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The conformational and functional changes of cholesterol esterase (CE) and isolipase (CRL) from Candida rugosa after exposure to a micellar interface and subsequent extraction to a fresh buffer were studied. These two enzymes were activated by interaction with the micellar interface of a sulphosuccinic acid bis[2-ethylhexyl] ester/n-heptane/water system. For the hydrolysis of p-nitrophenyl butyrate...
Two isoenzymes of Candida rugosa lipase, having the same mol.wt., size and similar aminoacid sequence, were studied in reverse micelles of AOT. The results demonstrated the relevance of lipase hydrophobicity in reactions in anionic micelles. This is a key factor in mitigating the inhibition effect of charged micelles. The more hydrophobic isolipase A was a better biocatalyst for hydrolytic processes...
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