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Macrokinetics and operational stability of immobilized glucose oxidase and catalase
Author(s) -
Buchholz K.,
Gödelmann B.
Publication year - 1978
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260200807
Subject(s) - glucose oxidase , chemistry , catalase , diffusion , reaction rate , enzyme , oxidase test , immobilized enzyme , kinetics , reaction–diffusion system , biochemistry , combinatorial chemistry , catalysis , thermodynamics , physics , quantum mechanics
Glucose oxidation by immobilized glucose oxidase (GlO) and catalase (Cat) has been investigated in batch and continuous reactions for operational studies. The macrokinetics of the process depend on coupled reaction steps and diffusion rates. The problem may be approximated by a simple pseudohomogeneous model taking into account both substrates of glucose oxidase and the intermediate reaction product H 2 O 2 . The effectiveness of both enzymes is enhanced in the coupled reaction path, the overall effectiveness nevertheless is very low. H 2 O 2 causes the inactivation of both GlO and Cat. The rates of deactivation depend on the oxidation rates of glucose that give different quasistationary levels of H 2 O 2 concentration. As a first approximation, the deactivation rates may be described by first‐order reactions with respect to H 2 O 2 .