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The esterase profile of a lipase from Candida cylindracea
M C Brahimi-Horn1, M L Guglielmino, L Elling
1Commonwealth Scientific and Industrial Research Organization, Division of Wool Technology, Parkvill Laboratory, Australia.
Abstract:
A commercial preparation of a lipase produced by Candida cylindracea catalysed the hydrolysis of both long- and short-chain esters of p-nitrophenol. Six major bands of hydrolytic activity to alpha-naphthyl acetate were detected on polyacrylamide gel electrophoresis and two on isoelectric focusing. The esterase activity fractionated into two major peaks of activity on ion-exchange chromatography and into several peaks of activity on hydrophobic interaction chromatography. These esterase activities showed different substrate specificities to p-nitrophenyl esters, tributyrin and cetyl palmitate.