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J. Biochem, 1977, Vol. 81, No. 5 1209-1215
© 1977 Japanese Biochemical Society

research-article

Studies on Sterol-ester Hydrolase from Fusarium oxysporum

I. Partial Purification and Properties

Yoshio OKAWA1 and Tsutomu YAMAGUCHI

Research Laboratory, Toyo Jozo Co., Ltd. Ohito-cho, Tagata-gun, Shizuoka 410-23

  1. A search for a long chain fatty acyl sterol-ester hydrolase in microorganisms led to the isolation from soil of five strains belonging to Fusarium sp. which produced strong activity in the culture medium.
  2. The cholesterol esterase from Fusarium oxysporum IGH-2 was purified about 270-fold by means of Cacl2 precipitation and Sephadex G-75 column chromatography.
  3. The cholesterol esterase was activated by adekatol and Triton X-l00. It was inhibited by lecithin and lysolecithin, and completely inactivated by heat treatment (60°C for 30 mm, at pH 7.0).
  4. The optimum pH of the enzyme was found to be around 7.0.
  5. Among various cholesterol esters tested, cholesterol linoleate was the most suitable substrate.
  6. Cholesterol esters in serum were also hydrolyzed by this enzyme.

1Present address: Department of Microbiology, Tohoku College of Pharmacy, Komatsushima, Sendai.


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