.60 , pp. 156
    • Gordillo, M.A.1    Sanz, A.2    Sánchez, A.3    Valero, F.4    Lafuente, J.L.5    Solá, C.6
  • 27
    • 0345425821 scopus 로고    scopus 로고
    • Characterisation of the lipase and esterase multiple forms in an enzyme preparation from a Candida rugosa pilot-plant scale fed-batch fermentation
    • A. Sánchez, P. Ferrer, A. Serrano, M.A. Pernas, F. Valero, and M.L. Rúa Characterisation of the lipase and esterase multiple forms in an enzyme preparation from a Candida rugosa pilot-plant scale fed-batch fermentation Enz Microb Technol 25 1999 214 223
    • (1999) Enz Microb Technol , vol.25 , pp. 214-223
    • Sánchez, A.1    Ferrer, P.2    Serrano, A.3    Pernas, M.A.4    Valero, F.5    Rúa, M.L.6
  • 29
    • 27844474625 scopus 로고    scopus 로고
    • Ph.D. Thesis. Universidad Complutense de Madrid
    • Domínguez de María P. Ph.D. Thesis. Universidad Complutense de Madrid, 2002.
    • (2002)
    • Domínguez De María, P.1
  • 30
    • 0002307655 scopus 로고
    • Enantiotopic selectivity of pig liver esterase isoenzymes
    • K. Öhrner, A. Mattson, T. Norin, and K. Hult Enantiotopic selectivity of pig liver esterase isoenzymes Biocatalysis 4 1990 81
    • (1990) Biocatalysis , vol.4 , pp. 81
    • Öhrner, K.1    Mattson, A.2    Norin, T.3    Hult, K.4
  • 31
    • 0029141885 scopus 로고
    • Hydrolysis of (R,S)-2-aryl propionic esters by pure lipase B from Candida cylindracea
    • M.J. Hernáiz, J.M. Sánchez-Montero, and J.V. Sinisterra Hydrolysis of (R,S)-2-aryl propionic esters by pure lipase B from Candida cylindracea J Mol Catal A: Chem 96 1995 317 327
    • (1995) J Mol Catal A: Chem , vol.96 , pp. 317-327
    • Hernáiz, M.J.1    Sánchez-Montero, J.M.2    Sinisterra, J.V.3
  • 33
    • 0031447887 scopus 로고    scopus 로고
    • Kinetic and enantioselective behaviour of isoenzymes a and B from Candida rugosa lipase in the hydrolysis of lipids and esters
    • F.J. Plou, P. Sogo, M.V. Calvo, F.J. Burguillo, and A. Ballesteros Kinetic and enantioselective behaviour of isoenzymes A and B from Candida rugosa lipase in the hydrolysis of lipids and esters Biocatal Biotrans 15 1997 75 89
    • (1997) Biocatal Biotrans , vol.15 , pp. 75-89
    • Plou, F.J.1    Sogo, P.2    Calvo, M.V.3    Burguillo, F.J.4    Ballesteros, A.5
  • 34
    • 0342617775 scopus 로고    scopus 로고
    • Molecular reasons for lipase-sensitivity against acetaldehyde
    • H.K. Weber, J. Zuegg, K. Faber, and J. Pleiss Molecular reasons for lipase-sensitivity against acetaldehyde J Mol Catal B: Enz 3 1997 131 138
    • (1997) J Mol Catal B: Enz , vol.3 , pp. 131-138
    • Weber, H.K.1    Zuegg, J.2    Faber, K.3    Pleiss, J.4
  • 35
    • 0025202709 scopus 로고
    • Reaction scheme of lipase production by Candida rugosa growing on olive oil
    • J.L. del Río, P. Serra, F. Valero, M. Poch, and C. Solá Reaction scheme of lipase production by Candida rugosa growing on olive oil Biotechnol Lett 12 1990 835 838
    • (1990) Biotechnol Lett , vol.12 , pp. 835-838
    • Del Río, J.L.1    Serra, P.2    Valero, F.3    Poch, M.4    Solá, C.5
  • 36
    • 0345593696 scopus 로고    scopus 로고
    • A controlled fed-batch cultivation for the production of new crude lipases from Candida rugosa with improved properties in fine chemistry
    • A. Sánchez, P. Ferrer, A. Serrano, F. Valero, C. Solá, and M. Pernas A controlled fed-batch cultivation for the production of new crude lipases from Candida rugosa with improved properties in fine chemistry J Biotechnol 69 1999 169 182
    • (1999) J Biotechnol , vol.69 , pp. 169-182
    • Sánchez, A.1    Ferrer, P.2    Serrano, A.3    Valero, F.4    Solá, C.5    Pernas, M.6
  • 37
    • 0031777548 scopus 로고    scopus 로고
    • Design, total synthesis and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase
    • S. Brocca, C. Schmidt-Dannert, M. Lotti, L. Alberghina, and R.D. Schmid Design, total synthesis and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase Protein Sci 7 1998 1415 1422
    • (1998) Protein Sci , vol.7 , pp. 1415-1422
    • Brocca, S.1    Schmidt-Dannert, C.2    Lotti, M.3    Alberghina, L.4    Schmid, R.D.5
  • 38
    • 27844561427 scopus 로고    scopus 로고
    • Enzymatic amidation and alkoxycarbonylation of amines using native and immobilised lipases with different origins: A comparative study
    • M.S. de Castro, P. Domínguez de María, and J.V. Sinisterra Enzymatic amidation and alkoxycarbonylation of amines using native and immobilised lipases with different origins: a comparative study Tetrahedron 54 1998 1387 1391
    • (1998) Tetrahedron , vol.54 , pp. 1387-1391
    • De Castro, M.S.1    Domínguez De María, P.2    Sinisterra, J.V.3
  • 39
    • 0032863698 scopus 로고    scopus 로고
    • Analysis of the gene family encoding lipases in Candida rugosa by competitive reverse transcription-PCR
    • G.C. Lee, S.J. Tang, K.H. Sung, and F. Shaw Analysis of the gene family encoding lipases in Candida rugosa by competitive reverse transcription-PCR Appl Environ Microbiol 65 1999 3888 3895
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3888-3895
    • Lee, G.C.1    Tang, S.J.2    Sung, K.H.3    Shaw, F.4
  • 40
    • 0029087514 scopus 로고
    • Enzyme catalysed irreversible transesterifications with vinyl acetate. Are they really irreversible?
