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Title: Immobilization of the serine protease from Thermomonospora fusca YX on porous glass. Author: Gusek TW, Tyn MT, Kinsella JE. Journal: Biotechnol Bioeng; 1990 Aug 05; 36(4):411-6. PubMed ID: 18595095. Abstract: 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 degrees C) and pH optimum (9.4) for activity compared to soluble YX-protease (80 degrees C and pH 9.0, respectively). Immobilization improved enzyme thermo-stability above 90 degrees C and reduced inactivation during prolonged storage (9% loss of activity after 90 days at 12 degrees C). A continuous-flow column reactor packed with immobilized protease readily hydrolyzed casein over broad ranges of temperature and pH.[Abstract] [Full Text] [Related] [New Search]