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The inhibition effect of AOT reverse micelles in the p-nitrophenol ester hydrolysis, has been compared with lipases from Pseudomonas sp., and isoespecies A and B from Candida rugosa. These anionic micelles induced a displacement of the optimal pH of lipase in opposite direction to that observed with other hydrophilic non surface-active enzymes. A relation between the hydrophobic character of each...
The immobilization/stabilization of pure and very labile lipases was studied. Two types of lipase-microgels derivatives, which may be used in aqueous and/or organic media were designed and optimized. The first type consisting in the covalent linkage of the protein to the surface of a previously formed microgel. The second type was obtained in a reverse micellar system of AOT. The lipase was microencapsulated...
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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