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Volumn 133, Issue , 2013, Pages 354-360

A thermostable and organic-solvent tolerant esterase from Pseudomonas putida ECU1011: Catalytic properties and performance in kinetic resolution of α-hydroxy acids

Author keywords

Deacetylation; Esterase; Organic solvent tolerance; Thermostability; Hydroxy (carboxylic) acids

Indexed keywords

ACETYLATION; CARBOXYLATION; CARBOXYLIC ACIDS; ENANTIOSELECTIVITY; ESCHERICHIA COLI; ESTERS; ETHERS; PARAFFINS; SOLVENTS;

EID: 84874436738     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2013.01.089     Document Type: Article
Times cited : (47)

References (32)
  • 1
    • 0028889234 scopus 로고
    • Synthesis of chiral α-aryl-α-hydroxyacetic acids: substituent effects in pig-liver acetone powder (PLAP) induced enantioselective hydrolysis
    • Basavaiah D., Krishna P.R. Synthesis of chiral α-aryl-α-hydroxyacetic acids: substituent effects in pig-liver acetone powder (PLAP) induced enantioselective hydrolysis. Tetrahedron 1995, 51:2403-2416.
    • (1995) Tetrahedron , vol.51 , pp. 2403-2416
    • Basavaiah, D.1    Krishna, P.R.2
  • 2
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • Bornscheuer U.T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev. 2002, 26:73-81.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 4
    • 76349104824 scopus 로고    scopus 로고
    • An organic-solvent-tolerant esterase from turkey pharyngeal tissue
    • Cherif S., Gargouri Y. An organic-solvent-tolerant esterase from turkey pharyngeal tissue. Bioresour. Technol. 2010, 101:3732-3736.
    • (2010) Bioresour. Technol. , vol.101 , pp. 3732-3736
    • Cherif, S.1    Gargouri, Y.2
  • 5
    • 67651084048 scopus 로고    scopus 로고
    • Kinetics of enantioselective enzymatic acylation of mandelic acid
    • Dabkowska K., Szewczyk K.W. Kinetics of enantioselective enzymatic acylation of mandelic acid. J. Biotechnol. 2007, 131:S79-S80.
    • (2007) J. Biotechnol. , vol.131
    • Dabkowska, K.1    Szewczyk, K.W.2
  • 7
    • 63649143883 scopus 로고    scopus 로고
    • Production, partial purification and characterization of organic solvent tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis
    • Dandavate V., Jinjala J., Keharia H., Madamwar D. Production, partial purification and characterization of organic solvent tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis. Bioresour. Technol. 2009, 100:3374-3381.
    • (2009) Bioresour. Technol. , vol.100 , pp. 3374-3381
    • Dandavate, V.1    Jinjala, J.2    Keharia, H.3    Madamwar, D.4
  • 9
    • 13644269613 scopus 로고    scopus 로고
    • Optimization of Serratia marcescens lipase production for enantioselective hydrolysis of 3-phenylglycidic acid ester
    • Gao L., Xu J.H., Li X.J., Liu Z.Z. Optimization of Serratia marcescens lipase production for enantioselective hydrolysis of 3-phenylglycidic acid ester. J. Ind. Microbiol. Biotechnol. 2004, 31:525-530.
    • (2004) J. Ind. Microbiol. Biotechnol. , vol.31 , pp. 525-530
    • Gao, L.1    Xu, J.H.2    Li, X.J.3    Liu, Z.Z.4
  • 10
    • 0035501534 scopus 로고    scopus 로고
    • Substrate spectrum of mandelate racemase-Part 1: Variation of the α-hydroxy acid moiety
    • Goriup M., Strauss U.T., Felfer U., Kroutil W., Faber K. Substrate spectrum of mandelate racemase-Part 1: Variation of the α-hydroxy acid moiety. J. Mol. Catal. B Enzym. 2001, 15:207-212.
    • (2001) J. Mol. Catal. B Enzym. , vol.15 , pp. 207-212
    • Goriup, M.1    Strauss, U.T.2    Felfer, U.3    Kroutil, W.4    Faber, K.5
  • 11
    • 0041590743 scopus 로고    scopus 로고
    • Enzymatic routes to enantiomerically pure aromatic alpha-hydroxy carboxylic acids: a further example for the diversity of biocatalysis
    • Groger H. Enzymatic routes to enantiomerically pure aromatic alpha-hydroxy carboxylic acids: a further example for the diversity of biocatalysis. Adv. Synth. Catal. 2001, 343:547-558.
    • (2001) Adv. Synth. Catal. , vol.343 , pp. 547-558
    • Groger, H.1
  • 12
    • 79952047534 scopus 로고    scopus 로고
    • Catalytic enantioselective protonation of α-oxygenated ester enolates prepared through phospha-brook rearrangement
    • Hayashi M., Nakamura S. Catalytic enantioselective protonation of α-oxygenated ester enolates prepared through phospha-brook rearrangement. Angew. Chem. Int. Ed. 2011, 50:2249-2252.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 2249-2252
