Modulation of enzyme activity and stability by high pressure : α-chymotrypsin

作者: V.V. Mozhaev , E.V. Kudryashova , N. Bec

DOI: 10.1016/S0921-0423(06)80039-0

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摘要: Abstract Examples of application high hydrostatic pressure for modulating important properties enzymes, namely catalytic activity, substrate specificity and thermal stability are presented in this paper. Enzymatic reactions characterised by negative values activation volumes (ΔV≠) accelerated at pressures as is the case with hydrolysis anilides α-chymotrypsin. Simultaneous action elevated temperature raises rate enzymatic more than 50 times compared to reaction studied 20 °C atmospheric pressure. Due different signs ΔV≠ esters, a 100-fold increase anilide-hydrolysing over ester-hydrolysing activity α-chymotrypsin sysytem reversed micelles was observed 2000 atm, comparison rates measured 1 atm. Another positive effect its ability significantly decelerate heat inactivation : 5–10-fold decrease enzyme applying 1.500–2.000 This protection becomes even presence glycerol. Possible explanations stabilisation effects discussed.

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