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Volumn 24, Issue 1-2, 1999, Pages 60-66

Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports

Author keywords

Conformational stability; Cutinase; Dextran; Immobilization; Thermostability

Indexed keywords

CATALYST SUPPORTS; CONFORMATIONS; DERIVATIVES; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME KINETICS; POLYSACCHARIDES; SILICA; SOLUBILITY; THERMODYNAMIC STABILITY;

EID: 0342459772     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(98)00089-1     Document Type: Article
Times cited : (26)

References (36)
  • 1
    • 0027572338 scopus 로고
    • Mechanism-based strategies for protein thermostabilization
    • Mozhaev V. Mechanism-based strategies for protein thermostabilization. Tibtech. 11:1993;88-95.
    • (1993) Tibtech , vol.11 , pp. 88-95
    • Mozhaev, V.1
  • 2
    • 0028172607 scopus 로고
    • Can immobilisation be exploited to modify enzyme activity?
    • Clark D.S. Can immobilisation be exploited to modify enzyme activity? Tibtech. 12:1994;439-443.
    • (1994) Tibtech , vol.12 , pp. 439-443
    • Clark, D.S.1
  • 3
    • 0018408815 scopus 로고
    • Enzyme stabilisation by immobilisation
    • Klibanov A.M. Enzyme stabilisation by immobilisation. Anal. Biochem. 93:1979;1-25.
    • (1979) Anal. Biochem. , vol.93 , pp. 1-25
    • Klibanov, A.M.1
  • 4
    • 0017670982 scopus 로고
    • Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion
    • Martinek K., Klibanov A.M., Goldmacher V.S., Berezin I.V.I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim. Biophys. Acta. 485:1977;1-12.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 1-12
    • Martinek, K.1    Klibanov, A.M.2    Goldmacher, V.S.3    Berezin, I.V.I.4
  • 5
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for the immobilisation-stabilisation of enzymes
    • Guísan J.M. Aldehyde-agarose gels as activated supports for the immobilisation-stabilisation of enzymes. Enzyme Microb. Technol. 10:1988;375-382.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guísan, J.M.1
  • 6
    • 0026417558 scopus 로고
    • Immobilisation-stabilisation of α-chymotrypsin by covalent attachment to aldehyde-agarose gels
    • Guísan J.M., Bastida A., Cuesta C., Fernandez-Lafuente R., Rosell C.M. Immobilisation-stabilisation of α-chymotrypsin by covalent attachment to aldehyde-agarose gels. Biotechnol. Bioeng. 38:1991;1144-1152.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 1144-1152
    • Guísan, J.M.1    Bastida, A.2    Cuesta, C.3    Fernandez-Lafuente, R.4    Rosell, C.M.5
  • 7
    • 0025405523 scopus 로고
    • Multipoint attachment to a support protects enzyme from inactivation by organic solvents: Α-chymotrypsin in aqueous solutions of alcohols and diols
    • Mozhaev V., Sergeeva A.B., Khmelnitsky Y. Multipoint attachment to a support protects enzyme from inactivation by organic solvents α-chymotrypsin in aqueous solutions of alcohols and diols . Biotechnol. Bioeng. 35:1990;653-659.
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 653-659
    • Mozhaev, V.1    Sergeeva, A.B.2    Khmelnitsky, Y.3
  • 8
    • 0015522130 scopus 로고
    • Microenvironmental effects on enzyme catalysis. A kinetic study of polyanionic and polycationic derivatives of chymotrypsin
    • Goldstein L. Microenvironmental effects on enzyme catalysis. A kinetic study of polyanionic and polycationic derivatives of chymotrypsin. Biochemistry. 11:1972;4072-4084.
    • (1972) Biochemistry , vol.11 , pp. 4072-4084
    • Goldstein, L.1
  • 9
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez C., De Geuss P., Lauwereys M., Matthyssens G., Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature. 356:1992;615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geuss, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 12
