Abstract：Under anaerobic condition, the reactions between Rhus vernicifera laccase and 5 klnds of substrates have been studied by I,KB-2lO7 Batch microcalorimetry system at 298. 15 K in O. l mol/I, phosphates salt buffer (pH 7. 4 ).The molar reaction enthalpy (Q.H,,, ), the Michaelis constant (K,,, ), the rate constantof electron transfer process (k, ), the laccase activity (EA ) and the Gibbs bindlng en-ergy (dG', ) for each substrate have been determ1ned. The stability of laccase suh-strate complexes,the electron transfer rate of the enzymatlc reaction and the struc-ture of products of non-enzymatic reaction are discussed for each substrate underthe same experiment condition.
收稿日期: 1999-02-25
引用本文:
谢修银 吴鼎泉. 漆酶与各种类型底物反应性能的微量热法研究[J]. , 1999, 38(2): 0-0.
谢修银 吴鼎泉. Studies on the character of the reaction between laccase and different substrates by microcalorimetry. , 1999, 38(2): 0-0.
