Commercially available proteomic and mass spec grade trypsin products contain nonspecific protease activity at a low but detectable level. Close analysis of this activity suggests it is chymotryptic in nature. The nonspecific, chymotryptic-like cleavage activity becomes evident if large amounts of trypsin are used in a digestion reaction (Figure 1, Panel A). These nonspecific cleavage activities compromise the quality of protein analysis. Our production procedure assures that Trypsin Platinum is free of any detectable traces of nonspecific cleavage activity (Figure 1, Panel B).

Autoproteolysis is another common negative side effect of trypsin digestion. To suppress trypsin autoproteolysis, trypsin used in protein mass spec sample preparation is chemically modified. Yet, a certain level of autoproteolysis is still observed (Figure 2, Panel A). The generated tryptic autoproteolytic peptides often compromise protein analysis, particularly if a large amount of trypsin is used in a digestion reaction. Our novel modification method further suppresses Trypsin Platinum autoproteolysis compared to the autoproteolysis observed in the currently available proteomic and mass spec grade trypsin products (Figure 2, Panel B), assuring that the level of autoproteolytic tryptic peptides remains negligibly low even if large quantities of Trypsin Platinum are used.