Torktaz Ibrahim, Hemmat Jafar, Karkhane Ali Asghar, Rigi Garshasb, Rostami Amin, Khezri Jafar, Behroozi Reza
National Institute of Genetic Engineering and Biotechnology, Tehran, Iran.
Biotechnology Department. Iranian Research Organization for Science and Technology (IROST) Tehran-Iran.
Iran J Biotechnol. 2018 Aug 11;16(3):e1284. doi: 10.15171/ijb.1284. eCollection 2018 Aug.
Considering natural thermal stability, amylase and Cel5E from are good candidates for industrial applications. To be compatible with the industrial applications, this enzyme should be stable in the high temperatures, so any improvement in their thermal stability is valuable.
Using approach and identifying point mutations in the structure amylase of and Cel5E from we tried to increase thermal stability of the enzymes along with their catalytic activity to reach a new industrial amylase with higher thermostability and an improved function.
In this study we predicted the 3D structure of the enzymes, then simulated the molecular docking study using MolDock, PLANTS, and Lamarkian genetic algorithm as scoring functions for the docking and in silico engineering of the protein aiming to increase the thermal stability and catalytic activity.
A series of thermal stability increasing point mutations were exerted around the active site of the enzyme, then by docking procedure, the binding affinity was measured and finally a list of mutations which theoretically improved the increased thermal stability as well as catalytic activity were proposed.
Based on the results obtained the modified enzymes seems to be suitable candidates for considering in both laboratory and industrial scales.
考虑到天然热稳定性，[来源未提及]的淀粉酶和Cel5E是工业应用的良好候选酶。为了与工业应用兼容，这种酶应在高温下稳定，因此提高它们的热稳定性具有重要价值。
通过[未提及的方法]并鉴定[来源未提及]的淀粉酶和Cel5E结构中的点突变，我们试图提高酶的热稳定性及其催化活性，以获得一种具有更高热稳定性和改进功能的新型工业淀粉酶。
在本研究中，我们预测了酶的三维结构，然后使用MolDock、PLANTS和拉马克遗传算法模拟分子对接研究，作为对接和蛋白质计算机工程的评分函数，旨在提高热稳定性和催化活性。
在酶的活性位点周围进行了一系列提高热稳定性的点突变，然后通过对接程序测量结合亲和力，最后提出了一系列理论上提高热稳定性和催化活性的突变列表。
基于获得的[未提及的结果]，修饰后的酶似乎是实验室和工业规模应用的合适候选酶。
