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Volumn 49, Issue 1, 1996, Pages 106-110

A rapid method for determining kinetic parameters of enzymes exhibiting nonlinear thermal inactivation behavior

Author keywords

alcohol dehydrogenase; enzymes; inactivation; kinetics; thermal inactivation

Indexed keywords

ALCOHOLS; DECAY (ORGANIC); ENZYMES; MATHEMATICAL MODELS; REGRESSION ANALYSIS; SUGAR (SUCROSE); THERMODYNAMICS; YEAST;

EID: 0030569734     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960105)49:1<106::AID-BIT14>3.3.CO;2-Q     Document Type: Article
Times cited : (21)

References (14)
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  • 2
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    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back, J. F., Oakenfull, D., Smith, M. B. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18: 5191-5196.
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  • 4
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    • Thermal inactivation kinetics of horseradish peroxidase
    • Chang, B. S., Park, K. H., Lund, D. B. 1988. Thermal inactivation kinetics of horseradish peroxidase. J. Food Sci. 53: 920-923.
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    • Chang, B.S.1    Park, K.H.2    Lund, D.B.3
  • 5
    • 0028098166 scopus 로고
    • The influence of polyalcohols and carbohydrates on the thermostability of α-amylase
    • DeCordt, S., Hendrickx, M., Maesmans, G., Tobback, P. 1994. The influence of polyalcohols and carbohydrates on the thermostability of α-amylase. Biotechnol. Bioeng. 43: 107-114.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 107-114
    • DeCordt, S.1    Hendrickx, M.2    Maesmans, G.3    Tobback, P.4
  • 7
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    • Enzyme stabilization: State of the art
    • Gianfreda, L., Scarfi, M. R. 1991. Enzyme stabilization: State of the art. Mol. Cell. Biochem. 100: 97-128.
    • (1991) Mol. Cell. Biochem. , vol.100 , pp. 97-128
    • Gianfreda, L.1    Scarfi, M.R.2
  • 10
    • 0021471834 scopus 로고
    • A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers
    • Henley, J. P., Sadana, A. 1984. A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers. Biotechnol. Bioeng, 26: 959-969.
    • (1984) Biotechnol. Bioeng , vol.26 , pp. 959-969
    • Henley, J.P.1    Sadana, A.2
  • 11
    • 84985225758 scopus 로고
    • Heat inactivation of peroxidase in corn-on-the-cob
    • Lee, Y. C , Hammes, K. 1979. Heat inactivation of peroxidase in corn-on-the-cob. J. Food Sci. 44: 785-788.
    • (1979) J. Food Sci. , vol.44 , pp. 785-788
    • Lee, Y.C.1    Hammes, K.2
  • 12
    • 0023785503 scopus 로고
    • Enzyme stabilization by immobilization
    • Monsan, P., Combes, D. 1988. Enzyme stabilization by immobilization. Methods Enzymol. 137: 584-598.
    • (1988) Methods Enzymol. , vol.137 , pp. 584-598
    • Monsan, P.1    Combes, D.2
  • 13
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    • Models of enzyme deactivation
    • M. N. Gupta (ed.). Narosa Publishing House, New Delhi
    • Sadana, A. 1993. Models of enzyme deactivation. pp. 84-93 In: M. N. Gupta (ed.), Thermostability of enzymes. Narosa Publishing House, New Delhi.
    • (1993) Thermostability of Enzymes , pp. 84-93
    • Sadana, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.