Studies on sterol-ester hydrolase from Fusarium oxysporum. I. Partial purification and properties.
Studies on sterol-ester hydrolase from Fusarium oxysporum. I. Partial purification and properties.
复制标题
尖孢镰刀菌甾醇酯水解酶的研究。
DOI:
10.1093/oxfordjournals.jbchem.a131571
复制
发表时间:
1977
影响因子:
2.7
通讯作者:
T. Yamaguchi
中科院分区:
文献类型:
--
作者:
Y. Okawa;T. Yamaguchi
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-100. It was inhibited by lecithin and lysolecithin, and completely inactivated by heat treatment (60 degrees C for 30 min, 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.