Secretion of the sweet-tasting plant protein thaumatin by Bacillus subtilis

Charles Illingworth, Gregg Larson, Goran Hellekant

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)587-592
Number of pages6
JournalBiotechnology Letters
Issue number8
StatePublished - Aug 1988


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