Purification and characterization of a noble thermostable algal starch liquefying alpha-amylase from Aeribacillus pallidus BTPS-2 isolated from geothermal spring of Nepal
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A thermophilic strain, Aeribacillus pallidus BTPS-2 was isolated from Bhurung geothermal spring of Nepal. The 16 s rRNA sequence showed 99.8 % similarity with the type strain Aeribacillus pallidus DSM 3670. The morphological, physiological and biochemical properties were similar to the type strain. Alpha-amylase from A. pallidus BTPS-2 was purified to 19-fold purification by DEAE-Cellulose ion exchange chromatography. The Km value of amylase on starch was 0.51 ± 0.05 mg/mL. The optimum pH and temperature were 7.0 and 70 °C. SDS-PAGE analysis showed a single band at 100 kDa. The half-life of the enzyme at 80 °C was 2.81 h. The enzyme showed an inhibitory effect in the presence of Fe2+, Pb2+, Sn2+ and Hg2+ at 10 mM concentrations. TLC analysis showed that the enzyme is a liquifying alpha-amylase. The enzyme reduced the viscosity of algal biomass suspension up to 74.2 ± 0.17 % which was more efficient than Bacillus amyloliquefaciens alpha-amylase (80.5 ± 0.2 %).
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α-amylase has an optimal temperature of 95-115 • C and an optimal pH of 5.0-7.5 and is applicable to microalgae.
“α-amylase | | 95-115 • C | 5.0-7.5 | Microalgae | [218]”
From A Review of Algae-Based Carbon Capture, Utilization, and Storage (Algae-Based CCUS) (2024) · cites this paper as [218]
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- Authors
- Timilsina, P. M., Pandey, G. R., Shrestha, A., Ojha, M., & Karki, T. B.
- Affiliations
- Kathmandu University (NP)
- Corresponding author
- Timilsina, Parash Mani
- Venue
- Biotechnology Reports
- Publisher
- Elsevier BV
- Published
- 2020-12
- Volume
- 28
- Pages
- e00551
- ISSN
- 2215-017X (ISSN-L)
- PMC
- PMC7674295
- OpenAlex
- W3094962730
- Cited by
- 16
- References
- 42
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 3
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biotechnology Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Organisation for the Prohibition of Chemical Weapons
- Utenriksdepartementet
- International Foundation for Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
- Keywords
- alpha-amylase, thermostable enzymes, Aeribacillus pallidus, enzyme purification, enzyme characterization, metal ion inhibition
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