Synthesis and characterization of the sweet protein brazzein
- 6 December 1998
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 39 (1) , 95-101
- https://doi.org/10.1002/(sici)1097-0282(199607)39:1<95::aid-bip10>3.0.co;2-b
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. © 1996 John Wiley & Sons, Inc.Keywords
This publication has 25 references indexed in Scilit:
- Brazzein, a new high‐potency thermostable sweet protein from Pentadiplandra brazzeana BFEBS Letters, 1994
- Solid-phase synthesis of crystalline monellin, a sweet protein.Agricultural and Biological Chemistry, 1991
- Expression and secretion of thaumatin from Aspergillus oryzae.Agricultural and Biological Chemistry, 1990
- Expression of synthetic thaumatin genes in yeastBiochemistry, 1988
- Zusammenhänge zwischen Struktur und Süßgeschmack bei AminosäurenZeitschrift für Lebensmittel-Untersuchung und Forschung, 1977
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Isolation and Characterization of Thaumatin I and II, the Sweet‐Tasting Proteins from Thaumatococcus daniellii BenthEuropean Journal of Biochemistry, 1972
- Isolation and characterization of the sweet principle fromDioscoreophyllum cumminsii (stapf) DielsFEBS Letters, 1972
- Miraculin, the Sweetness-inducing Protein from Miracle FruitNature, 1968
- Taste-Modifying Protein from Miracle FruitScience, 1968