Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 369946
Title Preparation and some properties of cholesterol oxidase from Rhodococcus sp. R14-2
Author(s) Wang, C.T.; Cao, Y.P.; Sun, B.G.; Ji, B.P.; Nout, M.J.R.; Wang, J.; Zhao, Y.H.
Source World Journal of Microbiology and Biotechnology 24 (2008)10. - ISSN 0959-3993 - p. 2149 - 2157.
DOI https://doi.org/10.1007/s11274-008-9722-6
Department(s) Food Microbiology Laboratory
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2008
Keyword(s) extracellular 3beta-hydroxysteroid oxidase - brevibacterium-sterolicum - streptomyces-sp - purification - gene - erythropolis - oxidation - sequence - enzyme
Abstract Rhodococcus sp. R14-2, isolated from Chinese Jin-hua ham, produces a novel extracellular cholesterol oxidase (COX). The enzyme was extracted from fermentation broth and purified 53.1-fold based on specific activity. The purified enzyme shows a single polypeptide band on SDS-PAGE with an estimated molecular weight of about 60 kDa, and has a pI of 8.5. The first 10 amino acid residues of the NH2-terminal sequence of the enzyme are A-P-P-V-A-S-C-R-Y-C, which differs from other known COXs. The enzyme is stable over a rather wide pH range of 4.0¿10.0. The optimum pH and temperature of the COX are pH 7.0 and 50°C, respectively. The COX rapidly oxidizes 3ß-hydroxysteroids such as cholesterol and phytosterols, but is inert toward 3¿-hydroxysteroids. Thus, the presence of a 3ß-hydroxyl group appears to be essential for substrate activity. The Michaelis constant (Km) for cholesterol is estimated at 55 ¿M; the COX activity was markedly inhibited by metal ions such as Hg2+ and Fe3+ and inhibitors such as p-chloromercuric benzoate, mercaptoethanol and fenpropimorph. Inhibition caused by p-chloromercuric benzoate, mercuric chloride, or silver nitrate was almost completely prevented by the addition of glutathione. These suggests that -SH groups may be involved in the catalytic activity of the present COX
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