Applied Microbiology and Biotechnology

, Volume 73, Issue 1, pp 158–165 | Cite as

Expression of the sweet-tasting plant protein brazzein in Escherichia coli and Lactococcus lactis: a path toward sweet lactic acid bacteria

  • Aleš Berlec
  • Zala Jevnikar
  • Andreja Čanžek Majhenič
  • Irena Rogelj
  • Borut Štrukelj
Applied Genetics and Molecular Biotechnology

Abstract

Brazzein is an intensely sweet-tasting plant protein with good stability, which makes it an attractive alternative to sucrose. A brazzein gene has been designed, synthesized, and expressed in Escherichia coli at 30 °C to yield brazzein in a soluble form and in considerable quantity. Antibodies have been produced using brazzein fused to His-tag. Brazzein without the tag was sweet and resembled closely the taste of its native counterpart. The brazzein gene was also expressed in Lactococcus lactis, using a nisin-controlled expression system, to produce sweet-tasting lactic acid bacteria. The low level of expression was detected with anti-brazzein antibodies. Secretion of brazzein into the medium has not led to significant yield increase. Surprisingly, optimizing the codon usage for Lactococcus lactis led to a decrease in the yield of brazzein.

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Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • Aleš Berlec
    • 1
  • Zala Jevnikar
    • 2
  • Andreja Čanžek Majhenič
    • 3
  • Irena Rogelj
    • 3
  • Borut Štrukelj
    • 1
    • 2
  1. 1.Department of Biochemistry and Molecular BiologyJožef Stefan InstituteLjubljanaSlovenia
  2. 2.Faculty of PharmacyUniversity of LjubljanaLjubljanaSlovenia
  3. 3.Biotechnical FacultyUniversity of LjubljanaLjubljanaSlovenia

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