Enzyme Inactivation by an Immobilized Protease in a Plug Flow Reactor

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.