IMMOBILIZATION OF THE SERINE PROTEASE FROM THERMOMONOSPORA-FUSCA YX ON POROUS-GLASS

As much as 84% of the thermostable serine protease from Thermomonospora fusca strain YX was covalently attached to silanized glass using glutaraldehyde. The immobilized protease exhibited a higher temperature optimum (86°C) and pH optimum (9.4) for activity compared to soluble YX‐protease (80°C and pH 9.0, respectively). Immobilization improved enzyme thermo‐stability above 90°C and reduced inactivation during prolonged storage (9% loss of activity after 90 days at 12°C). A continuous‐flow column reactor packed with immobilized protease readily hydrolyzed casein over broad ranges of temperature and pH. Copyright © 1990 John Wiley & Sons, Inc.