Purification and characterization of mono-and diacylglycerol lipase isolated from Penicillium camembertii U-150 |
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Authors: | Shotaro Yamaguchi Tamio Mase |
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Affiliation: | (1) Research andelopment Division, Amano Pharmaceutical Co., Ltd., Nishiharu-cho, 481 Nishikasugai-gun, Aichi, Japan;(2) Present address: Tsukuba Research Laboratories, Amano Pharmaceutical Co. Ltd., 22 Miyukigaoka, 305 Tsukuba, Ibaragi, Japan |
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Abstract: | Summary A novel enzyme hydrolysing mono- and diacylglycerol was found in the culture filtrate of an isolated fungus, Penicillium camembertii. The enzyme was separated into two forms (A- and B-enzyme) with almost the same molecular weight (37,000–39,000), amino acid composition and identical N-terminal amino acid sequence. B-Enzyme, a major component, was purified approximately 210-fold with an activity yield of 2.6%. The B-enzyme was specific to mono- and diacylglycerols and hydrolysed long-chain monoacylglycerols most efficiently. Triacylglycerols were completely inert as substrates for the enzyme. The B-enzyme preferred to attack -position to -position of monoacylglycerol, but showed no stereospecificity on mono- and diacylglycerol. Both Fe3+ and Hg2+ inhibited B-enzyme activity significantly.Offprint requests to: S. Yamaguchi |
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