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 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.
Gusek
T W
TW
Institute of Food Science, Cornell University, Stocking Hall, Ithaca, New York 14853, USA.
Tyn
M T
MT
Kinsella
J E
JE