ArticleProtein and peptide letters2019
Influence of Calcium Ions on the Thermal Characteristics of α-amylase from Thermophilic Anoxybacillus sp. GXS-BL.
Article in Protein and peptide letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 50 citations in OpenAlex.
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- Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from ThermotolerantJournal of microbiology and biotechnology · 2024Article
- Challenges and prospects of microbial α-amylases for industrial application: a review.World journal of microbiology & biotechnology · 2023Review
- An Accessible Method to Improve the Stability and Reusability of Porcine Pancreatic α-Amylase via Immobilization in Gellan-Based Hydrogel Particles Obtained by Ionic Cross-Linking with MgMolecules (Basel, Switzerland) · 2023Article
- Anoxybacillus: an overview of a versatile genus with recent biotechnological applications.World journal of microbiology & biotechnology · 2023Review
- A flexible kinetic assay efficiently sorts prospective biocatalysts for PET plastic subunit hydrolysis.RSC advances · 2022Article
- Structural Insight into a Yeast Maltase-TheJournal of fungi (Basel, Switzerland) · 2021Article
- Frationation of hydrolysate from corn germ protein by ultrafiltration: In vitro antidiabetic and antioxidant activity.Food science & nutrition · 2020Article
- Extremophile Microbial Communities and Enzymes for Bioenergetic Application Based on Multi-Omics Tools.Current genomics · 2020Review
- Recent Development of Extremophilic Bacteria and Their Application in Biorefinery.Frontiers in bioengineering and biotechnology · 2020Review
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9 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundα-Amylases are starch-degrading enzymes and used widely, the study on thermostability of α-amylase is a central requirement for its application in life science and biotechnology.
objectiveIn this article, our motivation is to study how the effect of Ca2+ ions on the structure and thermal characterization of α-amylase (AGXA) from thermophilic Anoxybacillus sp.GXS-BL.
methodsα-Amylase activity was assayed with soluble starch as the substrate, and the amount of sugar released was determined by DNS method. For AGXA with calcium ions and without calcium ions, optimum temperature (Topt), half-inactivation temperature (T50) and thermal inactivation (halflife, t1/2) was evaluated. The thermal denaturation of the enzymes was determined by DSC and CD methods. 3D structure of AGXA was homology modeled with α-amylase (5A2A) as the template.
resultsWith calcium ions, the values of Topt, T50, t1/2, Tm and ΔH in AGXA were significantly higher than those of AGXA without calcium ions, showing calcium ions had stabilizing effects on α-amylase structure with the increased temperature. Based on DSC measurements AGXA underwent thermal denaturation by adopting two-state irreversible unfolding processes. Based on the CD spectra, AGXA without calcium ions exhibited two transition states upon unfolding, including α- helical contents increasing, and the transition from α-helices to β-sheet structures, which was obviously different in AGXA with Ca2+ ions, and up to 4 Ca2+ ions were located on the inter-domain or intra-domain regions according to the modeling structure.
conclusionThese results reveal that Ca2+ ions have pronounced influences on the thermostability of AGXA structure.
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