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PubMed · 8655738

Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.

R Holland·T Coolbear
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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.

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Amino Acid SequenceChromatography, High Pressure LiquidEnzyme StabilityHydrogen-Ion ConcentrationLactococcus lactisLipaseMolecular Sequence DataMolecular WeightSubstrate SpecificityTemperatureJournal ArticleResearch Support, Non-U.S. Gov't

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R Holland, T Coolbear. 1996. Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.. https://doi.org/10.1017/s0022029900031605

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