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Peculiar properties of lipase from Candida parapsilosis (Ashford) langeron and talice
Author(s) -
Riaublanc A.,
Ratomahenina R.,
Galzy P.,
Nicolas M.
Publication year - 1993
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02542583
Subject(s) - lipase , chemistry , hydrolysis , candida parapsilosis , glyceride , candida antarctica , chromatography , polyunsaturated fatty acid , column chromatography , gel permeation chromatography , esterase , triolein , enzyme , organic chemistry , fatty acid , antifungal , biology , microbiology and biotechnology , polymer
A new Candida parapsilosis lipase was isolated and studied. This enzyme was purified by hydrophobic chromatography on a phenyl‐sepharose CL4B column followed by gel permeation on a Sephacryl S300 HR column. It was a 160 kg·mol −1 molecular‐weight oligomeric enzyme. Optimal activity was obtained at 45°C and pH 6.5. The lipase activity toward various acylglycerols and esters was studied. The hydrolysis rate was greater for secondary acylesters than for primary acylesters. This lipase showed a high specificity for long‐chain fatty acids and particularly for polyunsaturated fatty acids. This enzyme was able to catalyze the synthesis of various oleoylesters in aqueous medium.