메뉴 건너뛰기




Volumn 1, Issue 5, 2006, Pages 582-587

Immobilization of enzymes in microtiter plate scale

Author keywords

Esterase; High throughput screening; Immobilization; Microtiter plate

Indexed keywords

1-PROPANOL; 96-WELL MICROTITER PLATE; ALCOHOLYSIS; ANHYDROUS CONDITIONS; COVALENT BONDING; ESTERASE; HIGH-THROUGHPUT SCREENING; IMMOBILIZATION METHOD; MICROTITER PLATES; P-NITROPHENYL ACETATE; TEST REACTIONS;

EID: 33846189983     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200600031     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0033179684 scopus 로고    scopus 로고
    • Immobilized enzymes: crystals or carriers?
    • Tischer, W., Kasche, V., Immobilized enzymes: crystals or carriers? Trends Biotechnol. 1999, 17, 326-335.
    • (1999) Trends Biotechnol , vol.17 , pp. 326-335
    • Tischer, W.1    Kasche, V.2
  • 2
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • Schmid, A., Dordick, J.S., Hauer, B., Kiener, A. et al., Industrial biocatalysis today and tomorrow. Nature 2001, 409, 258-268.
    • (2001) Nature , vol.409 , pp. 258-268
    • Schmid, A.1    Dordick, J.S.2    Hauer, B.3    Kiener, A.4
  • 3
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • Yamada, H., Kobayashi, M., Nitrile hydratase and its application to industrial production of acrylamide. Biosci. Biotechnol. Bioeng. 1996, 60, 1391-1400.
    • (1996) Biosci. Biotechnol. Bioeng. , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 4
    • 84861544686 scopus 로고
    • report number V-89-61316 UNIDO/IPTC 93
    • Klyosov, A.A., report number V-89-61316 UNIDO/IPTC 93, United Nations, 1989, p. 111.
    • (1989) United Nations , pp. 111
    • Klyosov, A.A.1
  • 5
    • 0041528514 scopus 로고    scopus 로고
    • Immobilizing enzymes: how to create more suitable biocatalysts
    • Bornscheuer, U.T., Immobilizing enzymes: how to create more suitable biocatalysts. Angew. Chem. Int. Ed. 2003, 42, 3336-3337.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 3336-3337
    • Bornscheuer, U.T.1
  • 7
    • 10344227692 scopus 로고    scopus 로고
    • Metagenomics: application of genomics to uncultured microorganisms
    • Handelsman, J., Metagenomics: application of genomics to uncultured microorganisms. Microbiol. Mol. Biol. Rev. 2004, 68, 669-685.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 669-685
    • Handelsman, J.1
  • 8
    • 19144364745 scopus 로고    scopus 로고
    • Sorting out metagenomes
    • Handelsman, J., Sorting out metagenomes. Nat. Biotechnol. 2005, 23, 38-39.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 38-39
    • Handelsman, J.1
  • 9
    • 11144295610 scopus 로고    scopus 로고
    • Screening for novel industrial biocatalysts
    • Lorenz, P., Eck, J., Screening for novel industrial biocatalysts. Eng. Life Sci. 2004, 4, 501-504.
    • (2004) Eng. Life Sci. , vol.4 , pp. 501-504
    • Lorenz, P.1    Eck, J.2
  • 10
    • 19144369096 scopus 로고    scopus 로고
    • Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes
    • Uchiyama, T., Takashi, A., Ikemura, T., Watanabe, K., Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes. Nat. Biotechnol. 2005, 23, 88-93.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 88-93
    • Uchiyama, T.1    Takashi, A.2    Ikemura, T.3    Watanabe, K.4
  • 11
    • 0031300142 scopus 로고    scopus 로고
    • Molecular evolution: recombinant approaches for accessing biodiversity
    • Short, J.M., Molecular evolution: recombinant approaches for accessing biodiversity. Nat. Biotechnol. 1997, 15, 1322-1323.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 1322-1323
    • Short, J.M.1
  • 13
