Determination of Kinetic Parameters and The Effect of Ion Mg2+ Inhibition Into Pectinase Activities.

D. Anggraini, Devita Sulistiana, Dwi Kameluh Agustina, A. Ulimaz
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引用次数: 1

Abstract

The purpose of study was to determine kinetic parameters and inhibitory effect of Mg2+ ions on pectinase. Activity test performed at pH 4,5 temperature 55oC for 50' with 10 mm concentrations of each ion 0-10mm. Galacturonic acid content, as product of pectin substrate hydrolysis, was used as basis for determining activity and analyzed by visible spectrophotometry. At concentrations 2 and 4 mm Mg2+ act as an activator, but at concentrations 6, 8, and 10 mM as inhibitors. The value of KM with and without inhibitors is almost same, that is 0.3145% and 0.3105% but value of Vm from both are different, that is 80,645 μg.ml-1.minute-1 and 62,112 μg.ml-1.minute-1. The conclusion that type of inhibitory pectinase with Mg2+ is a non-competitive inhibition. The inhibition constant value (Ki) is 26,84.
动力学参数测定及Mg2+离子抑制对果胶酶活性的影响。
研究Mg2+离子对果胶酶的动力学参数及抑制作用。活性测试在pH值为4.5,温度为55℃,时间为50',每个离子浓度为10mm, 0-10mm。以果胶底物水解产物半乳糖醛酸含量为测定活性的依据,采用可见分光光度法进行分析。浓度为2和4mm的Mg2+作为活化剂,但浓度为6、8和10mm的Mg2+作为抑制剂。添加抑制剂和未添加抑制剂的KM值基本相同,分别为0.3145%和0.3105%,但Vm值不同,为80,645 μg.ml-1。Minute-1和62,112 μg.ml-1。结论Mg2+抑制型果胶酶是一种非竞争性抑制。抑制常数Ki为26,84。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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