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

Charles Illingworth, Gregg Larson, Goran Hellekant

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

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
Volume10
Issue number8
DOIs
StatePublished - Aug 1 1988

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