Serendipity berries

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... 

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... 

Increasing research has developed several new noncaloric sweeteners the dihydrochalcone group of disaccharide, glycyrrhizin (licorice extract), especially its ammoniated derivative dulcin (4-ethoxy-phenylurea), the glycoprotein of miracle fruit and a polypeptide from a tropical fruit called the serendipity berry, said to be 3000 times sweeter than sucrose. Aspartame (C14H18N205) has been approved by FDA. 

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