ArticleInternational journal of molecular sciences2019
Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance.
Article in International journal of molecular sciences, 2019. 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, 28 citations in OpenAlex.
- Molecular cloning and modelling of a thermostable α-amylase from a thermophilic Geobacillus sp. DS3.Biotechnology letters · 2025Article
- Article
- Enhanced saccharification levels of corn starch using as a strategy a novel amylolytic complex (AmyHb) from the thermophilic fungus3 Biotech · 2024Article
- Structural and Functional Characterization ofMolecules (Basel, Switzerland) · 2023Article
- In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites.Molecules (Basel, Switzerland) · 2021Article
- Article
- Development of an active site titration reagent for α-amylases.Chemical science · 2020Article
- Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products.International journal of molecular sciences · 2020Article
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)
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