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Synthesis and characterization of the sweet protein brazzein.
- Source :
-
Biopolymers [Biopolymers] 1996 Jul; Vol. 39 (1), pp. 95-101. - Publication Year :
- 1996
-
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.
- Subjects :
- Amino Acid Sequence
Amino Acids analysis
Chromatography, High Pressure Liquid
Humans
Mass Spectrometry
Molecular Sequence Data
Peptide Mapping
Plant Proteins pharmacology
Protein Folding
Stereoisomerism
Sweetening Agents pharmacology
Taste
Plant Proteins chemical synthesis
Plant Proteins chemistry
Sweetening Agents chemical synthesis
Sweetening Agents chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3525
- Volume :
- 39
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 8924630
- Full Text :
- https://doi.org/10.1002/(sici)1097-0282(199607)39:1<95::aid-bip10>3.0.co;2-b