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ENZYME INACTIVATION BY AN IMMOBILIZED PROTEASE IN A PLUG FLOW REACTOR
Author(s) -
BLISS FRANK M.,
HULTIN H. O.
Publication year - 1977
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1977.tb01514.x
Subject(s) - protease , streptomyces griseus , porous glass , chemistry , glucose oxidase , enzyme , adsorption , immobilized enzyme , chromatography , biochemistry , porosity , streptomyces , organic chemistry , biology , bacteria , genetics
Streptomyces griseus protease was immobilized to porous glass and characterized kinetically. The immobilized protease was then used in a plug flow reactor to inactivate enzymes in solution at low concentrations. The glass‐bound protease was effective against fungal glucose oxidase and partially effective against soluble S. griseus protease. Some enzymes were more efficiently inactivated by plain or silanized glass without enzyme, presumably due to adsorption. Less tomato pectin methylesterase was inactivated by glass‐bound protease than by plain glass. This is most likely due to masking of adsorption sites by the immobilized protease.