Abstract
The substrate protection effect on an enzyme in a reversible reaction was studied by using glucose isomerase immobilized in small particles (radius less than 100 micron). Deactivation of the enzyme at various substrate concentrations in Tris buffer, pH 8.25, at 62.1 degrees C was studied in eight-column reactor sets. At set times the immobilized enzyme in one of the eight reactors was taken out and rinsed thoroughly, and then its residual activity was determined. The conclusions are, first, that the protection by the reactant is equal to the protection by the product, and, secondly, that the half-life of the enzyme increases slowly at high sugar concentrations. Thus the experimental method described here appears to be a useful one for the determination of substrate protection of enzyme deactivation in reversible reactions.
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Selected References
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- Adler D., Lim H., Cottle D., Emery A. Proteolytic denaturation and methods of improving the stability of glucose isomerase preparations. Biotechnol Bioeng. 1979 Aug;21(8):1345–1359. doi: 10.1002/bit.260210804. [DOI] [PubMed] [Google Scholar]
- Cardoso J. P., Emery A. N. A new model to describe enzyme inactivation. Biotechnol Bioeng. 1978 Sep;20(9):1471–1477. doi: 10.1002/bit.260200913. [DOI] [PubMed] [Google Scholar]
- Ollis D. F. Diffusion influences in denaturable insolubilized enzyme catalysts. Biotechnol Bioeng. 1972 Nov;14(6):871–884. doi: 10.1002/bit.260140603. [DOI] [PubMed] [Google Scholar]
- Sproull R. D., Lim H. C., Schneider D. R. A model for enzymatic isomerization of D-glucose to D-fructose in a batch reactor. Biotechnol Bioeng. 1976 May;18(5):633–648. doi: 10.1002/bit.260180504. [DOI] [PubMed] [Google Scholar]