Purification of tributyrin esterase fromLactococcus lactissubsp.cremorisE8

Abstract

SummaryA 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.