Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.
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.
Holland
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New Zealand Dairy Research Institute, Palmerston North, New Zealand.
Coolbear
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D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D013294:Lactococcus lactis / Q000201:enzymology*; D008049:Lipase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature
D008049:Lipase