Biotechnology Letters

, Volume 10, Issue 8, pp 587–592 | Cite as

Secretion of the sweet-tasting plant protein thaumatin byBacillus subtilis

  • Charles Illingworth
  • Gregg Larson
  • Goran Hellekant
Article

Summary

With the α-amylase promoter and ribosome binding site,Bacillis subtilis was used to express the sweet plant protein thaumatin II cDNA fused in the correct reading frame to the α-amylase leader peptide. The r-thaumatin was purified from the medium on a S-Sepharose column and detected with western blots by sheep α-thaumatin antibodies. The r-thaumatin and authentic thaumatin were the same size when reduced by 2-ME and the same size when not reduced.

Keywords

Peptide Western Blot Organic Chemistry Binding Site Bacillis 

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Copyright information

© Kluwer Academic Publishers 1988

Authors and Affiliations

  • Charles Illingworth
    • 1
  • Gregg Larson
    • 1
  • Goran Hellekant
    • 1
  1. 1.Dept. of Veterinary ScienceUniv. of Wisconsin-MadisonMadisonUSA

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