메뉴 건너뛰기




Volumn 94, Issue 3, 2006, Pages 431-440

A kinetic model to explain the maximum in α-amylase activity measurements in the presence of small carbohydrates

Author keywords

amylase activity assay; Ceralpha method; Kinetic model; Maximum activity; Substrate competition; Substrate inhibition

Indexed keywords

CARBOHYDRATES; CATALYSIS; CONCENTRATION (PROCESS); GENETIC ENGINEERING; SUBSTRATES;

EID: 33745223864     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.20779     Document Type: Article
Times cited : (12)

References (16)
  • 1
    • 0017189067 scopus 로고
    • Subsite mapping of enzymes. Application of the depolymerase computer model to two α-amylases
    • Allen JD, Thoma JA. 1976. Subsite mapping of enzymes. Application of the depolymerase computer model to two α-amylases. Biochem J 159:121-132.
    • (1976) Biochem J , vol.159 , pp. 121-132
    • Allen, J.D.1    Thoma, J.A.2
  • 2
    • 0024469173 scopus 로고
    • Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase
    • Asther M, Meunier JC. 1989. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem J 263:665-670.
    • (1989) Biochem J , vol.263 , pp. 665-670
    • Asther, M.1    Meunier, J.C.2
  • 3
    • 33745217641 scopus 로고    scopus 로고
    • The effect of carbohydrate components on α-amylase activity measurements
    • accepted for publication
    • Baks T, Janssen AEM, Boom RM. 2005. The effect of carbohydrate components on α-amylase activity measurements. Enzyme Microb Technol, accepted for publication.
    • (2005) Enzyme Microb Technol
    • Baks, T.1    Janssen, A.E.M.2    Boom, R.M.3
  • 4
    • 25744439914 scopus 로고
    • The large-scale use of enzymes in solution
    • Chaplin MF, Bucke C, editors. Cambridge: Cambridge University Press
    • Chaplin MF, Bucke C. 1990. The large-scale use of enzymes in solution. In: Chaplin MF, Bucke C, editors. Enzyme technology. Cambridge: Cambridge University Press, pp 138-166.
    • (1990) Enzyme Technology , pp. 138-166
    • Chaplin, M.F.1    Bucke, C.2
  • 6
    • 0014943898 scopus 로고
    • Interpreatation of dependency of rate parameters of the degree of polymerization of substrate in enzyme-catalysed reactions. Evaluation of subsite affinities of exo-enzyme
    • Hiromi K. 1970. Interpreatation of dependency of rate parameters of the degree of polymerization of substrate in enzyme-catalysed reactions. Evaluation of subsite affinities of exo-enzyme. Biochem Biophys Res Commun 40:1-6.
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 7
    • 0029095940 scopus 로고
    • Model selection for extended quasi-likelihood models in small samples
    • Hurvich CM, Tsai CL. 1995. Model selection for extended quasi-likelihood models in small samples. Biometrics 51:1077-1084.
    • (1995) Biometrics , vol.51 , pp. 1077-1084
    • Hurvich, C.M.1    Tsai, C.L.2
  • 8
    • 0037042199 scopus 로고    scopus 로고
    • Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates
    • Kandra L, Gyémánt G, Remenyik J, Hovánszki G, Lipták A. 2002. Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates. FEBS lett 518:79-82.
    • (2002) FEBS Lett , vol.518 , pp. 79-82
    • Kandra, L.1    Gyémánt, G.2    Remenyik, J.3    Hovánszki, G.4    Lipták, A.5
  • 9
    • 0024955233 scopus 로고
    • Behavior of enzymes in the presence of carbohydrates. Influence of alcohols, polyols, and carbohydrates on activity and stability of yeast alcohol dehydrogenase
    • Larreta-Garde V, Xu ZF, Thomas D. 1988. Behavior of enzymes in the presence of carbohydrates. Influence of alcohols, polyols, and carbohydrates on activity and stability of yeast alcohol dehydrogenase. Ann NY Acad Sci 542:294-298.
    • (1988) Ann NY Acad Sci , vol.542 , pp. 294-298
    • Larreta-Garde, V.1    Xu, Z.F.2    Thomas, D.3
  • 11
    • 0011817910 scopus 로고
    • Measurement of cereal α-amylase: A new assay procedure
    • McCleary BV, Sheehan H. 1987. Measurement of cereal α-amylase: A new assay procedure. J Cereal Sci 6:237-251.
    • (1987) J Cereal Sci , vol.6 , pp. 237-251
    • McCleary, B.V.1    Sheehan, H.2
  • 12
    • 0036728536 scopus 로고    scopus 로고
    • Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the Ceralpha assay: Collaborative study
    • McCleary BV, McNally M, Monaghan D, Mugford DC. 2002. Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the Ceralpha assay: Collaborative study. J AOAC Int 85:1096-1102.
    • (2002) J AOAC Int , vol.85 , pp. 1096-1102
    • McCleary, B.V.1    McNally, M.2    Monaghan, D.3    Mugford, D.C.4
  • 14
    • 0000304044 scopus 로고
    • A new procedure for the measurement of fungal and bacterial α-amylase
    • Sheehan H, McCleary BV. 1988. A new procedure for the measurement of fungal and bacterial α-amylase. Biotechnol Tech 2:289-292.
    • (1988) Biotechnol Tech , vol.2 , pp. 289-292
    • Sheehan, H.1    McCleary, B.V.2
  • 16
    • 0025678165 scopus 로고
    • Kinetic indication for a conformational change of enzyme by a modified aqueous microenvironment
    • Xu ZF, Thomas D, Larreta-Garde V. 1990. Kinetic indication for a conformational change of enzyme by a modified aqueous microenvironment. Ann NY Acad Sci 613:506-510.
    • (1990) Ann NY Acad Sci , vol.613 , pp. 506-510
    • Xu, Z.F.1    Thomas, D.2    Larreta-Garde, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.