Synthesis and characterization of the sweet protein brazzein
Version of Record online: 6 DEC 1998
Copyright © 1996 John Wiley & Sons, Inc.
Volume 39, Issue 1, pages 95–101, July 1996
How to Cite
Izawa, H., Ota, M., Kohmura, M. and Ariyoshi, Y. (1996), Synthesis and characterization of the sweet protein brazzein. Biopolymers, 39: 95–101. doi: 10.1002/(SICI)1097-0282(199607)39:1<95::AID-BIP10>3.0.CO;2-B
- Issue online: 6 DEC 1998
- Version of Record online: 6 DEC 1998
- Manuscript Accepted: 16 OCT 1995
- Manuscript Received: 9 AUG 1995
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.