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A carboxylesterase that hydrolyzes Ml-236B (compactin) to Ml-236A (Ml-236B esterase) has been extracted from mycelia of Emericella unguis and purified to homogeneity by successive ammonium sulfate fractionation, chromatography on DEAE-cellulose, gel filtration on Sephadex G-75 and preparative gel electrophoresis. The molecular weight of the purified enzyme was found to be ~ 40,000 and its optimum pH to be around 8. Of the β-nitrophenylesters with different C-chain lengths tested, β-nitrophenylbutyrate (C4) was the best substrate for the enzyme. Since Ml-236B is an α-methylbutyryl ester of M1–236A, the data suggest that the E. unguis esterase is highly specific for the C4-chain length, p-Naphthylacetate, tributyrin, olive oil and casein were not hydrolyzed. The Ml-236B esterase was sensitive to 7V-ethylmaleimide and the organophosphate, DDVP, but resistant to eserine (carbamate), NaF and EDTA.

Purification and properties of carboxylesterase from Emericella unguis that catalyzes the conversion of ML-236B (compactin) to ML-236A.