Synthesis and characterization of the sweet protein brazzein.
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.
Izawa
H
H
Cental Research Laboratories, Ajinomoto Co, Inc., Kawasaki, Japan.
Ota
M
M
Kohmura
M
M
Ariyoshi
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010940:Plant Proteins / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D017510:Protein Folding; D013237:Stereoisomerism; D013549:Sweetening Agents / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D013649:Taste
D000596:Amino Acids; D010940:Plant Proteins; D013549:Sweetening Agents; C090521:brazzein protein, Pentadiplandra brazzeana