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Volumn 34, Issue 5, 2004, Pages 513-522

A mathematical model for glucose oxidase kinetics, including inhibitory, deactivant and diffusional effects, and their interactions

Author keywords

Glucose oxidase kinetics; Inhibitory, deactivant, diffusional effects

Indexed keywords

CATALYSTS; DIFFUSION; ENZYME INHIBITION; ENZYME KINETICS; GLUCOSE; MATHEMATICAL MODELS; MICROBIOLOGY;

EID: 1642289246     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2003.12.003     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 0014027999 scopus 로고
    • Substrate inhibition with glucose oxidase
    • Nicol M.J., Duke F.R. Substrate inhibition with glucose oxidase. J. Biol. Chem. 241(18):1966;4292-4293.
    • (1966) J. Biol. Chem. , vol.241 , Issue.18 , pp. 4292-4293
    • Nicol, M.J.1    Duke, F.R.2
  • 3
    • 0023324607 scopus 로고
    • Time-dependent inactivation of immobilized glucose oxidase and catalase
    • Tse P.H.S., Gough D.A. Time-dependent inactivation of immobilized glucose oxidase and catalase. Biotechnol. Bioeng. 29:1987;705-713.
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 705-713
    • Tse, P.H.S.1    Gough, D.A.2
  • 5
    • 0014197974 scopus 로고
    • The oxidation of 1-deuterated glucose by glucose oxidase
    • Bright H.J., Gibson Q.H. The oxidation of 1-deuterated glucose by glucose oxidase. J. Biol. Chem. 242(5):1967;994-1003.
    • (1967) J. Biol. Chem. , vol.242 , Issue.5 , pp. 994-1003
    • Bright, H.J.1    Gibson, Q.H.2
  • 6
    • 0014254950 scopus 로고
    • Action mechanism of glucose oxidase of Aspergillus niger
    • Nakamura S., Ogura Y. Action mechanism of glucose oxidase of Aspergillus niger. J. Biochem. Tokyo. 63(3):1968;308-316.
    • (1968) J. Biochem. Tokyo , vol.63 , Issue.3 , pp. 308-316
    • Nakamura, S.1    Ogura, Y.2
  • 7
    • 0014958407 scopus 로고
    • Preparation and characterization of glucose oxidase covalently linked to nickel oxide
    • Weetall H.H., Hersh L.S. Preparation and characterization of glucose oxidase covalently linked to nickel oxide. Biochim. Biophys. Acta. 206:1970;54-60.
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 54-60
    • Weetall, H.H.1    Hersh, L.S.2
  • 8
    • 0022160613 scopus 로고
    • Increase in operational stability of immobilized glucose oxidase by the use of an artificial cosubstrate
    • Bourdillon C., Hervagault C., Thomas D. Increase in operational stability of immobilized glucose oxidase by the use of an artificial cosubstrate. Biotechnol. Bioeng. 27:1985;1619-1622.
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 1619-1622
    • Bourdillon, C.1    Hervagault, C.2    Thomas, D.3
  • 9
    • 0024589936 scopus 로고
    • Immobilization of glucose oxidase with Bombyx mori silk fibroin by only stretching treatment and its application to glucose sensor
    • Demura M., Asakura T. Immobilization of glucose oxidase with Bombyx mori silk fibroin by only stretching treatment and its application to glucose sensor. Biotechnol. Bioeng. 33:1989;598-603.
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 598-603
    • Demura, M.1    Asakura, T.2
  • 10
    • 0017134737 scopus 로고
    • Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies
    • Hayashi S., Nakamura S. Comparison of fungal glucose oxidases. Chemical, physicochemical and immunological studies. Biochim. Biophys. Acta. 438:1976;37-48.
    • (1976) Biochim. Biophys. Acta , vol.438 , pp. 37-48
    • Hayashi, S.1    Nakamura, S.2
  • 11
    • 0017270696 scopus 로고
    • The glucose oxidase-catalase system
    • Wood WA, editor. New York: Academic Press
    • Bouin JC, Atallah MT, Hultin HO. The glucose oxidase-catalase system. In: Wood WA, editor. Methods in enzymology, vol. 44. New York: Academic Press, 1977. p. 478-88.
    • (1977) Methods in Enzymology , vol.44 , pp. 478-488
    • Bouin, J.C.1    Atallah, M.T.2    Hultin, H.O.3
  • 12
    • 0026863987 scopus 로고
    • Enzyme immobilization on a low-cost magnetic support: Kinetic studies on immobilized and coimmobilized glucose oxidase and glucoamylase
