ArticleMolecules (Basel, Switzerland)2016
Immobilization of α-Amylase from Anoxybacillus sp. SK3-4 on ReliZyme and Immobead Supports.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Crystallization-Assisted Asymmetric Synthesis of Enantiopure Amines Using Membrane-Immobilized Transaminase.Chem & bio engineering · 2025Article
- Recycling the recyclers: strategies for the immobilisation of a PET-degrading cutinase.Bioprocess and biosystems engineering · 2025Article
- Detergent-resistant α-amylase derived from Anoxybacillus karvacharensis K1 and its production based on whey.Scientific reports · 2024Article
- 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
- Improved Performance of D-Psicose 3-Epimerase by Immobilisation on Amino-Epoxide Support with Intense Multipoint Attachment.Foods (Basel, Switzerland) · 2021Article
- Global Transcriptomic Responses ofMicroorganisms · 2020Article
- Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.International journal of molecular sciences · 2019Article
- Special Issue: Enzyme Immobilization 2016.Molecules (Basel, Switzerland) · 2017Article
- Enhanced Performance of Magnetic Graphene Oxide-Immobilized Laccase and Its Application for the Decolorization of Dyes.Molecules (Basel, Switzerland) · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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Abstract
α-Amylase from Anoxybacillus sp. SK3-4 (ASKA) is a thermostable enzyme that produces a high level of maltose from starches. A truncated ASKA (TASKA) variant with improved expression and purification efficiency was characterized in an earlier study. In this work, TASKA was purified and immobilized through covalent attachment on three epoxide (ReliZyme EP403/M, Immobead IB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M) activated supports. Several parameters affecting immobilization were analyzed, including the pH, temperature, and quantity (mg) of enzyme added per gram of support. The influence of the carrier surface properties, pore sizes, and lengths of spacer arms (functional groups) on biocatalyst performances were studied. Free and immobilized TASKAs were stable at pH 6.0-9.0 and active at pH 8.0. The enzyme showed optimal activity and considerable stability at 60 °C. Immobilized TASKA retained 50% of its initial activity after 5-12 cycles of reuse. Upon degradation of starches and amylose, only immobilized TASKA on ReliZyme HFA403/M has comparable hydrolytic ability with the free enzyme. To the best of our knowledge, this is the first report of an immobilization study of an α-amylase from Anoxybacillus spp. and the first report of α-amylase immobilization using ReliZyme and Immobeads as supports.
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