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白腐菌漆酶的自由态和固定化酶的生物催化特性及其激活区域。

Biocatalytic characterization of free and immobilized laccase from Trametes versicolor in its activation zone.

机构信息

Université de Tunis El Manar, Faculté des Sciences de Tunis, Laboratoire de Physique de la Matière Molle et de la Modélisation Electromagnétique, 2092 Tunis, Tunisia.

Université de Tunis El Manar, Faculté des Sciences de Tunis, Laboratoire de Physique de la Matière Molle et de la Modélisation Electromagnétique, 2092 Tunis, Tunisia; Université de Carthage, Institut National des Sciences Appliquées et de Technologie, Centre Urbain Nord, BP. 676, Tunis, Tunisia.

出版信息

Int J Biol Macromol. 2019 May 1;128:681-691. doi: 10.1016/j.ijbiomac.2019.01.199. Epub 2019 Jan 31.

DOI:10.1016/j.ijbiomac.2019.01.199
PMID:30711566
Abstract

This investigation may be of interest for researchers working on the determination of several biocatalytic properties of the laccase from Trametes versicolor. So, We will treated the effects of pH, temperature, several organic components and heavy metals by performing enzyme assays in the presence of a 2,6 dimethoxyphenol (DMP) as substrate on the laccase activity. The optimum activity and temperature are 4 and 40 °C, respectively. The maximum rate of the reaction is 124.53 U/mg and the Michaelis constant is in order of 1.23 mM. The effect of metal ions on the laccase activity with a final concentrations range varying from 1 to 5 mM show that the Cu ions increase the activity for concentration inferiors to 4 mM and the other metal ions have a relative influence on the laccase activity. Four tri-block copolymers based on poly(ethylene oxide) and poly(propylene oxide) and two polyethylene glycols are used to study the synthetic polymers effects on the enzymatic activity. Also, we have demonstrated that the laccase keeps 95% of its initial activity at 60 °C in the PEGDA8000 and PEGDA6000 gel matrix. The maximum rate of the immobilized laccase is approximately around 21.03 and 47.22% smaller than the free one.

摘要

这项研究可能对研究白腐菌漆酶的几种生物催化特性的研究人员有兴趣。因此,我们将通过在存在 2,6-二甲氧基苯酚(DMP)作为底物的情况下进行酶测定来研究 pH、温度、几种有机成分和重金属对漆酶活性的影响。最适活性和温度分别为 4°C 和 40°C。反应的最大速率为 124.53 U/mg,米氏常数约为 1.23 mM。金属离子对漆酶活性的影响,终浓度范围从 1 到 5 mM,结果表明 Cu 离子在低于 4 mM 的浓度下增加了活性,而其他金属离子对漆酶活性有相对影响。使用了基于聚(氧化乙烯)和聚(氧化丙烯)的四种三嵌段共聚物和两种聚乙二醇来研究合成聚合物对酶活性的影响。此外,我们已经证明漆酶在 PEGDA8000 和 PEGDA6000 凝胶基质中在 60°C 下保持初始活性的 95%。固定化漆酶的最大速率比游离漆酶大约小 21.03%和 47.22%。

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