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Volumn 57, Issue 1, 2011, Pages 63-68

Improving Pseudomonas sp. esterase performance by engineering approaches for kinetic resolution of 2-acetoxyphenylacetic acids

Author keywords

Biocatalysis; Bioprocess design; Enantioseparation; Immobilized cells; Mandelic acid; O Chloromandelic acid; Pseudomonas sp. Esterase

Indexed keywords

BIOCATALYSIS; BIOPROCESS DESIGN; ENANTIOSEPARATIONS; IMMOBILIZED CELLS; MANDELIC ACID; PSEUDOMONAS SP;

EID: 80053604318     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2011.08.009     Document Type: Article
Times cited : (4)

References (29)
  • 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
  • 3
    • 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. 2009, 86:83-91.
    • (2009) 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
  • 5
    • 77956174740 scopus 로고    scopus 로고
    • Single enantiomeric β-blockers-the existing technologies
    • Agustian J., Kamaruddin A.H., Bhatia S. Single enantiomeric β-blockers-the existing technologies. Process Biochem. 2010, 45:1587-1604.
    • (2010) Process Biochem. , vol.45 , pp. 1587-1604
    • Agustian, J.1    Kamaruddin, A.H.2    Bhatia, S.3
  • 6
    • 0041402634 scopus 로고    scopus 로고
    • Dynamic kinetic resolution of α-hydroxy acid esters
    • Huerta F.F., Laxmi Y.R.S., Backvall J.E. Dynamic kinetic resolution of α-hydroxy acid esters. Org. Lett. 2000, 2:1037-1040.
    • (2000) Org. Lett. , vol.2 , pp. 1037-1040
    • Huerta, F.F.1    Laxmi, Y.R.S.2    Backvall, J.E.3
  • 7
    • 53549133970 scopus 로고    scopus 로고
    • Improvements of enzyme activity and enantioselectivity via combined substrate engineering and covalent immobilization
    • Wang P.Y., Tsai S.W., Chen T.L. Improvements of enzyme activity and enantioselectivity via combined substrate engineering and covalent immobilization. Biotechnol. Bioeng. 2008, 101:460-469.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 460-469
    • Wang, P.Y.1    Tsai, S.W.2    Chen, T.L.3
  • 8
    • 77952334011 scopus 로고    scopus 로고
    • Intensification and economic and ecological assessment of a biocatalytic oxyfunctionalization process
    • Kuhn D., Kholiq M.A., Heinzle E., Buhler B., Schmid A. Intensification and economic and ecological assessment of a biocatalytic oxyfunctionalization process. Green Chem. 2010, 12:815-827.
    • (2010) Green Chem. , vol.12 , pp. 815-827
    • Kuhn, D.1    Kholiq, M.A.2    Heinzle, E.3    Buhler, B.4    Schmid, A.5
  • 9
    • 55549108089 scopus 로고    scopus 로고
    • Engineered enzymes for chemical production
    • Luetz S., Giver L., Lalonde J. Engineered enzymes for chemical production. Biotechnol. Bioeng. 2008, 101:647-653.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 647-653
    • Luetz, S.1    Giver, L.2    Lalonde, J.3
  • 10
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilization
    • Brady D., Jordaan J. Advances in enzyme immobilization. Biotechnol. Lett. 2009, 31:1639-1650.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 11
    • 77953604136 scopus 로고    scopus 로고
    • Efficient production of diltiazem chiral intermediate using immobilized lipase from Serratia marcescens
    • Zhao L.L., Pan J., Xu J.H. Efficient production of diltiazem chiral intermediate using immobilized lipase from Serratia marcescens. Biotechnol. Bioprocess Eng. 2010, 15:199-207.
