Journal of Changshu Institute of Technology2025，Vol.39Issue(2)：46-53,8.
菠菜叶过氧化物酶的热失活及其动力学特性
Thermal Inactivation and Kinetic Characterisation of Peroxidase from Spinach Leaves
荣可瑜 1黄友如 1张宁 1许芳芳 1孙美琦 1周南南 1潘诗雯 1范晓玉 2宋莹莹 2陈义勇1
作者信息
- 1. 常熟理工学院 生物与食品工程学院,江苏 常熟 215500
- 2. 南通科技职业学院 环境与生物工程学院,江苏 南通 226007
- 折叠
摘要
Abstract
Fresh spinach leaves were used as raw material to extract POD,and its enzymatic properties such as optimal pH,optimal temperature,catalytic activation energy,Km and Vmax,thermal stability and thermal denaturation activation energy were discussed.In particular,the influence of heat treatment on POD activity and its related kinetics were studied.The results showed that with o-phenylenediamine as the hydrogen donor substrate of POD,H2O2 as the peroxide substrate,the optimal pH was 7.0,the optimal reaction temperature was 30℃,and the activation energy of the catalytic reaction was 29.49 kJ/mol in spinach leaves POD.As a double substrate reaction,the Km value of the enzyme was 1.976 mmol/L and Vmax was 120.48 U when o-phenylenediamine was used as substrate.When H2O2 was used as substrate,the Km value of the enzyme was 3.573 mmol/L and Vmax was 133.33 U.The thermal inactivation study showed first-order inactivation kinetic characteristics,and Arrhenius plotted a straight line with a slope equivalent to 168.47 kJ/mol of POD enzyme thermal denaturation activation energy.There was a jump change(the velocity constant k being from-0.042 to-0.286)between 55℃ and 60℃ in the thermal inactivation rate of spinach leaves POD.After 60℃,POD in spinach leaves was sensitive to temperature change,and the denaturation rate of the thermally unstable part of POD in spinach leaves was accelerated by increasing temperature.关键词
菠菜/过氧化物酶/热失活/动力学特征/活化能Key words
spinach/peroxidase/heat inactivation/kinetic characterisation/activation energy分类
轻工纺织引用本文复制引用
荣可瑜,黄友如,张宁,许芳芳,孙美琦,周南南,潘诗雯,范晓玉,宋莹莹,陈义勇..菠菜叶过氧化物酶的热失活及其动力学特性[J].Journal of Changshu Institute of Technology,2025,39(2):46-53,8.
