ArticleNanomaterials (Basel, Switzerland)2018
The Adsorption of Dextranase onto Mg/Fe-Layered Double Hydroxide: Insight into the Immobilization.
Article in Nanomaterials (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Triggering of Polymer-Degrading Enzymes from Layered Double Hydroxides for Recycling Strategies.International journal of molecular sciences · 2023Article
- Enhanced Removal of Sulfonated Lignite from Oil Wastewater with Multidimensional MgAl-LDH Nanoparticles.Nanomaterials (Basel, Switzerland) · 2021Article
- Layered Double Hydroxide-Based Nanomaterials-From Fundamentals to Applications.Nanomaterials (Basel, Switzerland) · 2019Article
- Applications of Mechanochemically Prepared Layered Double Hydroxides as Adsorbents and Catalysts: A Mini-Review.Nanomaterials (Basel, Switzerland) · 2019Review
- Characterization and mechanism of the effects of Mg-Fe layered double hydroxide nanoparticles on a marine bacterium: new insights from genomic and transcriptional analyses.Biotechnology for biofuels · 2019Article
- In-Situ Growth of NiAl-Layered Double Hydroxide on AZ31 Mg Alloy towards Enhanced Corrosion Protection.Nanomaterials (Basel, Switzerland) · 2018Article
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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
We report the adsorption of dextranase on a Mg/Fe-layered double hydroxide (Mg/Fe-LDH). We focused the effects of different buffers, pH, and amino acids. The Mg/Fe-LDH was synthesized, and adsorption experiments were performed to investigate the effects. The maximum adsorption occurred in pH 7.0 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) buffer, and the maximum dextranase adsorption uptake was 1.38 mg/g (416.67 U/mg); histidine and phenylalanine could affect the adsorption. A histidine tag could be added to the protein to increase the adsorption significantly. The performance features and mechanism were investigated with X-ray diffraction patterns (XRD) and Fourier transform infrared spectra (FTIR). The protein could affect the crystal structure of LDH, and the enzyme was adsorbed on the LDH surface. The main interactions between the protein and LDH were electrostatic and hydrophobic. Histidine and phenylalanine could significantly affect the adsorption. The hexagonal morphology of LDH was not affected after adsorption.
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