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Volumn 19, Issue 42130, 2001, Pages 489-503

Stabilization of Immobilized Enzymes Against Water-Soluble Organic Cosolvents and Generation of Hyper-Hydrophilic Micro-Environments Surrounding Enzyme Molecules

Author keywords

Enzyme polymers co aggregates; Enzymes in organic solvents; Hydrophilization of enzyme environments; Multipoint covalent attachment; Stabilization of enzymes

Indexed keywords

ENZYMES; HYDROPHILICITY; POROUS MATERIALS; SOLVENTS; WATER;

EID: 0035210770     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.3109/10242420108992032     Document Type: Article
Times cited : (50)

References (23)
  • 2
    • 0029142386 scopus 로고
    • Selective enzymic oxidations: stabilisation by multipoint covalent attachment of ferredoxin NADP-reductase, an interesting cofactor recycling enzyme
    • Bes T., Gómez-Moreno X, Guisán J. M., Fernández-Lafuente R. “Selective enzymic oxidations: stabilisation by multipoint covalent attachment of ferredoxin NADP-reductase, an interesting cofactor recycling enzyme”. J. Mol. Catal 1995; 98: 161 – 169
    • (1995) J. Mol. Catal , vol.98 , pp. 161-169
    • Bes, T.1    Gómez-Moreno, X.2    Guisán, J.M.3    Fernández-Lafuente, R.4
  • 3
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • Blanco R. M., Guisán J. M. “Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives”. Enzyme Microb. Technol 1989; 11: 360 – 366
    • (1989) Enzyme Microb. Technol , vol.11 , pp. 360-366
    • Blanco, R.M.1    Guisán, J.M.2
  • 4
    • 0026262142 scopus 로고
    • Enzyme reaction engineering: synthesis of antibiotics catalyzed by stabilized penicillin G acylase in the presence of organic solvents
    • Fernández-Lafuente R., Rosell CM, Guisán J. M. “Enzyme reaction engineering: synthesis of antibiotics catalyzed by stabilized penicillin G acylase in the presence of organic solvents”. Enzyme Microb. Technol 1991a; 13: 898 – 905
    • (1991) Enzyme Microb. Technol , vol.13 , pp. 898-905
    • Fernández-Lafuente, R.1    Rosell, C.M.2    Guisán, J.M.3
  • 5
    • 0001265849 scopus 로고
    • Equilibrium controlled synthesis of cephalotin in monophasic water-organic cosolvents systems catalysed by stabilised derivatives of penicillin G acylase
    • Fernández-Lafuente R., Álvaro G., Blanco R. M., Guisán J. M. “Equilibrium controlled synthesis of cephalotin in monophasic water-organic cosolvents systems catalysed by stabilised derivatives of penicillin G acylase”. Appl. Biochem. Biotechnol 1991b; 27: 277 – 280
    • (1991) Appl. Biochem. Biotechnol , vol.27 , pp. 277-280
    • Fernández-Lafuente, R.1    Álvaro, G.2    Blanco, R.M.3    Guisán, J.M.4
  • 6
    • 0029760450 scopus 로고    scopus 로고
    • Dynamic reaction design of enzymic biotransfomations in organic media: equilibrium controlled synthesis of antibiotics by penicillin G acylase
    • Fernández-Lafuente R., Rosell CM, Guisán J. M. “Dynamic reaction design of enzymic biotransfomations in organic media: equilibrium controlled synthesis of antibiotics by penicillin G acylase”. Biotechnol. Appl. Biochem 1996a; 24: 139 – 143
    • (1996) Biotechnol. Appl. Biochem , vol.24 , pp. 139-143
    • Fernández-Lafuente, R.1    Rosell, C.M.2    Guisán, J.M.3
  • 7
    • 0000797327 scopus 로고    scopus 로고
    • Synthesis of antibiotics (cephaloglycin) catalysed by penicillin G acylase. Evaluation and optimisation of different synthetic approaches
    • Fernández-Lafuente R., Rosell CM, Piatkowska B., Guisán J. M. “Synthesis of antibiotics (cephaloglycin) catalysed by penicillin G acylase. Evaluation and optimisation of different synthetic approaches”. Enzyme Microb. Technol 1996b; 17: 517 – 523
    • (1996) Enzyme Microb. Technol , vol.17 , pp. 517-523
    • Fernández-Lafuente, R.1    Rosell, C.M.2    Piatkowska, B.3    Guisán, J.M.4
  • 8
    • 0032126831 scopus 로고    scopus 로고
