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In situ assay of intracellular enzymes of yeast (Kluyveromyces fragilis) by digitonin permeabilization of cell membrane.

Gowda, L. R. and Joshi, M. S. and Bhat, S. G. (1988) In situ assay of intracellular enzymes of yeast (Kluyveromyces fragilis) by digitonin permeabilization of cell membrane. Analytical Biochemistry, 175 (2). pp. 531-6. ISSN 0003-2697

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Abstract

The yeast, Kluyveromyces fragilis was permeabilized to a number of low-molecular-weight substrates using digitonin. The activities of intracellular yeast enzymes, viz., alcohol dehydrogenase (ADH), beta-galactosidase, glucose-6-phosphate dehydrogenase, aspartase, and hexokinase were found to be much higher in the permeabilized cells than the untreated cells. The optimum conditions for permeabilization with reference to ADH were 0.1% digitonin at 37 degrees C for 15 min. The ADH activity in permeabilized cells was several-fold higher than that in cell free extracts prepared by either physical or chemical methods.

Item Type: Article
Uncontrolled Keywords: Kluyveromyces fragilis, permeabilization, digitonin, intracellular enzymes
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 19 Yeast
600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 01 Jun 2011 09:53
Last Modified: 01 Oct 2018 09:23
URI: http://ir.cftri.com/id/eprint/2365

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