    • 0027627398 scopus 로고
    • Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles
    • Sebastiao M.J., Cabral J.M.S., Aires-Barros M.R. Synthesis of fatty acid esters by a recombinant cutinase in reversed micelles. Biotechnol. Bioeng. 42:1993;326-332.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 326-332
    • Sebastiao, M.J.1    Cabral, J.M.S.2    Aires-Barros, M.R.3
  • 13
    • 0029205576 scopus 로고
    • Triglyceride hydrolysis and stability of recombinant cutinase from Fusarium solani in AOT-isooctane-reversed micelles
    • Melo E.P., Aires-Barros M.R., Cabral J.M.S. Triglyceride hydrolysis and stability of recombinant cutinase from Fusarium solani in AOT-isooctane-reversed micelles. Appl. Biochem. Biotechnol. 50:1995;45-56.
    • (1995) Appl. Biochem. Biotechnol. , vol.50 , pp. 45-56
    • Melo, E.P.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 14
    • 0030413045 scopus 로고    scopus 로고
    • Esterification and transesterification catalysed by cutinase in reversed micelles of CTAB for the synthesis of short chain esters
    • Cunnah P.J., Aires-Barros M.R., Cabral J.M.S. Esterification and transesterification catalysed by cutinase in reversed micelles of CTAB for the synthesis of short chain esters. Biocatal. Biotransform. 14:1996;125-146.
    • (1996) Biocatal. Biotransform. , vol.14 , pp. 125-146
    • Cunnah, P.J.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 15
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov P., Gill S.J. Stability of protein structure and hydrophobic interaction. Adv. Prot. Chem. 39:1988;191-234.
    • (1988) Adv. Prot. Chem. , vol.39 , pp. 191-234
    • Privalov, P.1    Gill, S.J.2
  • 16
    • 84990481835 scopus 로고
    • Influence of the solvent properties on protein stability in organic media
    • W. van den Tweel, & R.M. Buitelaar. New York: Elsevier Science Publishers
    • Battistel E., Bianchi D. Influence of the solvent properties on protein stability in organic media. van den Tweel W., Buitelaar R.M. Stability and Stabilisation of Enzymes. 1993;13-20 Elsevier Science Publishers, New York.
    • (1993) Stability and Stabilisation of Enzymes , pp. 13-20
    • Battistel, E.1    Bianchi, D.2
  • 18
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back J., Oakenfull D., Smith M. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry. 18:(23):1979;5191-5196.
    • (1979) Biochemistry , vol.18 , Issue.23 , pp. 5191-5196
    • Back, J.1    Oakenfull, D.2    Smith, M.3
  • 19
    • 0028765236 scopus 로고
    • A differential scanning calorimetric study of chymotrypsin in the presence of added polymers
    • Otamiri M., Adlercreutz P., Mattiasson B. A differential scanning calorimetric study of chymotrypsin in the presence of added polymers. Biotechnol. Bioeng. 44:1994;73-78.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 73-78
    • Otamiri, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 22
    • 0030606144 scopus 로고    scopus 로고
    • Dextran coated silica and its behaviour in high performance size exclusion chromatography
    • Matthijs G., Schacht E. Dextran coated silica and its behaviour in high performance size exclusion chromatography. J. Chromatogr. A. 755:1996;1-10.
    • (1996) J. Chromatogr. a , vol.755 , pp. 1-10
    • Matthijs, G.1    Schacht, E.2
  • 24
    • 0020478566 scopus 로고
    • Lipoprotein lipase-catalyzed hydiolysis of p-nitrophenyl butyrate
    • Jackson R.L., Shirai K. Lipoprotein lipase-catalyzed hydiolysis of p-nitrophenyl butyrate. J. Biol. Chem. 257:1982;1253-1258.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1253-1258
    • Jackson, R.L.1    Shirai, K.2
  • 25
