The animal-free, recombinant TrypsiNNex^® sequence is identical to porcine Trypsin and can be used as a direct replacement when converting to animal-free manufacturing. TrypsiNNex^® is expressed in E. coli as an inactive product. The trypsin remains inactivated during both the upstream and downstream manufacturing process, minimizing the level of auto degradation before final stabilization and packaging, thereby preserving a high content of β-trypsin.

Trypsin has intrinsic autolytic activity and is degraded in steps, where β-trypsin is converted into α-trypsin through proteolytic cleavage (red scissors).

This process continues until the trypsin is inactivated. Intermediate forms such as Ψ-trypsin display unspecific activity, which is undesirable. Thus, a high β-trypsin content is a quality indicator that ensures consistent activity and high specificity.

TrypsiNNex^® has a measured β-trypsin of typically well above the minimum specifications at 70% ensuring a high activity and consistent proteolytic pattern, which is critical when processing precursor proteins, such as pro-insulin.