    • Pieters B.R., Bardeletti G. Enzyme immobilization on a low-cost magnetic support: kinetic studies on immobilized and coimmobilized glucose oxidase and glucoamylase. Enzyme Microb. Technol. 14:1992;361-370.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 361-370
    • Pieters, B.R.1    Bardeletti, G.2
  • 15
    • 0000475128 scopus 로고
    • Purification and properties of the glucose oxidase from Aspergillus niger
    • Swoboda B.E.P., Massey V. Purification and properties of the glucose oxidase from Aspergillus niger. J. Biol. Chem. 240(5):1965;2209-2215.
    • (1965) J. Biol. Chem. , vol.240 , Issue.5 , pp. 2209-2215
    • Swoboda, B.E.P.1    Massey, V.2
  • 16
    • 1642348797 scopus 로고
    • Kinetic studies of gluconic acid fermentation, using Aspergillus niger
    • Miura Y., Tsuchiya K., Tsusho H., Miyamoto K. Kinetic studies of gluconic acid fermentation, using Aspergillus niger. J. Ferment. Technol. 48(12):1970;795-803.
    • (1970) J. Ferment. Technol. , vol.48 , Issue.12 , pp. 795-803
    • Miura, Y.1    Tsuchiya, K.2    Tsusho, H.3    Miyamoto, K.4
  • 18
    • 0024707969 scopus 로고
    • Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger
    • Takegawa K., Fujiwara K., Iwahara S., Yamamoto K., Tochikura T. Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger. Biochem. Cell Biol. 67:1989;460-464.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 460-464
    • Takegawa, K.1    Fujiwara, K.2    Iwahara, S.3    Yamamoto, K.4    Tochikura, T.5
  • 19
    • 11944250028 scopus 로고
    • Covalent electropolymerization of glucose oxidase in polypyrrole
    • Wolowacz S.E., Yon Hin B.F.Y., Lowe C.R. Covalent electropolymerization of glucose oxidase in polypyrrole. Anal. Chem. 64:1992;1541-1545.
    • (1992) Anal. Chem. , vol.64 , pp. 1541-1545
    • Wolowacz, S.E.1    Yon Hin, B.F.Y.2    Lowe, C.R.3
  • 20
    • 0013636670 scopus 로고
    • Kinetic studies on the action of glucose oxidase
    • Nakamura T., Ogura Y. Kinetic studies on the action of glucose oxidase. J. Biochem. Tokyo. 52(3):1962;214-220.
    • (1962) J. Biochem. Tokyo , vol.52 , Issue.3 , pp. 214-220
    • Nakamura, T.1    Ogura, Y.2
  • 21
    • 0015214394 scopus 로고
    • Interaction of D-glucal with Aspergillus niger glucose oxidase
    • Rogers M.J., Brandt K.G. Interaction of D-glucal with Aspergillus niger glucose oxidase. Biochemistry. 10(25):1971;4624-4630.
    • (1971) Biochemistry , vol.10 , Issue.25 , pp. 4624-4630
    • Rogers, M.J.1    Brandt, K.G.2
  • 22
    • 0032103106 scopus 로고    scopus 로고
    • Biotransformation of glucose to free gluconic acid by Gluconobacter oxydans: Substrate and product inhibition situations
    • Velizarov S., Beschkov V. Biotransformation of glucose to free gluconic acid by Gluconobacter oxydans: substrate and product inhibition situations. Process Biochem. 33(5):1998;527-534.
    • (1998) Process Biochem. , vol.33 , Issue.5 , pp. 527-534
    • Velizarov, S.1    Beschkov, V.2
  • 23
    • 0002941117 scopus 로고
    • Glucose transforming enzymes
    • Fogarty WM, Kelly CT, editors. New York: Elsevier
    • Crueger A, Crueger W. Glucose transforming enzymes. In: Fogarty WM, Kelly CT, editors. Microbial enzymes and biotechnology. New York: Elsevier, 1990. p. 177-226.
    • (1990) Microbial Enzymes and Biotechnology , pp. 177-226
    • Crueger, A.1    Crueger, W.2
  • 24
    • 0023324608 scopus 로고
    • Determination of the intrinsic kinetic constants of immobilized glucose oxidase and catalase
    • Tse P.H.S., Leypoldt J.K., Gough D.A. Determination of the intrinsic kinetic constants of immobilized glucose oxidase and catalase. Biotechnol. Bioeng. 29:1987;696-704.
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 696-704
    • Tse, P.H.S.1    Leypoldt, J.K.2    Gough, D.A.3
  • 25
    • 0014239163 scopus 로고
    • Comparative studies on the glucose oxidases of Aspergillus niger and Penicillium amagasakiense
    • Nakamura S., Fujiki S. Comparative studies on the glucose oxidases of Aspergillus niger and Penicillium amagasakiense. J. Biochem. Tokyo. 63(1):1968;51-58.
    • (1968) J. Biochem. Tokyo , vol.63 , Issue.1 , pp. 51-58
    • Nakamura, S.1    Fujiki, S.2
  • 26
    • 0019880351 scopus 로고
    • Multiple forms of glucose oxidase with different carbohydrate compositions
