Purification of tributyrin esterase fromLactococcus lactissubsp.cremorisE8

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Abstract
Summary: A tributyrin esterase was purified fromLactococcus lactissubsp.cremorisE8 using FPLC chromatography. This was the major esterase activity observed in strain E8 and was associated with a single protein with a subunit molecular mass of 29 kDa and a holoenzyme of molecular mass 109 kDa. The enzyme was active against tributyrin andp-nitrophenyl butyrate. The N-terminal sequence of the enzyme was determined. The enzyme had a pH optimum in the neutral range, was stable on freezing at −20 °C, and had a half life of 1 h at 50 °C.