Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.
作者信息
Holland R, Coolbear T
机构信息
New Zealand Dairy Research Institute, Palmerston North, New Zealand.
出版信息
J Dairy Res. 1996 Feb;63(1):131-40. doi: 10.1017/s0022029900031605.
PMID:8655738
Abstract
A tributyrin esterase was purified from Lactococcus lactis subsp. cremoris E8 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 and p-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 degrees C, and had a half life of 1 h at 50 degrees C.
摘要
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