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Synthesis and characterization of the sweet protein brazzein
Author(s) -
Izawa Hiroyuki,
Ota Masafumi,
Kohmura Masanori,
Ariyoshi Yasuo
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199607)39:1<95::aid-bip10>3.0.co;2-b
Subject(s) - chemistry , characterization (materials science) , food science , biochemistry , nanotechnology , materials science
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.