    • (2010) Biotechnol. Bioprocess Eng. , vol.15 , pp. 199-207
    • Zhao, L.L.1    Pan, J.2    Xu, J.H.3
  • 12
    • 68649126067 scopus 로고    scopus 로고
    • Calcium alginate-starch hybrid support for both surface immobilization and entrapment of bitter gourd (Momordica charantia) peroxidase
    • Matto M., Husain Q. Calcium alginate-starch hybrid support for both surface immobilization and entrapment of bitter gourd (Momordica charantia) peroxidase. J. Mol. Catal. B: Enzym. 2009, 57:164-170.
    • (2009) J. Mol. Catal. B: Enzym. , vol.57 , pp. 164-170
    • Matto, M.1    Husain, Q.2
  • 13
    • 67650257448 scopus 로고    scopus 로고
    • Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repetitive use in enzymatic synthesis of diltiazem intermediate
    • Hu B., Pan J., Yu H.L., Liu J.W., Xu J.H. Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repetitive use in enzymatic synthesis of diltiazem intermediate. Process Biochem. 2009, 44:1019-1024.
    • (2009) Process Biochem. , vol.44 , pp. 1019-1024
    • Hu, B.1    Pan, J.2    Yu, H.L.3    Liu, J.W.4    Xu, J.H.5
  • 14
    • 33745950323 scopus 로고    scopus 로고
    • Preparation and characterization of Pseudomonas putida esterase immobilized on magnetic nanoparticles
    • Shaw S.Y., Chen Y.J., Ou J.J., Ho L. Preparation and characterization of Pseudomonas putida esterase immobilized on magnetic nanoparticles. Enzyme Microb. Technol. 2006, 39:1089-1095.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 1089-1095
    • Shaw, S.Y.1    Chen, Y.J.2    Ou, J.J.3    Ho, L.4
  • 15
    • 70449644366 scopus 로고    scopus 로고
    • Optimization and evaluation of acetylcholine esterase immobilization on ceramic packing using response surface methodology
    • Ebrahimi B., Shojaosadati S.A., Ranaie S.O., Mousavi S.M. Optimization and evaluation of acetylcholine esterase immobilization on ceramic packing using response surface methodology. Process Biochem. 2010, 45:81-87.
    • (2010) Process Biochem. , vol.45 , pp. 81-87
    • Ebrahimi, B.1    Shojaosadati, S.A.2    Ranaie, S.O.3    Mousavi, S.M.4
  • 17
  • 19
    • 44649151272 scopus 로고    scopus 로고
    • Preparation of multipurpose cross-linked enzyme aggregates and their application to production of alkyl ferulates
    • Vafiadi C., Topakas E., Christakopoulos P. Preparation of multipurpose cross-linked enzyme aggregates and their application to production of alkyl ferulates. J. Mol. Catal. B: Enzym. 2008, 54:35-41.
    • (2008) J. Mol. Catal. B: Enzym. , vol.54 , pp. 35-41
    • Vafiadi, C.1    Topakas, E.2    Christakopoulos, P.3
  • 20
    • 33745727078 scopus 로고    scopus 로고
    • Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde
    • Cheng S.W., Wei D.Z., Song Q.X., Zhao X.G. Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde. Biotechnol. Lett. 2006, 28:1129-1133.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1129-1133
    • Cheng, S.W.1    Wei, D.Z.2    Song, Q.X.3    Zhao, X.G.4
  • 21
    • 77954690311 scopus 로고    scopus 로고
    • Biocatalytic synthesis of (R)-(-)-mandelic acid from racemic mandelonitrile by cetyltrimethyl ammonium bromide-permeabilized cells of Alcaligenes faecalis ECU0401
    • He Y.C., Zhang Z.J., Xu J.H., Liu Y.Y. Biocatalytic synthesis of (R)-(-)-mandelic acid from racemic mandelonitrile by cetyltrimethyl ammonium bromide-permeabilized cells of Alcaligenes faecalis ECU0401. J. Ind. Microbiol. Biotechnol. 2010, 37:741-750.
