作者: Praveen Kaul , U. C. Banerjee
DOI: 10.1007/S10295-008-0332-Y
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摘要: The insolubility of nitrile substrates in aqueous reaction mixture decreases the enzymatic rate. We studied interaction fourteen water miscible organic solvents with immobilized hydrolyzing biocatalyst. Correlation nitrilase function physico–chemical properties has allowed us to predict enzyme behavior such non-conventional media. Addition solvent up a critical concentration leads an enhancement rate, however, any further increase beyond latter decrease catalytic efficiency enzyme, probably due protein denaturation. dielectric constant (e) showed linear correlation used and extent hydrolysis. Unlike alcohols, rate case aprotic could be linearly correlated log P. Further, kinetic analysis confirmed that affinity for its substrate (Km) was highly dependent upon used. Finally, prospect engineering also permitted control enantioselectivity by regulating enantiomer traffic at active site.