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Brazzein

Brazzein
Brazzeinmj.png
Solution NMR structure of the brazzein protein.
Identifiers
Symbol MONA_DIOCU
PDB 1BRZ More structures
UniProt P56552

Brazzein is a sweet-tasting protein extracted from the West African fruit of the climbing plant Oubli (Pentadiplandra brazzeana Baillon). It was first isolated by the University of Wisconsin–Madison in 1994.

Brazzein is found in the extracellular region, in the pulp tissue surrounding the seeds. With pentadin, discovered in 1989, brazzein is the second sweet-tasting protein discovered in the Oubli fruit.

Like the other sweet proteins discovered in plants, such as monellin and thaumatin, it is extremely sweet compared to commonly used sweeteners (500 to 2000 times sweeter than sucrose). The fruit tastes sweet to humans, monkeys, and bonobos, but gorillas have mutations in their sweetness receptors so that they do not find brazzein sweet, and they are not known to eat the fruit.

The Oubli plant (from which the protein was isolated) grows in Gabon and Cameroon, where its fruit has been consumed by the apes and local people for a long time. Due to brazzein and pentadin, the berries of the plant are incredibly sweet. African locals call them "Oubli" (French for "forgot") in their vernacular language because their taste is said to encourage nursing infants to forget their mother's milk, as once they eat them they are said to forget to come back to the village to see their mother.

The monomer protein, consisting of 54 amino acid residues, is the smallest of the sweet proteins with a molecular weigh of 6.5 kDa. The amino acid sequence of brazzein, adapted from the Swiss-Prot biological database of protein, is as follows: QDKCKKVYEN YPVSKCQLAN QCNYDCKLDK HARSGECFYD EKRNLQCICD YCEY


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