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Volumn 62, Issue 5, 1999, Pages 554-561

Optimization of Pseudomonas cepacia lipase preparations for catalysis in organic solvents

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; CARBON TETRACHLORIDE; CATALYSIS; CATALYST ACTIVITY; CHEMICAL BONDS; CONFORMATIONS; CROSSLINKING; ENZYME IMMOBILIZATION; ESTERIFICATION; HYDROLYSIS; MOLECULAR STRUCTURE; ORGANIC SOLVENTS;

EID: 0033525431     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19990305)62:5<554::AID-BIT7>3.0.CO;2-2     Document Type: Article
Times cited : (54)

References (36)
  • 2
    • 0031149286 scopus 로고    scopus 로고
    • Water activity fails to predict critical hydration level for enzyme activity in polar organic solvents: Intercorvesion of water concentrations and activities
    • Bell G, Janssen AEM, Halling PJ. 1997. Water activity fails to predict critical hydration level for enzyme activity in polar organic solvents: Intercorvesion of water concentrations and activities. Enzyme Microb Technol 20:471-477.
    • (1997) Enzyme Microb Technol , vol.20 , pp. 471-477
    • Bell, G.1    Janssen, A.E.M.2    Halling, P.J.3
  • 3
    • 0027483513 scopus 로고
    • Water activity does not influence the enantioselectivity of lipase PS and lipoprotein lipase in organic solvents
    • Bovara R, Carrea G, Ottolina G, Riva S. 1993a. Water activity does not influence the enantioselectivity of lipase PS and lipoprotein lipase in organic solvents. Biotechnol Lett 15:169-174.
    • (1993) Biotechnol Lett , vol.15 , pp. 169-174
    • Bovara, R.1    Carrea, G.2    Ottolina, G.3    Riva, S.4
  • 5
    • 0031553971 scopus 로고    scopus 로고
    • Activity, stability, and conformation of methoxypoly(ethylene glycol)-subtilisin at different concentrations of water in dioxane
    • Bovara R, Carrea G, Gioacchini AM, Riva S, Secundo F. 1997. Activity, stability, and conformation of methoxypoly(ethylene glycol)-subtilisin at different concentrations of water in dioxane. Biotechnol Bioeng 54:50-57.
    • (1997) Biotechnol Bioeng , vol.54 , pp. 50-57
    • Bovara, R.1    Carrea, G.2    Gioacchini, A.M.3    Riva, S.4    Secundo, F.5
  • 6
    • 0028855057 scopus 로고
    • Role of solvents in the control of enzyme selectivity in organic media
    • Carrea G, Ottolina G, Riva S. 1995. Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol 13:63-70.
    • (1995) Trends Biotechnol , vol.13 , pp. 63-70
    • Carrea, G.1    Ottolina, G.2    Riva, S.3
  • 7
    • 0026892825 scopus 로고
    • Designing enzymes for use in organic solvents
    • Dordick JS. 1992. Designing enzymes for use in organic solvents. Biotechnol Prog 8:259-267.
    • (1992) Biotechnol Prog , vol.8 , pp. 259-267
    • Dordick, J.S.1
  • 12
    • 0022691550 scopus 로고
    • Engineering physicochemical and biological properties of proteins by chemical modification
    • Inada Y, Yoshimoto T, Matsushima T, Saito Y. 1986. Engineering physicochemical and biological properties of proteins by chemical modification. Trends Biotechnol 4:68-73.
    • (1986) Trends Biotechnol , vol.4 , pp. 68-73
    • Inada, Y.1    Yoshimoto, T.2    Matsushima, T.3    Saito, Y.4
  • 15
    • 2542506051 scopus 로고    scopus 로고
    • The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
    • Kim KK, Song HK, Shin DH, Hwang KY, Suh SW. 1997. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure 5:173-185.
    • (1997) Structure , vol.5 , pp. 173-185
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Suh, S.W.5
  • 16
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov AM. 1989. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem Sci 14:141-144.
    • (1989) Trends Biochem Sci , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 17
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvent than in water?
    • Klibanov AM. 1997. Why are enzymes less active in organic solvent than in water? Trends Biotechnol 15:97-101.
    • (1997) Trends Biotechnol , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 19
    • 0027604288 scopus 로고
    • Separation albumin-PEG: Transmission of PEG through ultrafiltration membranes
    • Lentsch S, Aimar P, Orozco JL. 1993. Separation albumin-PEG: Transmission of PEG through ultrafiltration membranes. Biotechnol Bioeng 41:1039-1047.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 1039-1047
    • Lentsch, S.1    Aimar, P.2    Orozco, J.L.3
  • 20
    • 0028052370 scopus 로고
    • Determination of peroxide in vegetable oils by an organic-phase enzyme electrode
    • Mannino S, Cosio MS, Wang J. 1994. Determination of peroxide in vegetable oils by an organic-phase enzyme electrode. Anal Lett 27: 299-308.
    • (1994) Anal Lett , vol.27 , pp. 299-308
    • Mannino, S.1    Cosio, M.S.2    Wang, J.3
  • 21
    • 0029769279 scopus 로고    scopus 로고
    • Trapping of different lipase conformers in water restricted environments
    • Mingarro I, Gonzales-Navarro H, Braco L. 1996. Trapping of different lipase conformers in water restricted environments. Biochemistry 35: 9935-9944.
