模拟过氧化物酶，采用愈创木酚法，求得了双６－氧－间－羧基苯磺酰基β－ＣＤ·Ｆｅ~３＋配合物（以下简称“模拟酶”）的酶促反应动力学曲线，所得曲线符合米氏方程（Ｍｉｃｈａｃｌｉｓ－ＭｅｎｔｅｎＥｑｕａ－ｔｉｏｎ）；采取米氏方程的双倒数方程（ＬｉｎｅｗｅａｖｅｒＢｕｒｋＥｑｕａｔｉｏｎ）作图，求得了模拟酶的特征常数Ｋｍ值（米氏常数）；在反应中，发现此模拟酶对底物Ｈ２Ｏ２具有较大亲合力，形成了“酶－底”复合物，由此求得模拟酶的反应机制．在相同实验条件下，分别测了两个参照物：ＦｅＣｌ３和双６－氧－间－羧基苯磺酰基β－ＣＤ对此反应的催化能力，作用不太明显． The kinetic curves of enzymatic reaction of bis-6-oxy-m-carboxybenzenesulfonyl β-CD · Fe ~ 3 + complex (hereinafter referred to as “mimic enzyme” , And the obtained curve is in accordance with the Michaeclis-MentenEquation; the characteristic constant Km value (Michaelis constant) of the mimic enzyme was obtained by plotting the double reciprocal equation (LineweaverBurkEquation) of the Mie equation; in the reaction, Mimic enzyme has a strong affinity to substrate H2O2, forming an “enzyme-substrate” complex, thus obtaining a mimic enzyme reaction mechanism. Under the same experimental conditions, two references were tested: the catalytic ability of FeCl3 and bis-6-oxy-m-carboxybenzenesulfonyl β-CD to this reaction was not obvious.