Esterolytic and Lipolytic Activities of Lactobacillus Casei‐subsp‐Casei LLG

The estcrolytic and lipolytic enzymes were produced by cell lysis of Lactobacillus casei‐subsp‐casei LLG during the late logarithmic growth phase. The enzyme was purified to 67 fold by ion exchange chromatography and gel filtration chromatography using the FPLC system. Polyacrylamide gel electrophoresis and sodium dodecyl sulfate‐poly‐acrylamide gel electrophoresis using the “Phast” system of the purified enzyme showed a single protein band for butyrate‐esterase (3.2 × 10 5 Dalton), caproate esterase (1.1 × 10 5 Dalton) and capryate esterase (4.0 × 10 4 Dalton), respectively. The maximum lipolytic activity was observed at pH 7.2 and 37°C. The enzyme activity was inhibited by silver and mercury ions but magnesium and calcium stimulated lipolytic activity. The Km and Vmax values for esterase‐lipase of the strain LLG were 76 μM/min/mg of protein, and 0.57 mM, respectively. This enzyme was stable at room temperature for at least 2 days.