木瓜凝乳蛋白酶的分离纯化及部分酶学性质研究

Purification and Characterization of Chymopapain

目的:从木瓜蛋白酶粗酶中分离木瓜凝乳蛋白酶,并对其部分酶学性质作初步研究。方法:采用离子交换层析分离木瓜凝乳蛋白酶,通过温度、Na+、Ca2+及其它金属离子等来研究其对酶性质的影响。结果:经离子交换得到了在PAGE中呈单一区的木瓜凝乳蛋白酶,该酶在37℃保温24h后其活力只有原来的7.5%,低浓度的Na+、Ca2+、K+、Cu2+对其有激活作用。结论:木瓜凝乳蛋白酶的分离纯化及酶学性质都值得进一步研究。

Objective:To purify chymopapain from spray-dried latex of papaya fruit and study on the characterization of purified product.Methods:Chymopapain was purified by ion exchange chromatograph and characterized by various methods.Results:Chromatography purity chymopapain was obtained.The activity of chymopapain was only 7.5% of original product after incubated at 37℃ for 24hours while enhanced by the low concentration of Na^+,Ca^(2+),K^+,Cu^(2+).Conclusion:Chymopapain for purification and its characterization deserve to study thoroughly.