    • 0038119762 scopus 로고    scopus 로고
    • Use of physicochemical tools to determine the choice of optimal enzyme: stabilization of D-amino acid oxidase
    • Betancor, L., Hidalgo, A., Fernandez-Lorente, G., Mateo, C. et al., Use of physicochemical tools to determine the choice of optimal enzyme: stabilization of D-amino acid oxidase. Biotechnol. Prog. 2003, 19, 784-788.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 784-788
    • Betancor, L.1    Hidalgo, A.2    Fernandez-Lorente, G.3    Mateo, C.4
  • 14
    • 0035931364 scopus 로고    scopus 로고
    • Biocatalyst engineering exerts a dramatic effect on selectivity of hydrolysis catalyzed by immobilized lipases in aqueous medium
    • Fernandez-Lorente, G., Fernandez-Lafuente, R., Palomo, J.M., Mateo, C. et al., Biocatalyst engineering exerts a dramatic effect on selectivity of hydrolysis catalyzed by immobilized lipases in aqueous medium. J. Mol. Catal. B: Enzymatic 2001, 11, 649-656.
    • (2001) J. Mol. Catal. B: Enzymatic , vol.11 , pp. 649-656
    • Fernandez-Lorente, G.1    Fernandez-Lafuente, R.2    Palomo, J.M.3    Mateo, C.4
  • 15
    • 0037450167 scopus 로고    scopus 로고
    • Modulation of Mucor miehei lipase properties via directed immobilization on different heterofunctional epoxi resins. Hydrolytic resolution of (R, S)-2-butyroyl-2-phenylacetic acid
    • Palomo, J.M., Muñoz, G., Fernandez-Lorente, G., Mateo, C. et al., Modulation of Mucor miehei lipase properties via directed immobilization on different heterofunctional epoxi resins. Hydrolytic resolution of (R, S)-2-butyroyl-2-phenylacetic acid. J. Mol. Catal. B: Enzymatic 2003, 21, 201-210.
    • (2003) J. Mol. Catal. B: Enzymatic , vol.21 , pp. 201-210
    • Palomo, J.M.1    Muñoz, G.2    Fernandez-Lorente, G.3    Mateo, C.4
  • 16
    • 0036843441 scopus 로고    scopus 로고
    • Modulation of the enantioselectivity of lipases via controlled immobilization and mediumm engineering: hydrolytic resolution of mandelic acid esters
    • Palomo, J.M., Fernandez-Lorente, G., Mateo, C., Ortiz, C. et al., Modulation of the enantioselectivity of lipases via controlled immobilization and mediumm engineering: hydrolytic resolution of mandelic acid esters. Enzyme Microb. Technol. 2002, 31, 775-783.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 775-783
    • Palomo, J.M.1    Fernandez-Lorente, G.2    Mateo, C.3    Ortiz, C.4
  • 18
    • 0032524178 scopus 로고    scopus 로고
    • Characterization, and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens
    • Krebsfänger, N., Zocher, F., Altenbuchner, J., Bornscheuer, U.T., Characterization, and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens. Enzyme Microb. Technol. 1998, 21, 641-646.
    • (1998) Enzyme Microb. Technol. , vol.21 , pp. 641-646
    • Krebsfänger, N.1    Zocher, F.2    Altenbuchner, J.3    Bornscheuer, U.T.4
  • 19
    • 0032955788 scopus 로고    scopus 로고
    • Overexpression and characterization of an esterase from Streptomyces diastatochromogenes
    • Khalameyzer, V., Bornscheuer, U.T., Overexpression and characterization of an esterase from Streptomyces diastatochromogenes. Biotechnol. Lett. 1999, 21, 101-104.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 101-104
    • Khalameyzer, V.1    Bornscheuer, U.T.2
  • 20
    • 0038236305 scopus 로고    scopus 로고
    • A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases
    • Henke, E., Bornscheuer, U.T., Schmid, R.D., Pleiss, J., A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. ChemBioChem 2003, 4, 485-493.
    • (2003) ChemBioChem , vol.4 , pp. 485-493
