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Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin.

Abstract：

:Brazzein is a 54-amino-acid sweet-tasting protein first isolated from the fruit of Pentadiplandra brazzeana Baillon found in West Africa. Brazzein, as isolated from the fruit, is 500 times sweeter than sucrose on a weight basis (9500 times sweeter on a per-molecule basis). A minor component of brazzein from fruit, des-pGlu1-brazzein, has 53 amino acid residues and has twice the sweetness of the parent protein. We have designed a gene for des-pGlu1- brazzein that incorporates codons that are optimal for protein production in Escherichia coli. Production of brazzein from the chemically synthesized gene resulted in recombinant protein with sweetness similar to that of brazzein isolated from the original source. The best yields were achieved by producing brazzein as a fusion with staphylococcal nuclease with a designed cyanogen bromide cleavage site. Because of its intense sweetness and stability at high pH and temperature, brazzein is an ideal system for investigating the chemical and structural requirements involved in sweet-taste properties. This efficient protein production system for brazzein will facilitate such investigations.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Assadi-Porter FM,Aceti DJ,Cheng H,Markley JL

doi

10.1006/abbi.2000.1725

subject

Has Abstract

pub_date

2000-04-15 00:00:00

pages

252-8

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(00)91725-9

journal_volume

376

pub_type

杂志文章

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