    • Hayashi S., Nakamura S. Multiple forms of glucose oxidase with different carbohydrate compositions. Biochim. Biophys. Acta. 657:1981;40-51.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 40-51
    • Hayashi, S.1    Nakamura, S.2
  • 27
    • 0037015415 scopus 로고    scopus 로고
    • Diauxic production of glucose oxidase by Aspergillus niger in submerged culture: A dynamic model
    • Mirón J., González M.P., Pastrana L., Murado M.A. Diauxic production of glucose oxidase by Aspergillus niger in submerged culture: a dynamic model. Enzyme Microb. Technol. 31:2002;615-620.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 615-620
    • Mirón, J.1    González, M.P.2    Pastrana, L.3    Murado, M.A.4
  • 28
    • 0014576376 scopus 로고
    • An improved method for enzymic determination of glucose in the presence of maltose
    • Lloyd J.B., Whelan W.J. An improved method for enzymic determination of glucose in the presence of maltose. J. Anal. Biochem. 30:1969;467-470.
    • (1969) J. Anal. Biochem. , vol.30 , pp. 467-470
    • Lloyd, J.B.1    Whelan, W.J.2
  • 29
    • 0022880775 scopus 로고
    • Screening and mutagenesis of moulds for the improvement of glucose oxidase production
    • Fiedurek J., Rogalski J., Ilczuk Z., Leonowcz A. Screening and mutagenesis of moulds for the improvement of glucose oxidase production. Enzyme Microb. Technol. 8:1986;734-736.
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 734-736
    • Fiedurek, J.1    Rogalski, J.2    Ilczuk, Z.3    Leonowcz, A.4
  • 30
    • 0014963343 scopus 로고
    • Purification and properties of yeast amylo-1,6-glucosidase-oligo-1, 4→1,4-glucantransferase
    • Lee E.Y.C., Carter J.H., Nielsen L.D., Fisher E.H. Purification and properties of yeast amylo-1,6-glucosidase-oligo-1,4→1,4-glucantransferase. Biochemistry. 9(11):1970;2347-2355.
    • (1970) Biochemistry , vol.9 , Issue.11 , pp. 2347-2355
    • Lee, E.Y.C.1    Carter, J.H.2    Nielsen, L.D.3    Fisher, E.H.4
  • 31
    • 0342313809 scopus 로고
    • D-Gluconate
    • Bergmeyer HU, editor. New York: Academic Press
    • Möllering H, Bergmeyer HU. D-Gluconate. In: Bergmeyer HU, editor. Methods of enzymatic analysis, vol. 3. New York: Academic Press, 1974. p. 1243-7.
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1243-1247
    • Möllering, H.1    Bergmeyer, H.U.2
  • 32
    • 0030571611 scopus 로고    scopus 로고
    • Modeling substrate inhibition of microbial growth
    • Tan Y., Wang Z.-X., Marshall K.C. Modeling substrate inhibition of microbial growth. Biotechnol. Bioeng. 52:1996;602-608.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 602-608
    • Tan, Y.1    Wang, Z.-X.2    Marshall, K.C.3
  • 33
    • 0026111222 scopus 로고
    • Mass transfer control of enzymatic hydrolysis of polysaccharides by glucoamylase
    • Miranda M., Murado M.A., Sanromán A., Lema J.M. Mass transfer control of enzymatic hydrolysis of polysaccharides by glucoamylase. Enzyme Microb. Technol. 13:1991;142-147.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 142-147
    • Miranda, M.1    Murado, M.A.2    Sanromán, A.3    Lema, J.M.4
  • 34
    • 0001376321 scopus 로고    scopus 로고
    • The influence of substrate structure on the kinetics of the hydrolysis of starch by glucoamylase
    • Sanromán A., Murado M.A., Lema J.M. The influence of substrate structure on the kinetics of the hydrolysis of starch by glucoamylase. Appl. Biochem. Biotechnol. 59:1996;329-336.
    • (1996) Appl. Biochem. Biotechnol. , vol.59 , pp. 329-336
    • Sanromán, A.1    Murado, M.A.2    Lema, J.M.3
  • 35
    • 0031908985 scopus 로고    scopus 로고
    • A new device for measuring diffusional restrictions and modelling substrate inhibition in a starch-glucoamylase system
    • Pastrana L.M., González M.P., Mirón J., Murado M.A. A new device for measuring diffusional restrictions and modelling substrate inhibition in a starch-glucoamylase system. Biotechnol. Lett. 20(2):1998;127-130.
    • (1998) Biotechnol. Lett. , vol.20 , Issue.2 , pp. 127-130
    • Pastrana, L.M.1    González, M.P.2    Mirón, J.3    Murado, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.