It has been known that most of the organic solvents have a detrimental effects on enzymes activity and structure but, if incubation of an enzyme in a specific organic solvent lead to an increase in the activity what could be the reason ?
Exposure of more hydrophobic residues that somehow increase the affinity recognition process.
Here is a paper that investigates this effect for one enzyme:
Article Effects of organic solvents on the enzyme activity of Trypan...
its not that pure organic solvent is used. The organic solvent is used in small amount (5-20%), which makes the hydrophobic Substrates more accesible to the enzyme, hence an increase in activity is observed.
one example is the epoxide hydrolase https://link.springer.com/article/10.1007%2Fs11274-017-2248-z
I tried 20% ethanol during beta-Lg hydrolysis by trypsin, at least the hydrolysis efficacy was not decreased, and the intact protein molecule was more preferred by trypsin. The change of accessibility of hydrophobic part could be one of the important reasons.
Thanks for your answers but the interesting question is , how two similar organic solvents (methanol and ethanol ) have opposite effect on the same enzyme ? I could not comment that
They are only similar in their functional group. The difference is established by the number of carbons. Ethanol is a little more hydrophobic than methanol.
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