Biopolymers. 1996 Jul;39(1):95-101.

Synthesis and characterization of the sweet protein brazzein.

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Cental Research Laboratories, Ajinomoto Co, Inc., Kawasaki, Japan.

Abstract

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.

PMID:: 8924630; [PubMed - indexed for MEDLINE]

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Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B. [FEBS Lett. 1994]
Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B.
Ming D, Hellekant G. FEBS Lett. 1994 Nov 21; 355(1):106-8.
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Cited by 2 PubMed Central articles

Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor. [J Mol Biol. 2010]
Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor.
Assadi-Porter FM, Maillet EL, Radek JT, Quijada J, Markley JL, Max M. J Mol Biol. 2010 May 14; 398(4):584-99. Epub 2010 Mar 17.
Review Sweet proteins--potential replacement for artificial low calorie sweeteners. [Nutr J. 2005]
Review Sweet proteins--potential replacement for artificial low calorie sweeteners.
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