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STUDIES OF THE REACTION BETWEEN LACCASE AND p-PHENYLENEDIAMIME BY MICROCALORIMETRY

STUDIES OF THE REACTION BETWEEN LACCASE AND p-PHENYLENEDIAMIME BY MICROCALORIMETRY
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摘要 The molar reation enthalpy,the Michaelis constant and the observed rate constant of the reaction between the Rhus vernicifera laccase and p-phenylenediamine have been determined at 298. 15 K by LKB-2107 microcalorimetry system in 0.1 mol/L phosphate salt buffer (pH7. 4) to be △rHm=-136.36±0. 36kJ/mol, Km= 5. 58×10-3 mol/L and k1 =8. 63×10-3s-1, respectively. The catalyst activity of laccase withp-phenylenediamine as substrate has been determined to be EA=0. 045 IU in the experimental condition.The observed activation energy of non-enzymic step of the reaction, the Gibbs binding energy of the combination process of laccase and substrate have been also calculated. The physical significance of the determined parameters were discussed for different step of the reaction. The molar reation enthalpy,the Michaelis constant and the observed rate constant of the reaction between the Rhus vernicifera laccase and p-phenylenediamine have been determined at 298. 15 K by LKB-2107 microcalorimetry system in 0.1 mol/L phosphate salt buffer (pH7. 4) to be △rHm=-136.36±0. 36kJ/mol, Km= 5. 58×10-3 mol/L and k1 =8. 63×10-3s-1, respectively. The catalyst activity of laccase withp-phenylenediamine as substrate has been determined to be EA=0. 045 IU in the experimental condition.The observed activation energy of non-enzymic step of the reaction, the Gibbs binding energy of the combination process of laccase and substrate have been also calculated. The physical significance of the determined parameters were discussed for different step of the reaction.
出处 《Wuhan University Journal of Natural Sciences》 CAS 1998年第1期107-107,共1页 武汉大学学报(自然科学英文版)
关键词 MICROCALORIMETRY rhus vernicifera laccase P-PHENYLENEDIAMINE enzymatic reaction microcalorimetry rhus vernicifera laccase p-phenylenediamine enzymatic reaction
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