    • The coimmobilization of D-aminoacid oxidase and catalase enables the quantitative transformation of D-amino acids (phenylalanine) into alpha-ceto acids (phenylpyruvic acid)
    • Fernández-Lafuente R., Rodríguez V., Guisán J. M. “The coimmobilization of D-aminoacid oxidase and catalase enables the quantitative transformation of D-amino acids (phenylalanine) into alpha-ceto acids (phenylpyruvic acid)”. Enzyme Microb. Technol 1998; 23: 28 – 33
    • (1998) Enzyme Microb. Technol , vol.23 , pp. 28-33
    • Fernández-Lafuente, R.1    Rodríguez, V.2    Guisán, J.M.3
  • 9
    • 0032890111 scopus 로고    scopus 로고
    • Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives dramatic stabilization of penicillin acylase versus organic solvents
    • Fernández-Lafuente R., Rosell CM, Guisán J. M., Caanan-Haden L., Rodes L. “Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives dramatic stabilization of penicillin acylase versus organic solvents”. Enzyme Microb. Technol 1999; 24: 96 – 103
    • (1999) Enzyme Microb. Technol , vol.24 , pp. 96-103
    • Fernández-Lafuente, R.1    Rosell, C.M.2    Guisán, J.M.3    Caanan-Haden, L.4    Rodes, L.5
  • 11
    • 0026655149 scopus 로고
    • Organic solvent changes the chymotrypsin specificity with respect to nucleophiles
    • Gololobov M. Y., Voyushima L. T., Stepanov V. M., Adlercreutz P. “Organic solvent changes the chymotrypsin specificity with respect to nucleophiles”. FEBS Lett 1992; 285: 307 – 312
    • (1992) FEBS Lett , vol.285 , pp. 307-312
    • Gololobov, M.Y.1    Voyushima, L.T.2    Stepanov, V.M.3    Adlercreutz, P.4
  • 12
    • 0024029957 scopus 로고
    • Aldehyde gels for immobilization-stabilization of enzymes
    • Guisán J. M. “Aldehyde gels for immobilization-stabilization of enzymes”. Enzyme Microb. Technol 1988; 10: 375 – 382
    • (1988) Enzyme Microb. Technol , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 13
  • 17
    • 0001785135 scopus 로고
    • Thermostabilization of proteins
    • Gupta M. N. “Thermostabilization of proteins”. Biotechnol. Appl. Biochem 1991; 4: 1 – 11
    • (1991) Biotechnol. Appl. Biochem , vol.4 , pp. 1-11
    • Gupta, M.N.1
  • 18
    • 0023610254 scopus 로고
    • Equilibrium and kinetically controlled synthesis with enzymes: semisynthesis of penicillins and peptides
    • Kasche V., Haufler U., Riechman L. “Equilibrium and kinetically controlled synthesis with enzymes: semisynthesis of penicillins and peptides”. Meth. Enzymol 1987; 136: 280 – 292
    • (1987) Meth. Enzymol , vol.136 , pp. 280-292
    • Kasche, V.1    Haufler, U.2    Riechman, L.3
  • 19
    • 0020799389 scopus 로고
    • Operational stability of copolymerized enzymes at elevated temperatures
    • Mozhaev V. V., Klibanov A. M., Goldmacher V. S., Berezin I. V. “Operational stability of copolymerized enzymes at elevated temperatures”. Biotechnol. Bioeng 1990; 25: 1937 – 1945
    • (1990) Biotechnol. Bioeng , vol.25 , pp. 1937-1945
    • Mozhaev, V.V.1    Klibanov, A.M.2    Goldmacher, V.S.3    Berezin, I.V.4
  • 22
    • 0032874447 scopus 로고    scopus 로고
    • Use of the enzyme penicillin G acylase in selective amidation/amide hydrolysis to resolve ethyl 3-amino-4 pentynoate isomers
    • Topgi R. S., Ng J. S., Landis B., Wang P., Behling J. B. “Use of the enzyme penicillin G acylase in selective amidation/amide hydrolysis to resolve ethyl 3-amino-4 pentynoate isomers”. Biorg. Med. Chem 1999; 7: 2221 – 2229
    • (1999) Biorg. Med. Chem , vol.7 , pp. 2221-2229
    • Topgi, R.S.1    Ng, J.S.2    Landis, B.3    Wang, P.4    Behling, J.B.5
  • 23
    • 0000680497 scopus 로고
    • Enzymatic protecting group techniques
    • Waldman H., Sebastian D. “Enzymatic protecting group techniques”. Chem. Rev 1994; 94: 911 – 937
    • (1994) Chem. Rev , vol.94 , pp. 911-937
    • Waldman, H.1    Sebastian, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.