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens
    • Winkler U.K., Stuckmann M. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J. Bacteriol. 138:1979;663-670.
    • (1979) J. Bacteriol. , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 26
    • 0021675149 scopus 로고
    • Effects of polyhydric alcohols on invertase stabilisation
    • Combes D., Monsan P. Effects of polyhydric alcohols on invertase stabilisation. Ann. N. Y. Acad. Sci. 434:1984;61-63.
    • (1984) Ann. N. Y. Acad. Sci. , vol.434 , pp. 61-63
    • Combes, D.1    Monsan, P.2
  • 27
    • 0021699812 scopus 로고
    • Effect of water activity on enzyme activity and stability
    • Monsan P., Combes D. Effect of water activity on enzyme activity and stability. Ann. N. Y. Acad. Sci. 542:1988;48-60.
    • (1988) Ann. N. Y. Acad. Sci. , vol.542 , pp. 48-60
    • Monsan, P.1    Combes, D.2
  • 28
    • 0000250076 scopus 로고
    • Additives and enzyme stability
    • Gray C.J. Additives and enzyme stability. Biocatalysis. 1:1988;187-196.
    • (1988) Biocatalysis , vol.1 , pp. 187-196
    • Gray, C.J.1
  • 29
    • 84987477530 scopus 로고
    • The stabilisation of analytical enzymes using polyelectrolytes and sugar derivatives
    • W. van den Tweel, & R.M. Buitelaar. Elsevier Science Publishers
    • Gibson T., Hulbert J.N., Pierce B., Webster J.I. The stabilisation of analytical enzymes using polyelectrolytes and sugar derivatives. van den Tweel W., Buitelaar R.M. Stability and Stabilisation of Enzymes. 1993;337-346 Elsevier Science Publishers.
    • (1993) Stability and Stabilisation of Enzymes , pp. 337-346
    • Gibson, T.1    Hulbert, J.N.2    Pierce, B.3    Webster, J.I.4
  • 30
    • 0028098166 scopus 로고
    • The influence of polyalcohols and carbohydrates on the thermostability of α-amylase
    • Hendrickx M., DeCordt S., Maesmans G., Tobback P. The influence of polyalcohols and carbohydrates on the thermostability of α-amylase. Biotechnol. Bioeng. 43:1994;107-114.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 107-114
    • Hendrickx, M.1    Decordt, S.2    Maesmans, G.3    Tobback, P.4
  • 31
    • 0026955799 scopus 로고
    • Chemical cross-linking and the stabilisation of proteins and enzymes
    • Wong S.S., Wong L.-J. Chemical cross-linking and the stabilisation of proteins and enzymes. Enzyme Microb. Technol. 14:1992;866-874.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 866-874
    • Wong, S.S.1    Wong, L.-J.2
  • 32
    • 0024677047 scopus 로고
    • Stabilisation of enzymes by multi-point covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • Blanco R., Guísan J.M. Stabilisation of enzymes by multi-point covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb. Technol. 11:1989;360-366.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 360-366
    • Blanco, R.1    Guísan, J.M.2
  • 33
    • 0028409645 scopus 로고
    • Blueprint for a lipase support: Use of hydrophobic controlled-pore glasses as model systems
    • Bosley J.A., Clayton J.C. Blueprint for a lipase support Use of hydrophobic controlled-pore glasses as model systems . Biotechnol. Bioeng. 43:1994;934-938.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 934-938
    • Bosley, J.A.1    Clayton, J.C.2
  • 35
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • Henley J.P., Sadana A. Categorization of enzyme deactivations using a series-type mechanism. Enzyme Microb. Technol. 7:1985;50-60.
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 36
    • 0344930826 scopus 로고    scopus 로고
    • Ph.D. thesis, University of Ghent, Ghent, Belgium
    • Matthys, G. Ph.D. thesis, University of Ghent, Ghent, Belgium, 1997.
    • (1997)
    • Matthys, G.1


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