ArticleWorld journal of microbiology & biotechnology2024
Optimization and purification of a novel calcium-independent thermostable, α-amylase produced by Bacillus licheniformis UDS-5.
Article in World journal of microbiology & biotechnology, 2024. 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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4 citing papers in PubMed.
- Construction of an industrial host for the efficient active expression of protein glutaminase (PG) in Bacillus licheniformis.Bioprocess and biosystems engineering · 2026Article
- Bacillus-based probiotics and fermented products as alternatives to antibiotic growth promoters in poultry: Current perspectives.Poultry science · 2026Review
- A cold-adapted and detergent-stable α-amylase from marine bacterium Photobacterium gaetbulicola Gung47Applied microbiology and biotechnology · 2026Article
- Characterization of a Thermostable α-Amylase fromMicroorganisms · 2025Article
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5 authors.
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Abstract
Microbial amylases should essentially remain active at higher temperatures, and in the alkaline pH and a range of surfactants to be suitable as detergent additives. In the present study, a thermophilic amylase producing bacterium, Bacillus licheniformis UDS-5 was isolated from Unai hot water spring in Gujarat, India. It was identified as a potent amylase producer during starch plate-based screening process. Therefore, the physicochemical parameters influencing amylase production were optimized using Plackett-Burman design and Central Composite Design. The amylase was purified through ammonium sulfate precipitation, size exclusion and ion exchange chromatography, achieving the purification fold and yield to be 9.2 and 40.6%, respectively. The enzyme displayed robust stability and activity across a wide range of temperatures and pHs, with an increased half-life and reduced deactivation rate constant. The amylase exhibited optimal catalysis at 70 °C and pH 8. The kinetic studies revealed Km and Vmax values of 0.58 mg/mL and 2528 μmol/mL/min, respectively. Besides, the purified amylase displayed stability in the presence of various metal ions, surfactants, and chelators suggesting its potential for industrial applications, particularly in the detergent industry. Moreover, detergent application studies demonstrated its efficacy in enhancing washing performance. A comparative profile on washing efficiency of the studied amylase and the commercial amylase with various detergents pointed towards its possible future use as a detergent additive.
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