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Related Experiment Videos

Lysozyme expression in Lactococcus lactis.

M van de Guchte1, F J van der Wal, J Kok

  • 1Department of Genetics, University of Groningen, Haren, The Netherlands.

Applied Microbiology and Biotechnology
|May 1, 1992
PubMed
Summary

Bacteriophage lysozymes were successfully produced as active proteins in Lactococcus lactis, unlike hen egg white lysozyme. This advancement holds potential for controlling food-spoilage bacteria growth.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Food Science

Background:

  • Lysozymes are enzymes with antimicrobial properties.
  • Expression of eukaryotic and prokaryotic lysozymes in Lactococcus lactis subsp. lactis was investigated.
  • Challenges in achieving active protein folding in microbial hosts are common.

Purpose of the Study:

  • To express eukaryotic (hen egg white lysozyme - HEL) and prokaryotic (bacteriophage T4 and lambda lysozymes) genes in Lactococcus lactis.
  • To assess the biological activity of the expressed lysozymes.
  • To optimize expression levels for potential food applications.

Main Methods:

  • Gene cloning and expression in Lactococcus lactis subsp. lactis.
  • Western blotting for protein detection.
  • Assays for lysozyme activity.
  • Translational coupling strategies for gene expression.

Main Results:

  • Hen egg white lysozyme (HEL) was detected but lacked activity, likely due to incorrect disulfide bond formation.
  • Active T4 and lambda bacteriophage lysozymes were successfully produced in L. lactis.
  • Highest expression of active bacteriophage lysozymes was achieved through translational coupling with a lactococcal open reading frame.

Conclusions:

  • Lactococcus lactis can produce active bacteriophage lysozymes, but struggles with correctly folded eukaryotic lysozymes.
  • Translational coupling is an effective strategy for enhancing active protein expression in L. lactis.
  • Active bacteriophage lysozymes produced in L. lactis show promise for controlling food-spoilage bacteria.

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