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An investigation of enzyme activities found in thaumatin preparations
Author(s) -
RAMSOHOYE PAMELA V.,
KOZLOV I. A.
Publication year - 1989
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1989.tb00688.x
Subject(s) - thaumatin , esterase , chemistry , enzyme , protease , biochemistry , chromatography , gene
Summary A new alkaline cathodic gel has been developed which improves on the acidic cathodic gel of Reisfeld, Lewis and Williams (1962) when resolving thaumatin isoproteins in commercial thaumatin by electrophoresis. This new gel was used in the investigation of protease and esterase activities in commercial thaumatin and thaumatin isoprotein preparations. Enzyme activity stainings of the thaumatins on the new gel indicate that these activities do not belong to thaumatin but to contaminating enzymes. Other data, such as the decrease in the protease and esterase activities as a result of further purification of the thaumatins and the titration of the proteolytic activities with the specific inhibitor, E‐64, also support this conclusion.