ISSN: 0973-7510

E-ISSN: 2581-690X

Sahar Jafari-Dehkordi1, Zahra Aghili2, Saharnaz Ahmadi2, Sepideh Jabbari2, Ilia Rezazadeh3, Rahele Hasani2 and Reza Rasoolzadeh4
1Department of Genetic, Shahrekord Branch, Shahrekord University, Shahrekord, Iran.
2Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
3Faculty of Sciences, Najafabad Branch, Islamic Azad University, Najafabad, Esfahan, Iran.
4Young Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran.
J Pure Appl Microbiol. 2015;9(1):607-611
© The Author(s). 2015
Received: 06/04/2014 | Accepted: 19/08/2014 | Published: 31/03/2015
Abstract

Among the wide variety of amylolytic enzymes synthesized by microorganisms, α-amylases are the most widely used in industry. α-amylase (α-1,4-glucan-4-glucanohydrolase, E.C.3.2.1.1) is alternatively known as 1,4-α-D-glucan glucanohydrolase or glycogenase and releasing α-anomeric products. These enzymes randomly cleave the α-1,4-glycosidic linkages in starch, generating maltose and malto-oligosaccharides. Amylases constitute a class of industrial enzymes representing approximately 30% of the world enzyme production. Thermostable enzymes are therefore highly attractive and have increasing attention because of their potential use in biotechnological processes. The purpose of this study was to evaluate the activity of the enzyme α-amylase at different temperatures. For this purpose was used HyperChem 8.0.8 software. HyperChem is a powerful program that enables us to do high quality molecular calculations. HyperChem puts more molecular modeling tools at your fingertips than any other windows program. Temperature was chosen at five levels 298, 310, 318, 333 and 358 K. Results of this study for Epot in Amber for five levels temperatures 298, 310, 318, 333 and 358 K was 1151.84, in bio obtained 5881.64, 6019.84, 6294.26, 6558.46 and 7026.43 and in opls obtained -18610, -18432, 18303, 15603 and -17880. Total energy for Amber, bio and opls respectively, were included 1151.843, 11457.08 and -8369.65 Kcalmol-1.

Keywords

α-amylase, Molecular mechanics, Thermostable enzyme

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© The Author(s) 2015. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.