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根据酶活性不可逆改变的动力学方法，研究了长毛对虾（Ｐｅｎａｅｕｓｐｅｎｉｃｉｌａｔｕｓ）酸性磷酸酶在变性剂胍，脲作用下的不可逆失活．结果表明，酶在不同变性剂中的失活行为不尽相同．测得该酶在１．２ｍｏｌ／Ｌ盐酸胍，３ｍｏｌ／Ｌ脲中的ｋ０／ｋ０′分别为５．０和４．３．ｋ０＞ｋ０′的事实说明游离酶比酶底物复合物具有更大的失活速度常数，底物的结合对酶的失活有明显的保护作用．酶底物复合物较大的抗失活能力也从一侧面证实了活性中心的柔曲性理论．
The irreversible inactivation of Penaeuspenicilatus acid phosphatase under the action of guanidine and urea was studied based on the irreversible kinetic method. The results show that the enzyme in different denaturants inactivation behavior varies. The k0 / k0 ’of the enzyme was found to be 5.0 and 4.3 in 1.2 mol / L guanidine hydrochloride and 3 mol / L urea, respectively. The fact that k0> k0 ’indicates that the free enzyme has a greater rate of inactivation rate than the enzyme substrate complex, and the substrate binding has a significant protective effect on the enzyme inactivation. The larger anti-inactivation ability of the enzyme substrate complex also confirmed the theory of pliability of the active center from one side.