Autolysis of trypsin can produce several undesirable outcomes. Firstly, autolysis reduces trypsin activity, leading to incomplete digestion and missed cleavages. Secondly, an intermediate autolysis product, ψ-trypsin, has relaxed specificity and cleaves amino acids other than lysine and arginine, exhibiting chymotrypsin-like activity. Thirdly, autolysis can also make aliquoting, storage and handling of trypsin challenging.
Recombinant trypsin is engineered to retain its enzymatic properties and is further methylated to make it exceptionally resistant to autolysis. This leads to better data quality, enzyme stability, and easy handling.
