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Determination of intrinsic parameters for immobilization reactions of catalase and amyloglucosidase in porous glass supports
Author(s) -
Hossain Md. M.,
Do D. D.
Publication year - 1988
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.260310716
Subject(s) - catalase , porosity , chemistry , amylase , chemical engineering , porous glass , immobilized enzyme , chromatography , enzyme , biochemistry , organic chemistry , engineering
Experiments have been carried out for immobilizing enzyme‐catalase and amyloglucosidase in controlled‐pore glass particles of two different pore sizes. The experimental results have been analyzed, initial‐stage analysis for the rate parameters of immobilization reactions and long‐time analysis for determining the evolution of the immobilization process. These investigations suggest that the overall process of immobilization is controlled by the restricted diffusion of enzymes into the pores of the support. As a result, immobilized enzyme (IME) can penetrate only up to a certain distance into the support. The penetration depth of IME for the support–enzyme system mentioned have been evaluated from the experimental bulk enzyme concentration data in a batch recirculation reactor.