Re: What determines the efficiency of trypsin cutting in varying concentrations

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.