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Related Experiment Videos

Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8

R Holland1, T Coolbear

  • 1New Zealand Dairy Research Institute, Palmerston North, New Zealand.

The Journal of Dairy Research
|February 1, 1996
PubMed
Summary

Researchers purified a key tributyrin esterase enzyme from Lactococcus lactis subsp. cremoris E8. This enzyme shows significant activity and stability, offering potential applications in various biotechnological processes.

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Area of Science:

  • Microbiology
  • Enzymology
  • Biochemistry

Background:

  • Lactococcus lactis subsp. cremoris E8 produces esterase activity.
  • Esterases are crucial enzymes in various industrial applications.

Purpose of the Study:

  • To purify and characterize the major esterase from Lactococcus lactis subsp. cremoris E8.
  • To determine the biochemical properties and N-terminal sequence of the purified esterase.

Main Methods:

  • Fast protein liquid chromatography (FPLC) for enzyme purification.
  • Enzyme activity assays using tributyrin and p-nitrophenyl butyrate.
  • Determination of molecular mass, pH optimum, and thermal stability.

Main Results:

  • A single esterase protein with a subunit molecular mass of 29 kDa and a holoenzyme of 109 kDa was purified.

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  • The enzyme exhibited activity against tributyrin and p-nitrophenyl butyrate.
  • Optimal activity was observed in the neutral pH range, with good stability at -20°C and a half-life of 1 hour at 50°C.

    • Conclusions:

    • The purified esterase from Lactococcus lactis subsp. cremoris E8 is a stable and active enzyme.
    • Its properties suggest potential utility in food processing and other biotechnological fields.