Study on Extraction and Catalytic Activity of Tyrosinase  

酶的提取及其催化活性研究（英文）

作　　者：王宁芳[1] 

机构地区：[1]青海师范大学,青海西宁810008

出　　处：《Agricultural Science & Technology》2016年第12期2893-2895,共3页农业科学与技术（英文版）

摘　　要：Objective] Tyrosinase is a kind of polyphenol oxidase used widely, and the study of tyrosinase attracts extensive attention. [Method] ln this experiment, A conversion kinetic curve of dopa solution was obtained using absorbance of potato extract at 480 nm in Na2HPO4-HCl buffer system at a pH value of 7.2 with the vari-ation rate of absorbance against time （ΔA/Δt） as reaction rate, and the activity of tyrosinase could thus be calculated. [Result] The results showed that at the wave-length, in the Na2HPO4-HCl buffer system with a pH value at 7.2, there was little in-terference to the system, the data showed smal fluctuations, and the activity of ty-rosinase was high and stable, further providing a theoretical foundation for the de-termination and study of factors influencing tyrosinase activity. [Conclusion] The catalytic activity of tyrosinase was studied and determined with buffer solution as substrate with high accuracy and good effect.[目的]酪氨酸酶是一种多酚氧化酶,具有广泛用途,因此对酪氨酸酶的研究受到广泛重视。[方法]试验以p H=7.2的Na2HPO4-HCl缓冲溶液为体系,用分光光度计在480nm处测定土豆提取液的吸光度,以吸光度对时间的变化率(ΔA/Δt)为反应速率,建立多巴溶液的转换动力学曲线,从而可计算出酪氨酸酶的活性。[结果]结果显示在此波长下,以p H=7.2的Na2HPO4-HCl缓冲溶液为体系,对测定体系干扰小,所测数据波动小,酪氨酸酶的活性稳定性高,为进一步确定和研究影响酪氨酸酶活性的因素提供理论依据。[结论]该试验以缓冲溶液为底物研究和测定酪氨酸酶的催化活性,准确度高,效果佳。

关 键 词：ABSORBANCE Kinetic curve TYROSINASE ACTIVITY 

分 类 号：Q55[生物学—生物化学]