Peculiar properties of lipase fromCandida parapsilosis (Ashford) langeron and talice |
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| Authors: | A. Riaublanc R. Ratomahenina P. Galzy M. Nicolas |
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| Affiliation: | (1) Chaire de Microbiologie Industrielle et de Génétique des Microorganismes, INRA-ENSA, Place Viala, 34060 Montpellier Cedex 1, France;(2) INSERM-U65, Immunologie, Institut de Biologie, 34000 Montpellier, France |
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| Abstract: | A newCandida 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. |
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| Keywords: | Candida parapsilosis 1,3 diglycerides esterase esters lipase lipids monoglycerides specificity synthesis |
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