Esterolytic Activities of Pediococcus Species

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Abstract
Six different strains of Pediococcus pentosaceus and two of Pediococcus acidilactici were examined for intracellular esterolytic enzyme activity. All strains of Pediococcus pentosaceus possessed esterase activity, which was highest in Pediococcus pentosaceus NCDO 559 with .alpha.-naphthyl acetate as substrate. However, no esterolytic activity was found in either strain of Pediococcus acidilactici tested. Esterolytic enzymes in crude cell-free extracts were separated using PAGE and identified by histochemical staining. Substrate specificity toward various .alpha.- and .beta.-naphthyl esters of acetic, propionic, and butyric acids were determined. All strains of Pediococcus pentosaceus exhibited active band(s) of esterase on gels and were most active toward .alpha.-naphthyl acetate. No active esterase band was detected in either strain of Pediococcus acidilactici.