A tributyrin esterase was antiseptic from Lactococcus lactis subsp. cremoris E8 application FPLC chromatography. This was the above esterase action empiric in ache E8 and was associated with a individual protein with a subunit atomic accumulation of 29 kDa and a holoenzyme of atomic accumulation 109 kDa. The agitator was alive adjoin tributyrin and p-nitrophenyl butyrate. The N-terminal arrangement of the agitator was determined. The agitator had a pH optimum in the aloof range, was abiding on freezing at −20 °C, and had a bisected activity of 1 h at 50 °C.