Volume 11, Issue 3 (2020)                   JMBS 2020, 11(3): 23-36 | Back to browse issues page

‎ 20.1001.1.23222115.1399.11.3.5.8

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mahnam K, Mosharf Ghahfarokhi A, Rafieepour H A. Comparative of structure of three isozymes of Glucoamylase in order to determination demonstrator parameters thermal stability of proteins via molecular dynamics simulation. JMBS 2020; 11 (3) :23-36
URL: http://biot.modares.ac.ir/article-22-34119-en.html
Comparative of structure of three isozymes of Glucoamylase in order to determination demonstrator parameters thermal stability of proteins via molecular dynamics simulation
Karim Mahnam * 1, Azin Mosharf Ghahfarokhi2 , Hosein Ali Rafieepour2
1- Department of Biology, Faculty of Science, Shahrekord University, Shahrekord, Iran, Iran, Shahrekord, Shahrekord University, Faculty of Science, Department of Biology , mahnam.karim@sci.sku.ac.ir
2- Department of Cell and Molecular Biology, Faculty of Chemistry, Kashan University, Kashan, Iran
Abstract:   (3774 Views)
Glucoamylase, is an important economic enzyme due to its ability to hydrolyze starch and β-D-glucose polymers. Understanding of factors affecting the thermal stability of the glucoamylase enzyme is critical in the production of isoenzymes with high heat or cold stability.  In this study, the effect of temperature on the structure and properties of each of the isoenzymes of the mesophilic, thermophilic and psychrophilic glucoamylase were studied. For this purpose, molecular dynamics simulation was used to assess these factors and structural differences. 240 nanosecond of MD simulation was done for three isoenzymes of glucoamylase in four temperatures at 300, 350, 400 and 450 K. The variations of each of these parameters were compared for three isoenzymes, and it was found that among the computable factors in molecular dynamics simulation, electrostatic energy of protein with water, van der Waals energy between proteins and water, free energy solubility (∆Gsolvation), instability parameter, nonpolar solvent accessible surface, and total solvent accessible surface can be used to predict thermal stability of a protein during increase of temperature.
 
Keywords: Glucoamylase enzyme, Mesophile, Thermophile, Psychrophile, Molecular dynamics simulation, Thermal stability
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Article Type: Original Research | Subject: Bioinformatics
Received: 2019/06/22 | Accepted: 2020/07/5 | Published: 2020/10/2
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