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Volumn 33, Issue 3, 2007, Pages 228-231

Catalytic properties of cross-linked enzyme crystals in organic media

Author keywords

Activity; Cross linked enzyme crystals; Enantioselectivity; Organic solvent

Indexed keywords

CROSS-LINKED ENZYME CRYSTALS; ENANTIOSELECTIVITY;

EID: 33846909524     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2006.10.024     Document Type: Article
Times cited : (13)

References (28)
  • 2
    • 33748996483 scopus 로고    scopus 로고
    • Biotransformations for a green future
    • Truesdell S. Biotransformations for a green future. Chem. Eng. Prog. 101 (2005) 44-47
    • (2005) Chem. Eng. Prog. , vol.101 , pp. 44-47
    • Truesdell, S.1
  • 3
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 409 (2001) 241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 4
    • 0025449548 scopus 로고
    • Protease-catalyzed synthetic reactions and immobilization-activation of the enzymes in hydrophilic organic solvents
    • Kise H., Hayakawa A., and Noritomi H. Protease-catalyzed synthetic reactions and immobilization-activation of the enzymes in hydrophilic organic solvents. J. Biotechnol. 14 (1990) 239-254
    • (1990) J. Biotechnol. , vol.14 , pp. 239-254
    • Kise, H.1    Hayakawa, A.2    Noritomi, H.3
  • 5
    • 0030570503 scopus 로고    scopus 로고
    • The influence of the mode of enzyme preparation on enzymatic enantioselectivity in organic solvents and its temperature dependence
    • Noritomi H., Almarsson O., Barletta G.L., and Klibanov A.M. The influence of the mode of enzyme preparation on enzymatic enantioselectivity in organic solvents and its temperature dependence. Biotechnol. Bioeng. 51 (1996) 95-99
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 95-99
    • Noritomi, H.1    Almarsson, O.2    Barletta, G.L.3    Klibanov, A.M.4
  • 6
    • 0033589368 scopus 로고    scopus 로고
    • Enantioselective recognition mechanism of secondary alcohol by surfactant-coated lipases in nonaqueous media
    • Kamiya N., Kasagi H., Inoue M., Kusunoki K., and Goto M. Enantioselective recognition mechanism of secondary alcohol by surfactant-coated lipases in nonaqueous media. Biotechnol. Bioeng. 65 (1999) 227-232
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 227-232
    • Kamiya, N.1    Kasagi, H.2    Inoue, M.3    Kusunoki, K.4    Goto, M.5
  • 7
    • 0000916487 scopus 로고
    • Cross-linked enzyme crystals as robust biocatalysts
    • St. Clair N.L., and Navia M.A. Cross-linked enzyme crystals as robust biocatalysts. J. Am. Chem. Soc. 114 (1992) 7314-7316
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7314-7316
    • St. Clair, N.L.1    Navia, M.A.2
  • 8
    • 0031878411 scopus 로고    scopus 로고
    • Increased thermostability of crosslinked enzyme crystals of subtilisin in organic solvents
    • Noritomi H., Koyama K., Kato S., and Nagahama K. Increased thermostability of crosslinked enzyme crystals of subtilisin in organic solvents. Biotechnol. Tech. 12 (1998) 467-469
    • (1998) Biotechnol. Tech. , vol.12 , pp. 467-469
    • Noritomi, H.1    Koyama, K.2    Kato, S.3    Nagahama, K.4
  • 9
    • 0036007990 scopus 로고    scopus 로고
    • Mechanical stability of immobilized biocatalysts (CLECs) in dilute agitated suspensions
    • Lee T.S., Turner M.K., and Lye G.J. Mechanical stability of immobilized biocatalysts (CLECs) in dilute agitated suspensions. Biotechnol. Prog. 18 (2002) 43-50
    • (2002) Biotechnol. Prog. , vol.18 , pp. 43-50
    • Lee, T.S.1    Turner, M.K.2    Lye, G.J.3
  • 10
    • 0242407525 scopus 로고    scopus 로고
    • Stability and activity of crosslinking enzyme crystals of cyclodextrin glucanotransferase isolated from Bacillus macerans
    • Kim W., Chae H., Park C., and Lee K. Stability and activity of crosslinking enzyme crystals of cyclodextrin glucanotransferase isolated from Bacillus macerans. J. Mol. Catal. B: Enzyme 26 (2003) 287-292
    • (2003) J. Mol. Catal. B: Enzyme , vol.26 , pp. 287-292
    • Kim, W.1    Chae, H.2    Park, C.3    Lee, K.4
  • 11