    • Henke, E.1    Bornscheuer, U.T.2    Schmid, R.D.3    Pleiss, J.4
  • 21
    • 0037049424 scopus 로고    scopus 로고
    • Enantioselective transesterification of a tertiary alcohol by lipase A from Candida antarctica
    • Krishna, H.S., Persson, M.M., Bornscheuer, U.T., Enantioselective transesterification of a tertiary alcohol by lipase A from Candida antarctica. Tetrahedron: Asymmetry 2002, 13, 2693-2696.
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 2693-2696
    • Krishna, H.S.1    Persson, M.M.2    Bornscheuer, U.T.3
  • 22
    • 0035927926 scopus 로고    scopus 로고
    • Enzyme-coated micro-crystals: a 1-step method for high activity biocatalyst preparation
    • Kreiner, M., Moore, B.D., Parker, M.C., Enzyme-coated micro-crystals: a 1-step method for high activity biocatalyst preparation. Chem. Commun. 2001, 1096-1097.
    • (2001) Chem. Commun. , pp. 1096-1097
    • Kreiner, M.1    Moore, B.D.2    Parker, M.C.3
  • 23
    • 0036671720 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates with enhanced activity: application to lipases
    • López-Serrano, P., Cao, L., van Rantwijk, F., Sheldon, R., Cross-linked enzyme aggregates with enhanced activity: application to lipases. Biotechnol. Lett. 2002, 24, 1379-1383.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 1379-1383
    • López-Serrano, P.1    Cao, L.2    van Rantwijk, F.3    Sheldon, R.4
  • 26
    • 0036671720 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates with enhanced activity: application to lipases
    • Lopez-Serrano, P., Cao, L., van Rantwijk, F., Sheldon, R., Cross-linked enzyme aggregates with enhanced activity: application to lipases. Biotechnol. Lett. 2002, 24, 1379-1383.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 1379-1383
    • Lopez-Serrano, P.1    Cao, L.2    van Rantwijk, F.3    Sheldon, R.4
  • 27
    • 0034575018 scopus 로고    scopus 로고
    • Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage
    • Mateo, C., Fernandez-Lorente, G., Abian, O., Fernandez-Lafuente, R., Guisan, J.M., Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 2000, 1, 739-745.
    • (2000) Biomacromolecules , vol.1 , pp. 739-745
    • Mateo, C.1    Fernandez-Lorente, G.2    Abian, O.3    Fernandez-Lafuente, R.4    Guisan, J.M.5
  • 28
    • 0002156239 scopus 로고    scopus 로고
    • Immobilized enzymes: methods and application
    • Tischer, W., Wedekind, F., Immobilized enzymes: methods and application. Topics Curr. Chem. 1998, 200, 95-126.
    • (1998) Topics Curr. Chem. , vol.200 , pp. 95-126
    • Tischer, W.1    Wedekind, F.2
  • 29
    • 0035210770 scopus 로고    scopus 로고
    • Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyper-hydrophilic micro-environments surrounding enzyme molecules
    • Abian, O., Mateo, C., Fernandez-Lorente, G., Palomo, J.M. et al., Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyper-hydrophilic micro-environments surrounding enzyme molecules. Biocatal. Biotrans. 2001, 19, 489-504.
    • (2001) Biocatal. Biotrans. , vol.19 , pp. 489-504
    • Abian, O.1    Mateo, C.2    Fernandez-Lorente, G.3    Palomo, J.M.4
  • 30
    • 0036644103 scopus 로고    scopus 로고
    • Isomerization of pentose and hexose sugars by an enzyme reactor packed with cross-linked xylose isomerase crystals
    • Jokela, J., Pastinen, O., Leisola, M., Isomerization of pentose and hexose sugars by an enzyme reactor packed with cross-linked xylose isomerase crystals. Enzyme Microb. Technol. 2002, 31, 67-76.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 67-76
    • Jokela, J.1    Pastinen, O.2    Leisola, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.