Guo Yong-Sheng, Wang Jie, Song Xi-Jin
Department of Chemistry, Zhejiang University, Hangzhou 310027, China.
J Zhejiang Univ Sci. 2004 Dec;5(12):1608-12. doi: 10.1631/jzus.2004.1608.
This paper describes an innovative method for the immobilization of acylase I, which was entrapped into the CA-CTA micropore membrane. The most suitable casting solutions proportion for immobilizing the enzyme was obtained through orthogonal experiment. Properties of the enzyme membrane were investigated and compared with those of free enzyme and blank membrane. The thermal stability and pH stability of the enzyme inside the membrane were changed by immobilization. The optimum pH was found to be 6.0, which changes 1.0 unit compared with that of free acylase I. The optimum temperature was found to be about 90 degrees C, which is higher than that of free acylase I (60 degrees C). Experimental results showed that immobilization had effects on the kinetic parameters of acylase I.
本文描述了一种将酰化酶I固定化的创新方法，该酶被包埋在CA-CTA微孔膜中。通过正交实验获得了固定化该酶的最合适铸膜液比例。对酶膜的性能进行了研究，并与游离酶和空白膜的性能进行了比较。固定化改变了膜内酶的热稳定性和pH稳定性。发现最佳pH值为6.0，与游离酰化酶I相比变化了1.0个单位。发现最佳温度约为90℃，高于游离酰化酶I的最佳温度（60℃）。实验结果表明，固定化对酰化酶I的动力学参数有影响。
