The reaction between Laccase and o methoxyphenol have been studied by LKB 2107 batch microcalorimetry system. Thermodynamic parameters Δ rH m , Δ G 0 , Δ G ≠ T ,) and kinetic parameters ( K m,k...The reaction between Laccase and o methoxyphenol have been studied by LKB 2107 batch microcalorimetry system. Thermodynamic parameters Δ rH m , Δ G 0 , Δ G ≠ T ,) and kinetic parameters ( K m,k 2 ) have been determined. The process of the reaction has been analyzed from changes in energy by using the transition state theory. Two methods for enhancing catalytic power of Laccase are proposed. The results shown that formation of an enzyme substrate complex is“anticatalytic”. The enter and sole source of catalytic power is the stabilization of transition state; reactant state interactions are by nature inhibitory and only waste catalytic power.展开更多
文摘The reaction between Laccase and o methoxyphenol have been studied by LKB 2107 batch microcalorimetry system. Thermodynamic parameters Δ rH m , Δ G 0 , Δ G ≠ T ,) and kinetic parameters ( K m,k 2 ) have been determined. The process of the reaction has been analyzed from changes in energy by using the transition state theory. Two methods for enhancing catalytic power of Laccase are proposed. The results shown that formation of an enzyme substrate complex is“anticatalytic”. The enter and sole source of catalytic power is the stabilization of transition state; reactant state interactions are by nature inhibitory and only waste catalytic power.