    • Hayashi, M.1    Nakamura, S.2
  • 13
    • 0036324633 scopus 로고    scopus 로고
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
    • Hotta Y., Ezaki S., Atomi H., Imanaka T. Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon. Appl. Environ. Microbiol. 2002, 68:3925-3931.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3925-3931
    • Hotta, Y.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 14
    • 0024512944 scopus 로고
    • A Pseudomonas thrives in high concentrations of toluene
    • Inoue A., Horikoshi K. A Pseudomonas thrives in high concentrations of toluene. Nature 1989, 338:264-266.
    • (1989) Nature , vol.338 , pp. 264-266
    • Inoue, A.1    Horikoshi, K.2
  • 15
    • 0001290303 scopus 로고
    • Optically-active α-acetoxycarboxylic acids and α-hydroxycarboxylic acids by enzyme-aided syntheses
    • Jeromin G.E., Albertz M. Optically-active α-acetoxycarboxylic acids and α-hydroxycarboxylic acids by enzyme-aided syntheses. J. Prakt. Chem. 1992, 334:526-528.
    • (1992) J. Prakt. Chem. , vol.334 , pp. 526-528
    • Jeromin, G.E.1    Albertz, M.2
  • 16
    • 84861678826 scopus 로고    scopus 로고
    • Overexpression and characterization of a new organic solvent-tolerant esterase derived from soil metagenomic DNA
    • Jin P., Pei X., Du P., Yin X., Xiong X., Wu H., Zhou X., Wang Q. Overexpression and characterization of a new organic solvent-tolerant esterase derived from soil metagenomic DNA. Bioresour. Technol. 2012, 116:234-240.
    • (2012) Bioresour. Technol. , vol.116 , pp. 234-240
    • Jin, P.1    Pei, X.2    Du, P.3    Yin, X.4    Xiong, X.5    Wu, H.6    Zhou, X.7    Wang, Q.8
  • 17
    • 80053604318 scopus 로고    scopus 로고
    • Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids
    • Ju X., Pan J., Yu H.L., Li C.X., Xu J.H. Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids. Biochem. Eng. J. 2011, 57:63-68.
    • (2011) Biochem. Eng. J. , vol.57 , pp. 63-68
    • Ju, X.1    Pan, J.2    Yu, H.L.3    Li, C.X.4    Xu, J.H.5
  • 18
    • 77149162001 scopus 로고    scopus 로고
    • Bioproduction of chiral mandelate by enantioselective deacylation of α-acetoxyphenylacetic acid using whole cells of newly isolated Pseudomonas sp. ECU1011
    • Ju X., Yu H.L., Pan J., Wei D.Z., Xu J.H. Bioproduction of chiral mandelate by enantioselective deacylation of α-acetoxyphenylacetic acid using whole cells of newly isolated Pseudomonas sp. ECU1011. Appl. Microbiol. Biotechnol. 2010, 86:83-91.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 83-91
    • Ju, X.1    Yu, H.L.2    Pan, J.3    Wei, D.Z.4    Xu, J.H.5
  • 19
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • Laane C., Boeren S., Vos K., Veeger C. Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 1987, 30:81-87.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 20
    • 32844456411 scopus 로고    scopus 로고
    • Enantio-complementary deracemization of (±)-2-hydroxy-4-phenylbutanoic acid and (±)-3-phenyllactic acid using lipase-catalyzed kinetic resolution combined with biocatalytic racemization
    • Larissegger-Schnell B., Glueck S.M., Kroutil W., Faber K. Enantio-complementary deracemization of (±)-2-hydroxy-4-phenylbutanoic acid and (±)-3-phenyllactic acid using lipase-catalyzed kinetic resolution combined with biocatalytic racemization. Tetrahedron 2006, 62:2912-2916.
    • (2006) Tetrahedron , vol.62 , pp. 2912-2916
    • Larissegger-Schnell, B.1    Glueck, S.M.2    Kroutil, W.3    Faber, K.4
  • 21
    • 0032524806 scopus 로고    scopus 로고
    • Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily
    • Manco G., Adinolfi E., Pisani F.M., Ottolina G., Carrea G., Rossi M. Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily. Biochem. J. 1998, 332:203-212.
    • (1998) Biochem. J. , vol.332 , pp. 203-212
    • Manco, G.1    Adinolfi, E.2    Pisani, F.M.3    Ottolina, G.4    Carrea, G.5    Rossi, M.6
  • 23
    • 0033917914 scopus 로고    scopus 로고
    • Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03
    • Ogino H., Nakagawa S., Shinya K., Muto T., Fujimura N., Yasuda M., Ishikawa H. Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03. J. Biosci. Bioeng. 2000, 89:451-457.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 451-457
    • Ogino, H.1    Nakagawa, S.2    Shinya, K.3    Muto, T.4    Fujimura, N.5    Yasuda, M.6    Ishikawa, H.7
