Abstract
An intracellular esterase from Enterococcus faecium ACA-DC 237, isolated from Greek Feta cheese, was purified on DEAE-cellulose and Sephadex G-150. The enzyme had a molecular weight of 45 000, with an optimum activity on 4-nitrophenyl butyrate at pH 8.0 and at 35°C, with K m = 0.85 mM. The esterase was capable of degrading synthetic substrates of low and medium molecular weight (C2 to C12). It was inactivated by PMSF; sulfhydryl group reagents and metal chelators had little or no effect on enzyme activity.
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