纯酶酶催化动力学分析数据集

采用数据处理软件Origin对不同酶的部分突变体的动力学参数，首先通过分光光度计岛津-UV 1900采集酶在不同底物浓度下的酶活力数据，活力测定时环境温度对应分布于25-40℃，底物浓度分布于1-20 mM，添加适量的纯酶进行反应，控制最初一分钟内分光光度计在340 nm处的吸光度变化值在0.05-0.15之间，每个浓度测定三次取平均值，通过吸光度的变化值计算对应在每个底物浓度条件下的酶的比活力。将所得的数据导入Origin，使用非线性拟合中的米氏方程函数对数据进行拟合，得到酶的动力学参数。

Kinetic parameters of partial mutants of various enzymes were analyzed using the data processing software Origin. First, enzyme activity data of the enzymes under different substrate concentrations were collected with the Shimadzu UV-1900 spectrophotometer. During activity assays, the ambient temperature ranged from 25 to 40 °C, and substrate concentrations varied between 1 and 20 mM. An appropriate amount of purified enzyme was added to initiate the reaction, and the absorbance change at 340 nm within the first minute was controlled to fall within 0.05–0.15. Each substrate concentration was measured three times, and the average value was calculated. The specific activity of the enzyme under each substrate concentration was then computed based on the absorbance change. The obtained data were imported into Origin, and fitted using the Michaelis-Menten equation via non-linear curve fitting to derive the kinetic parameters of the enzymes.

搜集汇总

背景与挑战

背景概述

该数据集由华东理工大学创建，来源于国家重点研发计划项目，专注于纯酶的催化动力学分析。它通过分光光度计采集酶活力数据，并利用Origin软件和米氏方程进行非线性拟合，以获取酶的动力学参数。