Fig. 4From: Enhanced trypsin thermostability in Pichia pastoris through truncating the flexible regionNatural-logarithmic plot of residual activity of WT and variants (D3, D5, D7, D9, and D11). After incubation at 50 °C for different minutes, the residual activity of each trypsin was assayed. The original activity was defined as 100%. Each value is the mean of three independent experimentsBack to article page