Cited by 16Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationBiofuel production and bioconversion

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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Timilsina, Parash Mani, Pandey, Gyanu Raj, Shrestha, Asmita, Ojha, Manish, Karki, Tika Bahadur·2020·Biotechnology Reports

Abstract

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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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)
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
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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