Dioscoreophyllum cumminsii monellin from

Monellin can be purified from the fruit of Dioscoreophyllum cumminsii grown in West Africa and is approximately 100 000 times sweeter than sugar on a molar basis and several thousand times sweeter on a weight basis.Single-chain monellin (SCM), which is an engineered 94-residue polypeptide, has proven to be as the sweet as native two-chain monellin. It is more stable than the native monellin at high temperature and in acidic... 

Monellin is a sweet protein that was isolated from the fruit of Dioscoreophyllum cumminsii (Staff Diels, which is known as the serendipity berry and is native to West Africa. It is a basic protein with an isoelectric point of approximately 9.3 and is 3000 times sweeter than sucrose.65 66 Perception lasts for more than 1 h and leaves an aftertaste. Heat denatures monellin proteins they lose their sweetness when heated over 50 °C at low pH. Monellin has a molecular mass of 10.7 kDa. Monellin has two noncovalently associated polypeptide chains chain A contains 44 amino acid residues and chain B has 50 residues. In 1976, the primary structure of monellin was proposed independently by three groups but their results all differed somewhat.67-69... 

Monellin, an intensively sweet protein from the West African berries Dioscoreophyllum cumminsii. On a weight basis, monellin is several thousand times more potent in sweetness than sucrose. It consists of two non-covalently associated polypeptide chains, A and B, with 44 and 50 residues, respectively. According to the X-ray crystal structure, the natural protein consists of an anti-parallel /S-sheet with five strands and an a-hdix. Single-chain moneUin (SCM), an engineered 94 aa polypeptide, has been proven to be as sweet as the native two-chain molecule, and is more stable in both high-temperature and acidic environments compared to the native monellin [T. Mizukoshi et al., FEBS Lett. 1997, 413, 409 ... 

Monellin is extracted from the fruit Dioscoreophyllum volkensii (syn. D. cumminsii, Menispermaceae) native to tropical African rainforests. Monellin is a sweet protein with liquorice-like flavour, which consists of two peptide chains, A and B, composed of a sequence of 45 and 50 amino acids, respectively (11.5 kDa). Under food processing conditions it is unstable and has no practical significance as a sweet substance. 

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