Abstract
Sweet proteins are the sweetest natural molecules. This aspect prompted several proposals for their use as food additives, mainly because the amounts to be added to food would be very small and safe for people suffering from sucrose-linked diseases. During studies of sweet proteins as food additives we found that their sweetness is affected by water salinity, while there is no influence on protein’s structure. Parallel tasting of small size sweeteners revealed no influence of the water quality. This result is explained by the interference of ionic strength with the mechanism of action of sweet proteins and provides an experimental validation of the wedge model for the interaction of proteins with the sweet receptor.
Highlights
Sweetness is elicited by a very large variety of molecules, both natural and synthetic (Temussi, 2006a; Temussi, 2007)
MNEI and Thaumatin were dissolved at a 10 mg/L concentration in HPLC water containing a NaCl concentration calculated to reproduce the ionic strength of the three mineral waters, according to the data reported on the labels
Upon increasing the protein concentration to 10 mg/L, the sweetness intensity of MNEI, Mut3, and Mut9 was assessed between the rates of slightly sweet to very sweet (Figures 1A,C,E)
Summary
Sweetness is elicited by a very large variety of molecules, both natural and synthetic (Temussi, 2006a; Temussi, 2007). Thaumatin is very soluble in water, up to 600 mg/ml, and is endowed by high thermal stability under acidic conditions, with retained sweetness at 80°C for several hours (Kaneko and Kitabatake, 2001). Monellin is another intensely sweet protein, isolated from Dioscoreophyllum cumminsii, a West Africa tropical plant (Inglett and May 1969). It is a small globular protein (94 residues), composed of two polypeptide chains. MNEI and others single chain Monellin variants reach temperatures higher than 70°C without loss of sweetness power (Kim et al, 1989)
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