Elucidation of pressure-induced lid movement and catalysis behavior of Rhizopus chinensis lipase

Publication date: October 2017
Source:International Journal of Biological Macromolecules, Volume 103
Author(s): Gang Chen, Jing Tang, Ming Miao, Bo Jiang, Jian Jin, Biao Feng
The changes of lid movement and catalysis behavior of Rhizopus chinensis lipase under high hydrostatic pressure treatment was studied. Molecular dynamics simulation showed that the lipase lid under pressure was partially opened at below 200MPa but got more closed at over 400MPa. The interfacial activation changed little at pressure below 400MPa but became marginal with the pressure increased to 500MPa. The lipase hydrolysis ability by high pressure treatment underwent a course of initial increasing then reducing with maximum activity obtained at 200MPa and 40°C. At moderate given pressure, the pressure treatment lowered the volume between the reactants and the transition state. Km decreased from 0.592 to 0.441mmol/L with pressure increasing from 0.1 to 200MPa. Meanwhile, vmax and Kcat increased 24.2% and 20% respectively. The change trend of reaction kinetic parameters under 400–500MPa was contrary to that under 0.1–200MPa.



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