02150nas a2200253   4500008004100000022001400041245011200055210006900167260005700236300001400293490000700307520127000314653002801584653002401612653000901636653001301645653002101658100001501679700001901694700001801713700002001731700002401751856012101775       2013                        eng d  a0959-399300aProduction, purification and characterization of cholesterol oxidase from a newly isolated streptomyces sp.0 aProduction purification and characterization of cholesterol oxid  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcNOV  a2077-20850 v293 a<p>Cholesterol oxidase production (COD) by a new isolate characterized as Streptomyces sp. was studied in different production media and fermentation conditions. Individual supplementation of 1 % maltose, lactose, sucrose, peptone, soybean meal and yeast extract enhanced COD production by 80-110 % in comparison to the basal production medium (2.4 U/ml). Supplementation of 0.05 % cholesterol (inducer) enhanced COD production by 150 %. COD was purified 14.3-fold and its molecular weight was found to be 62 kDa. V-max (21.93 mu M/min mg) and substrate affinity K-m (101.3 mu M) suggested high affinity of the COD for cholesterol. In presence of Ba2+ and Hg2+ the enzyme activity was inhibited while Cu2+ enhanced the activity nearly threefold. Relative activity of the enzyme was found maximum in triton X-100 whereas sodium dodecyl sulfate inactivated the enzyme. The enzyme activity was also inhibited by the thiol-reducing reagents like Dithiothreitol and beta-mercaptoethanol. The COD showed moderate stability towards all organic solvents except acetone, benzene and chloroform. The activity increased in presence of isopropanol and ethanol. The enzyme was most active at pH 7 and 37 A degrees C temperature. This organism is not reported to produce COD.</p>10aAffinity chromatography10aCholesterol oxidase10aHPLC10aSDS PAGE10aStreptomyces sp.1 aNiwas, Ram1 aSingh, Vineeta1 aSingh, Rajbir1 aTripathi, Divya1 aTripathi, C., K. M.  uhttps://library.ncl.res.in/content/production-purification-and-characterization-cholesterol-oxidase-newly-isolated-0