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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Izawa H,Ota M,Kohmura M,Ariyoshi Ydoi
10.1002/(sici)1097-0282(199607)39:1<95::aid-bip10>subject
Has Abstractpub_date
1996-07-01 00:00:00pages
95-101issue
1eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(199607)39:1<95::AID-BIP10>journal_volume
39pub_type
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