    • (1996) Biochemistry , vol.35 , pp. 9935-9944
    • Mingarro, I.1    Gonzales-Navarro, H.2    Braco, L.3
  • 22
    • 0000714375 scopus 로고
    • Complex formation between chymotrypsin and ethyl cellulose as means to solubilize the enzyme in active form in toluene
    • Otamiri M, Adlercreutz P, Mattiasson B. 1992. Complex formation between chymotrypsin and ethyl cellulose as means to solubilize the enzyme in active form in toluene. Biocatalysis 6:291-305.
    • (1992) Biocatalysis , vol.6 , pp. 291-305
    • Otamiri, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 23
    • 0028753336 scopus 로고
    • Effects of enantiomeric solvents on the activity, thermostability and activation energy of lipoprotein lipase
    • Ottolina G, Gianinetti F, Riva S, Carrea G. 1994. Effects of enantiomeric solvents on the activity, thermostability and activation energy of lipoprotein lipase. Catal Today 22:511-516.
    • (1994) Catal Today , vol.22 , pp. 511-516
    • Ottolina, G.1    Gianinetti, F.2    Riva, S.3    Carrea, G.4
  • 24
    • 0029134278 scopus 로고
    • Efficient heterogeneous biocatalyst by entrapment of lipases in hydrophobic sol-gel materials
    • Reetz M, Zonta A, Simpelkamp J. 1995. Efficient heterogeneous biocatalyst by entrapment of lipases in hydrophobic sol-gel materials. Angew Chem, Int Ed Engl 34:301-303.
    • (1995) Angew Chem, Int Ed Engl , vol.34 , pp. 301-303
    • Reetz, M.1    Zonta, A.2    Simpelkamp, J.3
  • 25
    • 0038992211 scopus 로고
    • Solvation of CBZ-amino acid nitrophenyl esters in organic media and kinetics of their transesterification by subtilisin
    • Reimann A, Robb DA, Halling PJ. 1993. Solvation of CBZ-amino acid nitrophenyl esters in organic media and kinetics of their transesterification by subtilisin. Biotechnol Bioeng 40:1069-1077.
    • (1993) Biotechnol Bioeng , vol.40 , pp. 1069-1077
    • Reimann, A.1    Robb, D.A.2    Halling, P.J.3
  • 26
    • 0003228042 scopus 로고
    • Organic solvents: Physical properties and methods of purification
    • Weissberger A, editor. New York: Wiley
    • Riddick JA, Bunger WB, Sakano TK. 1986. Organic solvents: Physical properties and methods of purification. In: Weissberger A, editor. Techniques of Chemistry, 4th edition. New York: Wiley. Vol. 2.
    • (1986) Techniques of Chemistry, 4th Edition , vol.2
    • Riddick, J.A.1    Bunger, W.B.2    Sakano, T.K.3
  • 27
    • 0015072056 scopus 로고
    • Fluorescence reaction for amino acid
    • Roth M. 1971. Fluorescence reaction for amino acid. Anal Chem 43: 880-882.
    • (1971) Anal Chem , vol.43 , pp. 880-882
    • Roth, M.1
  • 28
    • 0029883864 scopus 로고    scopus 로고
    • The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents
    • Schmitke JL, Wescott CR, Klibanov AM. 1996. The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents. J Am Chem Soc 118:3360-3365.
    • (1996) J Am Chem Soc , vol.118 , pp. 3360-3365
    • Schmitke, J.L.1    Wescott, C.R.2    Klibanov, A.M.3
  • 29
    • 0030662088 scopus 로고    scopus 로고
    • The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents
    • Toba S, Merz M, Jr. 1997. The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents. J Am Chem Soc 119:9939-9948.
    • (1997) J Am Chem Soc , vol.119 , pp. 9939-9948
    • Toba, S.1    Merz M., Jr.2
  • 31
    • 0026544459 scopus 로고
    • Reaction rate with suspended lipase catalyst shows similar dependence on water activity in different organic solvents
    • Valivety RH, Halling PJ, Macrae AR. 1992. Reaction rate with suspended lipase catalyst shows similar dependence on water activity in different organic solvents. Biochim Biophys Acta 1118:218-222.
    • (1992) Biochim Biophys Acta , vol.1118 , pp. 218-222
    • Valivety, R.H.1    Halling, P.J.2    Macrae, A.R.3
  • 33
    • 0027439598 scopus 로고
    • Improved activity retention of enzymes deposited on solid supports
    • Wehtje E, Adlercreutz P, Mattiason B. 1993. Improved activity retention of enzymes deposited on solid supports. Biotechnol Bioeng 41:171-178.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 171-178
    • Wehtje, E.1    Adlercreutz, P.2    Mattiason, B.3
  • 34
    • 0242528545 scopus 로고
    • Enantiopreferences of lipase from Pseudomonas cepacia toward primary alcohols
    • Weissfloch ANE, Kazlauskas RJ. 1995. Enantiopreferences of lipase from Pseudomonas cepacia toward primary alcohols. J Org Chem 60: 6959-6969.
    • (1995) J Org Chem , vol.60 , pp. 6959-6969
    • Weissfloch, A.N.E.1    Kazlauskas, R.J.2
  • 35
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A, Klibanov AM. 1988a. Enzymatic catalysis in nonaqueous solvents. J Biol Chem 263:3194-3201.
    • (1988) J Biol Chem , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 36
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • Zaks A, Klibanov AM. 1988b. The effect of water on enzyme action in organic media. J Biol Chem 263:8017-8021.
    • (1988) J Biol Chem , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.