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Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology

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Abstract

α-Amylase is the most significant glycoside hydrolase having applications in various industries. It cleaves the α,1–4 glucosidic linkages of polysaccharides like starch, glycogen to yield a small polymer of glucose in α-anomeric configuration. α-Amylase is produced by all the three domains of life but microorganisms are preferred sources for industrial-scale production due to several advantages. Enormous studies and research have been done in this field in the past few decades. Still, it is requisite to work on enzyme stability and catalysis, as it loses its functionality in extreme. As the enzyme loses its structural and catalytic property under extreme environmental conditions, it is mandatory to confer some potential strategies for enhancing enzyme behaviour in such conditions. This limitation of an enzyme can be overcome up to some extent by extremophiles. They serve as an excellent source of α-amylase with outstanding features. This review is an attempt to encapsulate some structure-based strategies for improving enzyme behaviour thereby enabling researchers to selectively amend any of the strategies as per requirement during upstream and downstream processing for higher enzyme yield and stability. Thus, it will provide some cutting-edge strategies for tailoring α-amylase producing organism and enzyme with the help of several computational biology tools.

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Acknowledgements

The authors acknowledge the School of Studies in Biotechnology, Pt. Ravishankar Shukla University Raipur, Chhattisgarh for providing facilities to conduct this study. The authors also acknowledge the Department of Biotechnology (DBT), Government of India, New Delhi, for providing financial support as DBT-JRF fellowship to author Nisha Gupta during the tenure of this study (Sanction no. DBTHRDPMU/JRF/BET-20/I/2020/AL/319).

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The idea for writing the review and concept: SKJ, JSP; literature search, analysis and study: JSP, NG, EB, SK, ST; Drafting of review: JSP, NG; Editing: SKJ, JSP, EB; critically revised the work: JSP, NG.

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Correspondence to Jai Shankar Paul.

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All authors declare that they have no conflicts of interest in any part of this study.

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This article does not contain any studies with human and animal participants performed by any of the authors.

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Communicated by S. Albers.

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Gupta, N., Beliya, E., Paul, J.S. et al. Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology. Extremophiles 25, 221–233 (2021). https://doi.org/10.1007/s00792-021-01223-2

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  • DOI: https://doi.org/10.1007/s00792-021-01223-2

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