Effects of proteolysis on the sensory properties of the sweet protein, thaumatin

Citation

Shamil S, Cusack M & Beynon R (1990) Effects of proteolysis on the sensory properties of the sweet protein, thaumatin. Journal of the Science of Food and Agriculture, 53 (1), pp. 73-84. https://doi.org/10.1002/jsfa.2740530108

Abstract
We have examined the effects of different proteases on the sensory properties of the sweet protein, thaumatin. Trypsin and thermolysin, proteases with quite different primary specificities, have little effect upon the sweetness of ihaumatin, although in each instance the protein has been extensively cleaved. The retention of the sweet taste is probably due to the disulphide bridge cross‐linking which serves to maintain the overall structure of the molecule even when it has incurred proteolytic cleavages. By contrast, subtilisin and chymotrypsin effect greater digestion, to the extent that the protein is reduced to small peptides even when the disulphide bridges are intact. Under these circumstances the sweet taste is lost. The sensory properties of thaumatin depend upon the maintenance of a part of the polypeptide chain in a particular conformation. Copyright © 1990 John Wiley & Sons, Ltd

Keywords
Thaumatin; sensory; proteolysis; sweetness; conformation

Journal
Journal of the Science of Food and Agriculture: Volume 53, Issue 1