Abstract
When various protease solutions in dynamic ranges of activity-enzyme concentration profiles were treated at the medium high pressure of 100 and 300 MPa for 60, 120, and 300 min, characteristic changes in enzyme activity were found. The most conspicuous facts observed were the increase in the activity of trypsin with increasing pressurizing time and nearly complete inactivation of thermolysin at 300 MPa, which seemed to suggest that serine proteases hold better pressure tolerance compared with metallo-proteases. Electrophoretic analysis on wheat gluten hydrolyzates that were prepared by trypsin and thermolysin at ambient pressure and 300 MPa supported time-dependent changes in protease activity.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
