ArticleBMC biotechnology2017
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization.
Article in BMC biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 63 citations in OpenAlex.
- Immobilized enzymes: exploring its potential in food industry applications.Food science and biotechnology · 2025Review
- Cold-Active Enzymes and Their Potential Industrial Applications-A Review.Molecules (Basel, Switzerland) · 2022Review
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Highly Efficient Computationally Derived Novel Metagenome α-Amylase With Robust Stability Under Extreme Denaturing Conditions.Frontiers in microbiology · 2021Article
- Magnetic Iron Oxide Nanoparticle (IONP) Synthesis to Applications: Present and Future.Materials (Basel, Switzerland) · 2020Review
- Microbial Alpha-Amylase Production: Progress, Challenges and Perspectives.Advanced pharmaceutical bulletin · 2020Review
- Low-Cost Cellulase-Hemicellulase Mixture Secreted byInternational journal of molecular sciences · 2020Article
- Aspergillus oryzae S2 AmyA amylase expression in Pichia pastoris: production, purification and novel properties.Molecular biology reports · 2019Article
- Directly mining a fungal thermostable α-amylase from Chinese Nong-flavor liquor starter.Microbial cell factories · 2018Article
- Living strategy of cold-adapted fungi with the reference to several representative species.Mycology · 2017Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundα-Amylase plays a pivotal role in a broad range of industrial processes. To meet increasing demands of biocatalytic tasks, considerable efforts have been made to isolate enzymes produced by extremophiles. However, the relevant data of α-amylases from cold-adapted fungi are still insufficient. In addition, bread quality presents a particular interest due to its high consummation. Thus developing amylases to improve textural properties could combine health benefits with good sensory properties. Furthermore, iron oxide nanoparticles provide an economical and convenient method for separation of biomacromolecules. In order to maximize the catalytic efficiency of α-amylase and support further applications, a comprehensive characterization of magnetic immobilization of α-amylase is crucial and needed.
resultsA novel α-amylase (AmyA1) containing an open reading frame of 1482 bp was cloned from Antarctic psychrotolerant fungus G. pannorum and then expressed in the newly constructed Aspergillus oryzae system. The purified recombinant AmyA1 was approximate 52 kDa. AmyA1 was optimally active at pH 5.0 and 40 °C, and retained over 20% of maximal activity at 0-20 °C. The K
conclusionsA novel α-amylase (AmyA1) from Antarctic psychrotolerant fungus was cloned, heterologous expression in Aspergillus oryzae, and characterized. The detailed report of the enzymatic properties of AmyA1 gives new insights into fungal cold-adapted amylase. Application study showed potential value of AmyA1 in the food and starch fields. In addition, AmyA1 was immobilized on magnetic nanoparticles and characterized. The improved stability and longer service life of AmyA1 could potentially benefit industrial applications.
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