A novel method of determination of the internal enzyme distribution within porous solid supports and the deactivation rate constant

D. D. Do, M. M. Hossain

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

This article presents a method for determining the rate constant for deactivation and the internal distribution of immobilized enzyme. This method makes use of the parallel deactivation process in a diffusion‐controlled regime, in which the internal activity profile behaves like a penetration front. This front basically traces through the initial active enzymatic profile, and one can determine the internal profile and the rate constant for deactivation from the experimentally observable bulk concentration versus time. This method is applied to the experimental data of the system of hydrogen‐peroxide‐immobilized catalase on controlled pore glass and Si–Al particles.

Original languageEnglish
Pages (from-to)486-493
Number of pages8
JournalBiotechnology and Bioengineering
Volume28
Issue number4
DOIs
Publication statusPublished - Apr 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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