Premium
Protease stabilization by carboxylic acid salts: Relative efficiencies and mechanisms
Author(s) -
Crossin Michael C.
Publication year - 1989
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02682628
Subject(s) - proteolysis , protease , carboxylic acid , subtilisin , chemistry , substrate (aquarium) , salt (chemistry) , enzyme , biochemistry , organic chemistry , biology , ecology
Kinetic studies are presented on the inhibition of proteolysis by carboxylic acid salts on the synthetic substrate succinyl ala‐ala‐pro‐phe‐para nitroanilide. The inhibition of proteolysis/autodigestion is shown to be the major factor in the stabilization of a detergent protease [i.e., Maxatase (subtilisin Carlsberg)] in an unbuilt, liquid, heavy duty laundry formulation. The inhibition of autodigestion by a carboxylic acid salt as a function of pH parallels the protease stability increase during accelerated aging. Relative inhibition of proteolysis and protease stabilization by various carboxylic acid salts are compared.