Cholesterol esterase produced by Streptomyces lavendulae.

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Abstract
Cholesterol esterase was purified from the culture filtrate of S. lavendulae by a procedure involving precipitation with (NH4)2SO4 and acetone, gel filtration on Sepharose CL-4B and rechromatography on Sepharose CL-4B after treatment of Triton X-100. The purified enzyme was detected as a single band by polyacrylamide disc electrophoresis, while 1 main band and 3 minor bands were observed by SDS [sodium dodecyl sulfate] gel electrophoresis. The MW of the main band was 29,000. The enzyme was inhibited by Hg2+, Ag+ and DFP [diisopropylfluorophosphate]. Long-chain fatty acid esters of cholesterol were hydrolyzed preferentially and pH optimum was 6.0. This enzyme could be used for the determination of total serum cholesterol with cholesterol oxidase from S. violascens.

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