ArticleBioMed research international2015
Purification and Characterization of a Polyextremophilic α -Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents.
Article in BioMed research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 46 citations in OpenAlex.
- Utilization of potato peels waste for production, purification, and characterization of cold-adapted amylase under solid state fermentation by Penicillium goetzii AUMC 498.Microbial cell factories · 2026Article
- Biotechnological potential of salt tolerant and xerophilic species of Aspergillus.Applied microbiology and biotechnology · 2024Review
- 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
- Metabolic Potential of Halophilic Filamentous Fungi-Current Perspective.International journal of molecular sciences · 2022Review
- Determination of Community Structure and Diversity of Seed-Vectored Endophytic Fungi inFrontiers in microbiology · 2022Article
- A Mesohaline Thraustochytrid Produces Extremely Halophilic Alpha-Amylases.Marine biotechnology (New York, N.Y.) · 2020Article
- AmyZ1: a novel α-amylase from marine bacteriumBiotechnology for biofuels · 2019Article
- Halophiles and Their Vast Potential in Biofuel Production.Frontiers in microbiology · 2019Review
- Phylogeny of xerophilic aspergilli (subgenusStudies in mycology · 2017Article
- Optimization, Purification, and Starch Stain Wash Application of Two NewBioMed research international · 2017Article
- Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An extracellular α-amylase from the obligate halophilic Aspergillus penicillioides TISTR3639 strain was produced and enriched to apparent homogeneity by ammonium sulfate precipitation and Sephadex G100 gel filtration column chromatography. The mass of the purified amylase was estimated to be 42 kDa by SDS-PAGE. With soluble starch as the substrate it had a specific activity of 118.42 U · mg(-1) and Vmax and Km values of 1.05 µmol · min(-1) · mg(-1) and 5.41 mg · mL(-1), respectively. The enzyme was found to have certain polyextremophilic characteristics, with an optimum activity at pH 9, 80 °C, and 300 g · L(-1) NaCl. The addition of CaCl2 at 2 mM was found to slightly enhance the amylase activity, while ZnCl2, FeCl2, or EDTA at 2 mM was strongly or moderately inhibitory, respectively, suggesting the requirement for a (non-Fe(2+) or Zn(2+)) divalent cation. The enzyme retained more than 80% of its activity when incubated with three different laundry detergents and had a better performance compared to a commercial amylase and three detergents in the presence of increasing NaCl concentrations up to 300 g · L(-1). Accordingly, it has a good potential for use as an α-amylase in a low water activity (high salt concentration) and at high pH and temperatures.
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