  • 24
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • Reetz M.T. Lipases as practical biocatalysts. Curr. Opin. Chem. Biol. 2002, 6:145-150.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 145-150
    • Reetz, M.T.1
  • 25
    • 13544253396 scopus 로고    scopus 로고
    • New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library
    • Rhee J.K., Ahn D.G., Kim Y.G., Oh J.W. New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library. Appl. Environ. Microbiol. 2005, 71:817-825.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 817-825
    • Rhee, J.K.1    Ahn, D.G.2    Kim, Y.G.3    Oh, J.W.4
  • 26
    • 79959849303 scopus 로고    scopus 로고
    • Acylation of Meldrum's acid with arylacetic acid imidazolides as a convenient method for the synthesis of 4-aryl-3-oxobutanoates
    • Shimkin A.A., Shirinian V.Z., Mailian A.K., Lonshakov D.V., Gorokhov V.V., Krayushkin M.M. Acylation of Meldrum's acid with arylacetic acid imidazolides as a convenient method for the synthesis of 4-aryl-3-oxobutanoates. Russ. Chem. B 2011, 60:139-142.
    • (2011) Russ. Chem. B , vol.60 , pp. 139-142
    • Shimkin, A.A.1    Shirinian, V.Z.2    Mailian, A.K.3    Lonshakov, D.V.4    Gorokhov, V.V.5    Krayushkin, M.M.6
  • 27
    • 84859926383 scopus 로고    scopus 로고
    • Kinetic investigation of a solvent-free, chemoenzymatic reaction sequence towards enantioselective synthesis of a β-amino acid ester
    • Strompen S., Weiß M., Ingram T., Smirnova I., Gröger H., Hilterhaus L., Liese A. Kinetic investigation of a solvent-free, chemoenzymatic reaction sequence towards enantioselective synthesis of a β-amino acid ester. Biotechnol. Bioeng. 2012, 109:1479-1489.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1479-1489
    • Strompen, S.1    Weiß, M.2    Ingram, T.3    Smirnova, I.4    Gröger, H.5    Hilterhaus, L.6    Liese, A.7
  • 28
    • 0037181347 scopus 로고    scopus 로고
    • Dynamic kinetic resolution via dual-function catalysis of modified cinchona alkaloids: asymmetric synthesis of α-hydroxy carboxylic acids
    • Tang L., Deng L. Dynamic kinetic resolution via dual-function catalysis of modified cinchona alkaloids: asymmetric synthesis of α-hydroxy carboxylic acids. J. Am. Chem. Soc. 2002, 124:2870-2871.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2870-2871
    • Tang, L.1    Deng, L.2
  • 29
    • 78049372365 scopus 로고    scopus 로고
    • Escherichia coli BioH: a highly enantioselective and organic solvent tolerant esterase for kinetic resolution of sec-alcohols
    • Wang B., Tang X., Liu J., Yu H. Escherichia coli BioH: a highly enantioselective and organic solvent tolerant esterase for kinetic resolution of sec-alcohols. Tetrahedron Lett. 2010, 51:6360-6364.
    • (2010) Tetrahedron Lett. , vol.51 , pp. 6360-6364
    • Wang, B.1    Tang, X.2    Liu, J.3    Yu, H.4
  • 30
    • 79957851192 scopus 로고    scopus 로고
    • Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor
    • Wang L.J., Li C.X., Ni Y., Zhang J., Liu X., Xu J.H. Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor. Bioresour. Technol. 2011, 102:7023-7028.
    • (2011) Bioresour. Technol. , vol.102 , pp. 7023-7028
    • Wang, L.J.1    Li, C.X.2    Ni, Y.3    Zhang, J.4    Liu, X.5    Xu, J.H.6
  • 31
    • 2342489872 scopus 로고    scopus 로고
    • Enzyme-catalysed optical resolution of mandelic acid via RS (±)-methyl mandelate in non-aqueous media
    • Yadav G.D., Sivakumar P. Enzyme-catalysed optical resolution of mandelic acid via RS (±)-methyl mandelate in non-aqueous media. Biochem. Eng. J. 2004, 19:101-107.
    • (2004) Biochem. Eng. J. , vol.19 , pp. 101-107
    • Yadav, G.D.1    Sivakumar, P.2
  • 32
    • 84862820358 scopus 로고    scopus 로고
    • Efficient production of (R)-o-chloromandelic acid by deracemization of o-chloromandelonitrile with a new nitrilase mined from Labrenzia aggregata
    • Zhang C.S., Zhang Z.J., Li C.X., Yu H.L., Zheng G.W., Xu J.H. Efficient production of (R)-o-chloromandelic acid by deracemization of o-chloromandelonitrile with a new nitrilase mined from Labrenzia aggregata. Appl. Microbiol. Biotechnol. 2012, 95:91-99.
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , pp. 91-99
    • Zhang, C.S.1    Zhang, Z.J.2    Li, C.X.3    Yu, H.L.4    Zheng, G.W.5    Xu, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.