Artigo Revisado por pares

Synthesis and characterization of the sweet protein brazzein

1998; Wiley; Volume: 39; Issue: 1 Linguagem: Inglês

10.1002/(sici)1097-0282(199607)39

ISSN

1097-0282

Autores

Hiroyuki Izawa, Masafumi Ota, Masanori Kohmura, Yasuo Ariyoshi,

Tópico(s)

Microbial Metabolic Engineering and Bioproduction

Resumo

The sweet protein brazzein isolated from the fruit of the African plant, Pentadiplandra brazzeana Baillon is 2000-500 times sweeter than sucrose, and consists of 54 amino acid residues with four intramolecular disulfide bonds. Brazzein was prepared by the fluoren-9-yl-methoxycarbonyl solid-phase method, and was identical to natural brazzein by high performance liquid chromatography, mass spectroscopy, peptide mapping, and taste evaluation. The D enantiomer of brazzein was also synthesized, and was shown to be the mirror image of brazzein. The D enantiomer (ent-brazzein) was devoid of any sweetness and was essentially tasteless. © 1996 John Wiley & Sons, Inc.

Referência(s)
Altmetric
PlumX