Dioscoreophyllum cumminsii

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 Dioscoreophyllum cumminsii (serendipity Sweet protein... 

Additional evidence that the exterior surface of the taste receptor cell plasma membrane is the location of the sweet receptor is provided by the action of the chemostimulatory proteins, monellin and thaumatin. Monellin occurs in the fruit of the African serendipity berry (Dioscoreophyllum cumminsii), and thaumatin is found in the fruit of Thaumatococcus daniellii, also... 

Monellin Dioscoreophyllum cumminsii (Stapf) Diels. (Menispermaceae) 3,000 28,106... 

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 ... 

Definition Two polypeptide chains derived from the noncultivated African plant Dioscoreophyllum cumminsii... 

Dioscoreophyllum cumminsii (family Menispermaceae) This is also distributed in West Africa. The fruit of this species is 3000 times sweeter than sucrose. 

Isol. from T. venulosum and Dioscoreophyllum cumminsii seed oils and from a strain of Bacillus megaterium (biosynthetically from hexadecanoic acid). 

Furuya T, Yoshikawa T, Kiyohara H 1983 Alkaloid production in cultured cells of Dioscoreophyllum cumminsii. Phytochemistry 22 1671-1673... 

The pulp of Dioscoreophyllum cumminsii fruit contains monellin, a sweet protein with a molecular weight of ll.Skdal. It consists of two peptide chains, A and B, which are not covalently bound. Their amino acid sequences are shown in Table 8.4. 

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