    • M. Lundh, O. Nordin, E. Hedenström, and H.E. Högberg Enzyme catalysed irreversible transesterifications with vinyl acetate. Are they really irreversible? Tetrahedron: Asymmetry 6 1995 2237
    • (1995) Tetrahedron: Asymmetry , vol.6 , pp. 2237
    • Lundh, M.1    Nordin, O.2    Hedenström, E.3    Högberg, H.E.4
  • 41
    • 0026483924 scopus 로고
    • Lipase-mediated alkoxycarbonylation of nucleosides with oxime carbonates
    • F. Morís, and V. Gotor Lipase-mediated alkoxycarbonylation of nucleosides with oxime carbonates Tetrahedron 48 1992 9869 9876
    • (1992) Tetrahedron , vol.48 , pp. 9869-9876
    • Morís, F.1    Gotor, V.2
  • 42
    • 0029644244 scopus 로고
    • Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase
    • D. Ghosh, Z. Wawrzak, V.Z. Pletnev, N. Li, R. Kaiser, and W. Pangborn Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase Structure 3 1995 279 288
    • (1995) Structure , vol.3 , pp. 279-288
    • Ghosh, D.1    Wawrzak, Z.2    Pletnev, V.Z.3    Li, N.4    Kaiser, R.5    Pangborn, W.6
  • 43
    • 0037237565 scopus 로고    scopus 로고
    • Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 Å resolution
    • V. Pletnev, A. Addlagatta, Z. Wawrzak, and W. Duax Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 Å resolution Acta Cryst D 59 2003 50
    • (2003) Acta Cryst D , vol.59 , pp. 50
    • Pletnev, V.1    Addlagatta, A.2    Wawrzak, Z.3    Duax, W.4
  • 44
    • 0037193187 scopus 로고    scopus 로고
    • Inhibition of yeast lipase (CRL1) and cholesterol esterase (CRL3) by 6-chloro-2-pyrones: Comparison with porcine cholesterol esterase
    • M. Stoddard Hatch, W.M. Brown, J.A. Deck, L.A. Hunsaker, J.M. Deck, and D.L. Vander Jagt Inhibition of yeast lipase (CRL1) and cholesterol esterase (CRL3) by 6-chloro-2-pyrones: comparison with porcine cholesterol esterase Biochim Biophys Acta 1596 2002 381 391
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 381-391
    • Stoddard Hatch, M.1    Brown, W.M.2    Deck, J.A.3    Hunsaker, L.A.4    Deck, J.M.5    Vander Jagt, D.L.6
  • 45
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalysed by cholesterol esterase, lipase from Pseudomonas cepacia and lipase from Candida rugosa
    • R.J. Kazlauskas, A.N.E. Weissfloch, A.T. Rappaport, and L.A. Ciuccia A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalysed by cholesterol esterase, lipase from Pseudomonas cepacia and lipase from Candida rugosa J Org Chem 56 1991 2656 2665
    • (1991) J Org Chem , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Ciuccia, L.A.4
  • 46
    • 0032007895 scopus 로고    scopus 로고
    • Enantioselectivity of Pseudomonas cepacia and Candida rugosa lipases for the resolution of secondary alcohols: The effect of Candida rugosa isoenzymes
    • K. Lundell, T. Raijola, and L.T. Kanerva Enantioselectivity of Pseudomonas cepacia and Candida rugosa lipases for the resolution of secondary alcohols: the effect of Candida rugosa isoenzymes Enz Microb Technol 22 1998 86 93
    • (1998) Enz Microb Technol , vol.22 , pp. 86-93
    • Lundell, K.1    Raijola, T.2    Kanerva, L.T.3


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