The hydrolytic activity of the purified yeast lipase OF 360 was greatly decreased by heating above 45°C and the residual activity after heating at 50°C for 15 min was about one-tenth of the original. Treatment of the lipase with a bifunctional reagent, dimethyl suberimidate (DMS), increased the heat stability. Stabilization by DMS treatment was supposed to be caused by non-covalent interaction between the lipase and DMS through electrostatic and/or hydrophobic forces. In addition, analysis of FT-IR spectra of the DMS- and non-treated lipases suggested that the main skeleton of the treated lipase was little perturbed by heating.
All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)