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- W1938348047 abstract "The lipase of Candida parapsilosis catalyses the formation of esters in aqueous media. In addition, the hydrolytic activity of the enzyme has been described in a recent publication as being selective for the 2 position, which is extremely rare. These features led to deeper investigation of the functioning and regioselectivity of the lipase in a biphasic aqueous medium. It is shown that, in addition to hydrolysis, the lipase of C. parapsilosis catalyses an alcoholysis reaction in the strict sense of the term, i.e. the transfer of fatty acyls groups from acylglycerols to various alcohols without direct involvement of water. In the presence of alcohol in the aqueous medium, alcoholysis occurred preferentially to hydrolysis. The enzyme thus displays transferase activity in which the acyl acceptor may be either water or alcohol. This activity is not stereospecific to either the acyl donor or acceptor. Hydrolysis and alcoholysis of monooleoylglycerols, dioleoylglycerols and trioleoylglycerols were studied successively. Investigation of the regiospecificity of alcoholysis in the presence of the lipase of C. parapsilosis showed that the selectivity of hydrolysis for the 2 position was, in fact, only apparent. In certain cases, and particularly when the initial substrate was a triacylglycerol, the similtaneous functioning of the two hydrolysis and alcoholysis reactions led to the appearance of equivalent quantities of 1,2(2,3)-diacylglycerol and 1,3-diacylglycerol in the reaction mixture; this proportion might then be interpreted as the result of selectivity of the hydrolysis reaction for position 2 of the triacylglycerol." @default.
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- W1938348047 date "1995-02-01" @default.
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- W1938348047 title "Functioning and Regioselectivity of the Lipase of Candida Parapsilosis (Ashford) Langeron and Talice in Aqueous Medium. New Interpretation of Regioselectivity Taking Acyl Migration into Account" @default.
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- W1938348047 doi "https://doi.org/10.1111/j.1432-1033.1995.0169o.x" @default.
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