Fe^(2+)-催化臧红T褪色光度法测定过氧化氢酶活性  

Determination of catalase activity with Fe^(2+)-catalyzed safranine T fading spectrophotometry

作　　者：张爱菊 董娜 白莹 戴兴德 薛林科 张小林 ZHANG Aijü;DONG Na;BAI Ying;DAI Xingde;XUE Linke;ZHANG Xiaolin(Department of Pharmacy,Gansu Medical College,Pingliang 744000)

机构地区：[1]甘肃医学院药学系,平凉744000

出　　处：《中国食品添加剂》2022年第2期181-185,共5页China Food Additives

基　　金：2021年甘肃省高等学校创新基金项目2021B-341,2021年甘肃省高等学校青年博士基金。

摘　　要：基于Fe^(2+)-H_(2)O_(2)-臧红T褪色体系完成过氧化氢酶活性测定。H_(2)O_(2)氧化臧红T引起吸光度变小,褪色反应又受酶分解反应的抑制,加酶前后吸光度变化(ΔA)与酶活性有相关性。取酶分解反应和褪色反应的最佳条件,CAT活性在0.00~0.02U/mL之间与ΔA呈现良好的线性关系:ΔA=-0.0012+9.5528E(U/mL)(r=0.9990),检出限为6.28×10^(-3)U/mL;采用酶失活样品液作空白,可有效排除样品共存还原性物质的干扰。方法用于新鲜大米样品检测,结果令人满意。In this paper,the activity of catalase was determined based on the Fe^(2+)-H_(2)O_(2)-safranine T fading system.When safranine T was oxidized by H_(2)O_(2),the absorbance decreased,and the fading reaction was inhibited by enzyme decomposition reaction.The absorbance change(ΔA)before and after adding enzyme was related to its activity.The absorbance change value(ΔA)before and after the addition of catalase showed catalase activity.Under optimal conditions,the catalase activity had a good linear relationship withΔA in 0.00~0.02U/mL,ΔA=-0.0012+9.5528 E(U/mL)(r=0.9990),and detection limit of catalase activity was 6.28×10^(-3) U/mL.Using enzyme inactivation sample solution as blank could effectively eliminate the interference of coexisting reducing substances in the sample.The method was used in fresh rice sample analysis and detection,and the results were satisfactory.

关 键 词：过氧化氢酶 过氧化氢 臧红T 褪色光度法 

分 类 号：O657.3[理学—分析化学]