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- W2073524441 abstract "Abstract The reactions between Laccase and various substrates (3,4-Dihydroxybenzaldehyde, Guaiacol, Pyrogallol, Gallic acid) have been studied using LKB-2107 batch microcalorimetry system. Thermodynamic parameters (ΔrHm, ΔG0, ΔG≠T, Ea, ΔS≠T) and kinetic parameters (Km, k2) have been calculated. The reactions process have been analyzed from free energy changes by using the transition state theory which showed that formation of an enzyme-substrate complex is ‘anticatalytic.’ The experimental results also indicated that stabilization of enzyme-substrate complex slows down the reaction, whereas stabilization of transition state accelerates it. Two methods are proposed to enhance catalytic power of Laccase. The decrease of activation entropy (ΔS≠T" @default.
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- W2073524441 date "1997-10-01" @default.
- W2073524441 modified "2023-10-18" @default.
- W2073524441 title "Studies on single-substrate, enzyme-catalyzed reactions and analysis of transition state by microcalorimetry" @default.
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- W2073524441 doi "https://doi.org/10.1016/s0040-6031(97)00249-9" @default.
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