Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency
- PMID: 28478894
- DOI: 10.1016/j.biortech.2017.04.098
Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency
Retraction in
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Retraction notice to "Molecular improvements in microbial α-amylases for enhanced stability and catalytic efficiency" [Bioresour. Technol. 245 (2017) 1740-1748].Bioresour Technol. 2025 Jan;415:131675. doi: 10.1016/j.biortech.2024.131675. Epub 2024 Oct 23. Bioresour Technol. 2025. PMID: 39447505 No abstract available.
Abstract
α-Amylases is one of the most important industrial enzyme which contributes to 25% of the industrial enzyme market. Though it is produced by plant, animals and microbial source, those from microbial source seems to have potential applications due to their stability and economic viability. However a large number of α-amylases from different sources have been detailed in the literature, only few numbers of them could withstand the harsh industrial conditions. Thermo-stability, pH tolerance, calcium independency and oxidant stability and starch hydrolyzing efficiency are the crucial qualities for α-amylase in starch based industries. Microbes can be genetically modified and fine tuning can be done for the production of enzymes with desired characteristics for specific applications. This review focuses on the native and recombinant α-amylases from microorganisms, their heterologous production and the recent molecular strategies which help to improve the properties of this industrial enzyme.
Keywords: Amylases; Bioprocesses; Fermentation; Recombinant; Site-directed mutagenesis.
Copyright © 2017 Elsevier Ltd. All rights reserved.
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