ISOLATION AND PARTIAL CHARACTERIZATION OF AN INTRACELLULAR ESTERASE FROM ENTEROCOCCUS-FAECIUM ACA-DC-237

An intracellular esterase from Enterococcus faecium ACA-DC 237, isolat ed 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 a ctivity on 4-nitrophenyl butyrate at pH 8.0 and at 35 degrees C, with K-m = 0.85 mM. The esterase was capable of degrading synthetic substra tes 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.