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A., and Klibanov A.M. Enzymatic catalysis in nonaqueous solvents. J. Biol. Chem. 263 (1988) 3194-3201
    • (1988) J. Biol. Chem. , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 13
    • 0028302684 scopus 로고
    • The solvent dependence of enzyme specificity
    • Wescott C.R., and Klibanov A.M. The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1206 (1994) 1-9
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 1-9
    • Wescott, C.R.1    Klibanov, A.M.2
  • 14
    • 0029883864 scopus 로고    scopus 로고
    • The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents
    • Schmitke J.L., Wescott C.R., and Klibanov A.M. The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents. J. Am. Chem. Soc. 118 (1996) 3360-3365
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3360-3365
    • Schmitke, J.L.1    Wescott, C.R.2    Klibanov, A.M.3
  • 17
    • 0030185060 scopus 로고    scopus 로고
    • Novel crystalline catalysts
    • Margolin A.L. Novel crystalline catalysts. TIBTECH 14 (1996) 223-230
    • (1996) TIBTECH , vol.14 , pp. 223-230
    • Margolin, A.L.1
  • 18
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • Zaks A., and Klibanov A.M. The effect of water on enzyme action in organic media. J. Biol. Chem. 263 (1988) 8017-8021
    • (1988) J. Biol. Chem. , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, A.M.2
  • 19
    • 45249131071 scopus 로고
    • Organic liquids and biocatalysts: theory and practice
    • Halling P.J. Organic liquids and biocatalysts: theory and practice. Trends Biotechnol. 7 (1989) 50-52
    • (1989) Trends Biotechnol. , vol.7 , pp. 50-52
    • Halling, P.J.1
  • 20
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvents than in water?
    • Klibanov A.M. Why are enzymes less active in organic solvents than in water?. Trends Biotechnol. 15 (1997) 97-101
    • (1997) Trends Biotechnol. , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 21
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • Laane C., Boeren S., Vos K., and Veeger C. Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 30 (1987) 81-87
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 22
    • 0032573075 scopus 로고    scopus 로고
    • Comparison of X-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water
    • Schmitke J.L., Stern L.J., and Klibanov A.M. Comparison of X-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 12918-12923
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12918-12923
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 24
    • 0029818293 scopus 로고    scopus 로고
    • Rational control of enzymatic enantioselectivity through solvation thermodynamics
    • Wescott C.R., Noritomi H., and Klibanov A.M. Rational control of enzymatic enantioselectivity through solvation thermodynamics. J. Am. Chem. Soc. 118 (1996) 10365-10370
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10365-10370
    • Wescott, C.R.1    Noritomi, H.2    Klibanov, A.M.3
  • 26
    • 78651149328 scopus 로고
    • Intermolecular cross linking of protein in crystalline state
    • Quiocho F.A., and Richards F.M. Intermolecular cross linking of protein in crystalline state. Proc. Natl. Acad. Sci. U.S.A. 52 (1964) 833-839
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 27
    • 0028035218 scopus 로고
    • Cross-linked enzyme crystals of fructose diphosphate aldolase: development as a biocatalyst for synthesis
    • Sobolov S.B., Bartoszko-Malik A., Oeschger T.R., and Montelbano M.M. Cross-linked enzyme crystals of fructose diphosphate aldolase: development as a biocatalyst for synthesis. Tetrahedron Lett. 35 (1994) 7751-7754
    • (1994) Tetrahedron Lett. , vol.35 , pp. 7751-7754
    • Sobolov, S.B.1    Bartoszko-Malik, A.2    Oeschger, T.R.3    Montelbano, M.M.4
  • 28
    • 0003548906 scopus 로고    scopus 로고
    • Koskinen A.M.P., and Klibanov A.M. (Eds), Blackie A & P, London
    • In: Koskinen A.M.P., and Klibanov A.M. (Eds). Enzymatic Reactions in Organic Media (1996), Blackie A & P, London
    • (1996) Enzymatic Reactions in Organic Media


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.