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Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8

Published online by Cambridge University Press:  01 June 2009

Ross Holland
Affiliation:
Neiv Zealand Dairy Research Institute, Private Bag 11029, Palmerston North, New Zealand
Tim Coolbear
Affiliation:
Neiv Zealand Dairy Research Institute, Private Bag 11029, Palmerston North, New Zealand

Summary

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 °C, and had a half life of 1 h at 50 °C.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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