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. 2021 Aug 30;12:713125. doi: 10.3389/fmicb.2021.713125

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Copyright © 2021 Ariaeenejad, Zolfaghari, Sadeghian Motahar, Kavousi, Maleki, Roy and Hosseini Salekdeh.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Predicted 3D structure of PersiAmy1 obtained from the Phyre2 prediction server. The Conserved Domains Database (CDD) revealed the active sites and alignment of PersiAmy1 and the pfam00150 and cd14256 catalytic domain. (B) Comparison sequences of PersiAmy1 and Thermotoga neapolitana α-amylases (ACF75909.1) were done. The highly conserved sequences and regions are emphasized by a highlight. (C) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram analysis of PersiAmy1.