SynthesisWorld journal of microbiology & biotechnology2022
Hunt for α-amylase from metagenome and strategies to improve its thermostability: a systematic review.
Synthesis in World journal of microbiology & biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 22 citations in OpenAlex.
- Prospects and problems in enzyme immobilization methodology: comprehensive review.Biophysical reviews · 2025Review
- Various Options for Covalent Immobilization of Cysteine Proteases-Ficin, Papain, Bromelain.International journal of molecular sciences · 2025Article
- Optimization and purification of a novel calcium-independent thermostable, α-amylase produced by Bacillus licheniformis UDS-5.World journal of microbiology & biotechnology · 2024Article
- Automated optimization of the solubility of a hyper-stable α-amylase.Open biology · 2024Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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Abstract
With the advent of green chemistry, the use of enzymes in industrial processes serves as an alternative to the conventional chemical catalysts. A high demand for sustainable processes for catalysis has brought a significant attention to hunt for novel enzymes. Among various hydrolases, the α-amylase has a gamut of biotechnological applications owing to its pivotal role in starch-hydrolysis. Industrial demand requires enzymes with thermostability and to ameliorate this crucial property, various methods such as protein engineering, directed evolution and enzyme immobilisation strategies are devised. Besides the traditional culture-dependent approach, metagenome from uncultured bacteria serves as a bountiful resource for novel genes/biocatalysts. Exploring the extreme-niches metagenome, advancements in protein engineering and biotechnology tools encourage the mining of novel α-amylase and its stable variants to tap its robust biotechnological and industrial potential. This review outlines α-amylase and its genetics, its catalytic domain architecture and mechanism of action, and various molecular methods to ameliorate its production. It aims to impart understanding on mechanisms involved in thermostability of α-amylase, cover strategies to screen novel genes from futile habitats and some molecular methods to ameliorate its properties.
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