ArticleArchives of microbiology2021
A novel pH and thermo-tolerant halophilic alpha-amylase from moderate halophile Nesterenkonia sp. strain F: gene analysis, molecular cloning, heterologous expression and biochemical characterization.
Article in Archives of microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 12 citations in OpenAlex.
- A wide array of extreme halophilic enzymes derived from solar salterns of Bejaia in the north of Algeria: a focus on amylases from Haloarcula sp. strain ICHS1, Natrinema altunense strain MS1 and Haloferax gibbonsii strain MS2.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- A cold-adapted and detergent-stable α-amylase from marine bacterium Photobacterium gaetbulicola Gung47Applied microbiology and biotechnology · 2026Article
- Recombinant Expression and Characterization of a New Endogenous and Halophilic GH13_5 Subfamily α-Amylase from Paenibacillus pabuli.Applied biochemistry and biotechnology · 2026Article
- Characterization and Development of Salt-Resistant Aspergillus oryzae for Marine-Derived Enzyme Expression.Applied biochemistry and biotechnology · 2025Article
- Heterologous expression, characterization, and application of recombinant thermostable α-amylase fromBiochemistry and biophysics reports · 2024Article
- Effects of Zinc Compounds on Lysozyme, Peroxidase, and α-Amylase from the Perspective of Oral Health: a Scoping Review.Biological trace element research · 2024Article
- Article
- Heterologous expression and characterization of salt-tolerant β-glucosidase from xerophilic Aspergillus chevalieri for hydrolysis of marine biomass.Archives of microbiology · 2023Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A novel pH and thermo-tolerate halophilic alpha-amylase from moderately halophilic bacterium, Nesterenkonia sp.strain F was cloned and expressed in Escherichia coli. 16S rRNA sequence of the strain shared 99.46% similarities with closely related type species. Also, the genome sequence shared ANI values below 92% and dDDH values below 52% with the closely related type species. Consequently, it is proposed that strain F represents a novel species. The AmyF gene was 1390 bp long and encodes an alpha-amylase of 463 amino acid residues with pI of 4.62. The deduced AmyF shared very low sequence similarity (< 24%) with functionally characterized recombinant halophilic alpha-amylases. The recombinant alpha-amylase was successfully purified from Ni-NTA columns with a molecular mass of about 52 KDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme was active over a wide range of temperature (25-75 °C) and pH (4-9) with optimum activity at 45 °C and 7.5, respectively. Also, although it was active over a various concentrations of NaCl and KCl (0-4 M), increasing activity of the enzyme was observed with increasing concentration of these salts. Low concentrations of Ca
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