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Coupled effects of salt and pressure on catalytic ability of Rhizopus chinensis lipase.

BACKGROUND: Both high pressure and environmental factors could influence the catalytic abilities of enzymes. This work investigated coupled effects of pressure and salts on Rhizopus chinensis lipase (RCL) to provide significant information for its further applications.

RESULTS: The maximum activity of RCL was observed under 200 MPa at 40 °C. The highest activity was achieved at concentrations of 0.06-0.1 mol L-1 for tested salts. The effect of monovalent cations on RCL activity followed the Hofmeister series (K+ > Na+ > Li+ ) at 0.1 MPa but the order of Na+ and K+ was changed under 200 MPa. Meanwhile, the effects of anions did not follow the Hofmeister series. KCl slightly improved the thermostability of RCL at moderate concentration. At 60 °C, LiCl only stabilised RCL at 0.1 mol L-1 . The pre-transition unfolding point was shifted from 4.5 to 3.5 mol L-1 with pressure increasing from 0.1 to 600 MPa. In addition, KCl could not change the lipase's extrinsic fluorescence evolution versus pressure.

CONCLUSION: Pressure and salts could improve catalytic ability and stability of RCL under appropriate conditions. The effect of high pressure on RCL was influenced by salts. Meanwhile salts cannot prevent high pressure-induced damage to RCL. © 2017 Society of Chemical Industry.

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