Studies of the Heterogeneity of a Candida cylindracea (rugosa) Lipase: Monitoring of Esterolytic Activity and Enantioselectivity by Chiral Liquid Chromatography

A method for the determination of lipase activity in terms of rate and enantioselectivity of hydrolysis of a chiral ester substrate has been developed. When this method was applied to fractions, isolated from preparative, column chromatographic separations (anion-exchange, molecular sieve) of the lipase, significant differences in enantioselectivity (E) was found between the fractions. The highest enantioselectivity was found in the first main peak obtained on DEAE-Sepharose chromatography, meaning that the enzyme with the highest isoelectric point shows the highest esterolytic enantioselectivity.

The experimental results are discussed in the light of some earlier reported results and with respect to the possible existence of subunit aggregates and isoenzymes.