Characterization of the Recombinant Thermostable Lipase (Pf2001) from Pyrococcus furiosus: Effects of Thioredoxin Fusion Tag and Triton X-100
Figure 4
(a) Effect of Triton X-100 on optimal temperature. The lipase PF2001Δ60 was assayed at temperatures ranging from 50 to 80°C, in 50 mM phosphate buffer, pH 7.0, in the presence and absence of Triton X-100. (b) Effects of Triton X-100 on thermal stability of the PF2001Δ60. The enzyme samples in phosphate buffer (50 mM pH 7.0) containing 0.1% gum arabic were incubated at 70°C for 85 min and in the same conditions with 0.4% Triton X-100. The residual enzyme activity was assayed at 70°C, pH 7.0, using the substrate MUF-Hep.
