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Diffusion influences in denaturable insolubilized enzyme catalysis
Author(s) -
Ollis David F.
Publication year - 1972
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.260140603
Subject(s) - diffusion , michaelis–menten kinetics , enzyme , chemistry , catalysis , yield (engineering) , thermal stability , immobilized enzyme , enzyme catalysis , thermodynamics , enzyme assay , porosity , chromatography , chemical engineering , biochemistry , organic chemistry , physics , engineering
Abstract The influence of diffusion on the apparent thermal stability of a reversibly or irreversibly denaturable enzyme is examined theoretically when he enzyme is uniformly distributed in a porous solid. If the overall reaction rate is influenced by diffusion through the catalyst, the insolubilized catalyst is shown to yield an apparently more thermally stable enzyme even though the maximal velocity V m , and the Michaelis constant, K m , are the same for the free and insolubilized forms of enzyme. Brief consideration is given to the experimental conditions needed to clearly demonstrate whether insolubilization does or does not effect the thermal stability of the enzyme.