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The brazzein protein was originally purified from the fruit of Pentadiplandra brazzeana Baillon originated in Africa, a climbing vine that grows in Gabon, Zaire and Cameroon. The brazzein protein, which consists of 54 amino acids, is highly compact and contains one short α-helix and three anti-paralled (I-strands held together by four disulfide bridges, and possesses the smallest molecular weight among the sweet tasting proteins. A minor component of brazzein from fruit, des-pGlul-brazzein, with 53 amino acid residues has twice the sweetness of the parent protein. Brazzein is a stable protein with over wild temperature and pH ranges, but it is expected because it would be digested just as any other dietary protein. Brazzein could be used as a potential economic sweetener, since it is 2000 times sweeter than sucrose in comparison to 2％ sucrose solution. Its taste is more similar to sucrose than that of thaumatin with a clean sweet taste, lingering aftertaste and a slight delay longer than aspartame in an equi-sweet solution.