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Physicochemical Properties of Mono- and Diacylglycerol Lipase from Penicillium camembertii
Isobe, K. Nokihara, Kiyoshi
Isobe, K.
Nokihara, Kiyoshi
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
In the course of investigations on the enzymatic synthesis of monoglycerides and the partial hydrolysis of glycerides, Yamaguchi and Mase found a newlipase havingstrict specificity to mono- and diacylglycerols but not to triacylglycerols in the culture broth of Penicillium camembertii U-150 (1). The newlipase was purified into four active fractions by a procedure involving ethanol precipitation, ammanium sulfate fractionation, and aminooctyl-Sepharose, hydroxyapatite and concanavalin A-Sepharose (con A Sepharose) column chromatographies. One active fraction, enzyme 1, was not adsorbed on con A-Sepharose but others, enzymes 2- 4, were adsorbed on con A Sepharose and separated into three active fractions by linear gradient elution with Methyl-X-D-glycopyranoside. No significant difference was observed in substrate specificity among enzymes 1-4, but other enzymatic properties, e. g., pH and heatstabilities, and optimum pH and temperature, were clearly different between enzyme 1 and three adsorbed components (three adsorbed components weresimilar to each other)(2). In oder to elusidate multiple forms of this enzyme, the physicochemical properties were compared among four active components.
Citation
Lipases : structure, mechanism and genetic engineering, 345 - 348
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International