Secretion of the sweet-tasting plant protein thaumatin by Streptomyces lividans

Charles Illingworth, Gregg Larson, Goran Hellekant

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

To produce and direct the export in Streptomyces lividans of the sweet plant protein thaumatin, thaumatin II cDNA was fused in the correct reading frame to the β-galactosidase leader peptide, under the control of the β-galactosidase promoter and ribosome binding site. The export of the recombinant thaumatin may allow the correct formation of the thaumatin disulfide bonds. The recombinant thaumatin was purified from the medium on an S-Sepharose column and detected with western blots by sheep α-thaumatin antibodies. The recombinant thaumatin was the same size as authentic thaumatin and changed position on an acrylamide gel in response to reduction by 2-mercaptoethanol in the same manner.

Original languageEnglish (US)
Pages (from-to)37-42
Number of pages6
JournalJournal of Industrial Microbiology
Volume4
Issue number1
DOIs
StatePublished - Jan 1 1989

Keywords

  • Exported recombinant protein
  • Leader peptide
  • Recombinant protein
  • Thaumatin
  • β-Galactosidase

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