Effect of immobilization on the physical and kinetic properties of soluble and insoluble trypsin-albumin polymers.
Bovine trypsin was crosslinked to human serum albumin (HSA) with glutaraldehyde to form soluble and insoluble copolymers. The physical and kinetic properties of trypsin and trypsin-HSA polymers were compared. Trypsin was heat labile, retaining only 24% of its enzymic activity after heating for 5 min at 60 degrees C. In contrast, under the same condition both the soluble and insoluble trypsin-HSA polymers showed enhanced resistance to heat in-activation, retaining 81 and 100% of their original activities, respectively. The trypsin-HSA polymers also showed shifts in pH optima, an increase in activation energy, and a broadening of their pH stability profiles.
Scott Laboratories Inc., West Warwick, Rhode Island 02983.
M A
MA
Cohenford
P F
PF
Santoro
J C
JC
Urbanowski
J A
JA
Dain