Abstract
Physicochemical approaches, which enable an increase in the yields of end products in enzyme-catalyzed reactions, have been analyzed comprehensively (1). These are: I) equilibrium approaches where higher yields are due to a shift in the thermodynamic equilibrium of the reacton; e.g., a) a method based on low solubility of the end product; b) a method of consecutive reactions; c) enzymatic synthesis in aqueous-organic mixtures, and d) water-water-immiscible organic solvent biphasic systems; and II) nonequilibrium (kinetic) approaches, where the yield of the end product considerably exceeds the equilibrium level. These are, first and foremost, hydrolytic enzyme-catalyzed transfer reactions and kinetically controlled equilibrium. Some recently established unexplained facts are reported on the regulation of enzymatic reaction by light.
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