|MadSci Network: Biochemistry|
For a good introduction to Trypsin you can go here: http://www.rcsb.org/pdb/molecules/pdb46_1.html Like a lot of enzymes, its efficiency is based on: amount of substrate present, the pH of the solution (Trypsin's optimum is just under pH 8), temperature, salt concentrations, and any inhibitors present. What usually decreases efficiency is disruption of the tertiary structure and/or the noncovalent forces (like hydrogen bonding). Both of these can lead to distortions in the active site on the enzyme. I think most college level biochem books would have a section on enzymes that would provide a general overview. Here is a journal paper for more information on salts and trypsin: Castaneda-Agullo M, Del Castillo LM, Whitaker JR, Tappel AL. (1961) Effect of ionic strength on the kinetics of trypsin and alpha chymotrypsin. J Gen Physiol. 44:1103-20.
Try the links in the MadSci Library for more information on Biochemistry.