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Effects of proteolysis on the sensory properties of the sweet protein, thaumatin
Author(s) -
Shamil Syed,
Cusack Maggie,
Bey Robert J
Publication year - 1990
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740530108
Subject(s) - thaumatin , thermolysin , proteases , proteolysis , sweetness , subtilisin , chemistry , trypsin , taste , chymotrypsin , biochemistry , proteolytic enzymes , sensory system , food science , enzyme , biology , gene , neuroscience
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.