Substrate Specificity and Mode of Action of the Lipase Produced by Pseudomonas fragi22.39 B |
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Authors: | Toshiyuki Nishio Takahide Chkano Minoru Kamimura |
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Affiliation: | 1. Research &2. Development Laboratories, Sapporo Breweries Ltd., 10 Okatohme, Yaizu, Shizuoka 425, Japan |
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Abstract: | The lipase purified from Pseudomonas fragi 22.39 B hydrolyzed not only triglycerides but also synthetic esters such as Tween, Span and methyl oleate. Of the saturated monoacid triglycerides tested, tributyrin was hydrolyzed most quickly. The lipase did not produce 1,3-diolein as a hydrolysis product from triolein. The addition of the Ca2+ ion to the reaction mixture promoted the hydrolysis rate for triglycerides and monoesters with longer-chain fatty acids (C14, C16, C18). The enzyme could hydrolyze various kinds of natural fats and oils, and the extent their hydrolysis reached above 90%. |
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