    • (2010) J. Ind. Microbiol. Biotechnol. , vol.37 , pp. 741-750
    • He, Y.C.1    Zhang, Z.J.2    Xu, J.H.3    Liu, Y.Y.4
  • 22
    • 0034551766 scopus 로고    scopus 로고
    • Preparation of high activity whole cell biocatalyst by permeabilization of recombinant flocculent yeast with alcohol
    • Kondo A., Liu Y., Furuta M., Fujita Y., Matsumoto T., Fukuda H. Preparation of high activity whole cell biocatalyst by permeabilization of recombinant flocculent yeast with alcohol. Enzyme Microb. Technol. 2000, 27:806-811.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 806-811
    • Kondo, A.1    Liu, Y.2    Furuta, M.3    Fujita, Y.4    Matsumoto, T.5    Fukuda, H.6
  • 25
    • 68649084001 scopus 로고    scopus 로고
    • Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports
    • Cabrera Z., Fernandez-Lorente G., Fernandez-Lafuente R., Palomo J.M., Guisan J.M. Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports. J. Mol. Catal. B: Enzym. 2009, 57:171-176.
    • (2009) J. Mol. Catal. B: Enzym. , vol.57 , pp. 171-176
    • Cabrera, Z.1    Fernandez-Lorente, G.2    Fernandez-Lafuente, R.3    Palomo, J.M.4    Guisan, J.M.5
  • 26
    • 79952042445 scopus 로고    scopus 로고
    • Significant enhancement of (R)-mandelic acid production by relieving substrate inhibition of recombinant nitrilase in toluene-water biphasic system
    • Zhang Z.J., Pan J., Liu J.F., Xu J.H., He Y.C., Liu Y.Y. Significant enhancement of (R)-mandelic acid production by relieving substrate inhibition of recombinant nitrilase in toluene-water biphasic system. J. Biotechnol. 2011, 152:24-29.
    • (2011) J. Biotechnol. , vol.152 , pp. 24-29
    • Zhang, Z.J.1    Pan, J.2    Liu, J.F.3    Xu, J.H.4    He, Y.C.5    Liu, Y.Y.6
  • 27
    • 77956062851 scopus 로고    scopus 로고
    • Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric syntheis of (R)-methyl mandelate
    • Guo J.L., Mu X.Q., Xu Y. Integration of newly isolated biocatalyst and resin-based in situ product removal technique for the asymmetric syntheis of (R)-methyl mandelate. Bioprocess Biosyst. Eng. 2010, 33:797-804.
    • (2010) Bioprocess Biosyst. Eng. , vol.33 , pp. 797-804
    • Guo, J.L.1    Mu, X.Q.2    Xu, Y.3
  • 28
    • 57249105046 scopus 로고    scopus 로고
    • So you think your process is green, how do you know? Using principles of sustainability to determine what is green-a corporate perspective
    • Curzons A.D., Constable D.J.C., Mortimer D.N., Cunningham V.L. So you think your process is green, how do you know? Using principles of sustainability to determine what is green-a corporate perspective. Green Chem. 2001, 3:1-6.
    • (2001) Green Chem. , vol.3 , pp. 1-6
    • Curzons, A.D.1    Constable, D.J.C.2    Mortimer, D.N.3    Cunningham, V.L.4
  • 29
    • 40049090038 scopus 로고    scopus 로고
    • Study on the kinetic characteristics of the asymmetric production of R-(-)-mandelic acid with immobilized Saccharomyces cerevisiae FD11b
    • Xiao M.T., Huang Y.Y., Ye J., Guo Y.H. Study on the kinetic characteristics of the asymmetric production of R-(-)-mandelic acid with immobilized Saccharomyces cerevisiae FD11b. Biochem. Eng. J. 2008, 39:311-318.
    • (2008) Biochem. Eng. J. , vol.39 , pp. 311-318
    • Xiao, M.T.1    Huang, Y.Y.2    Ye, J.3    Guo, Y.H.4


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