Yazar "Sanz-Pérez, Eloy S." seçeneğine göre listele

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    Co-evaluation of interaction parameters of genomic and plasmid DNA for a new chromatographic medium
    (Elsevier B.V., 2019) Önal, Burcu; Acet, Ömür; Sanz, Raúl; Sanz-Pérez, Eloy S.; Erdönmez, Demet; Odabaşı, Mehmet
    Preparation of new sorbents specific to DNA has a great significance in many biomedical fields. This study reports a new sorbent with high surface area and porosity to immobilize nucleic acids having both high molecular weight like genomic DNA (gDNA) for potential use in therapy of some immune system disease and low molecular weight like plasmid DNA (pDNA) for diagnosis, gene therapy and DNA vaccination. For this aim, silica-based pore-expanded SBA-15 nanoparticles with aminopropyl-trimethoxysilane (APTMS) for decoration of Fe+3 ions (PE SBA-15-APTMS/Fe+3) were synthesized to get high surface area for high adsorption, and embedded into cryogel column for obtaining interconnected pores to avoid diffusion limitation of DNA samples because of their viscosity features. SEM, XRD, BET, and FTIR techniques were used for characterization of samples. Synthesized hybrid column showed a superior adsorption capacity of 751.5 mg/g NP for gDNA at pH 6 with an initial concentration of 2.0 mg/mL. Hybrid column presented excellent performance for pDNA when evaluated with agarose gel electrophoresis.
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    Öğe
    Comparative study of ASNase immobilization on tannic acid-modified magnetic Fe3O4/SBA-15 nanoparticles to enhance stability and reusability
    (Royal Society of Chemistry, 2020) Noma, Samir Abbas Ali; Ulu, Ahmet; Acet, Ömür; Sanz, Raúl; Sanz-Pérez, Eloy S.; Odabaşı, Mehmet; Ateş, Burhan
    In this work, l-asparaginase was immobilized on tannic acid-modified magnetic mesoporous particles. In brief, Fe3O4/SBA-15/tannic acid magnetic particles were synthesized, and their structures and morphologies were fully characterized using various methods. The properties of the free and immobilized enzyme were examined in terms of pH, temperature, thermal stability, storage stability, and reusability. Moreover, the effects of metal ions, inhibitors and organic solvents on the activity of the immobilized enzyme were investigated. Compared to the free enzyme, the immobilized enzyme possessed better tolerance to changes in ambient temperature and pH. Additionally, thermal incubation results showed that the free enzyme lost its activity, while the immobilized enzyme exhibited the opposite behavior. Most strikingly, the immobilized l-asparaginase exhibited a high degree of activity (70%) after being reused 16 times while also demonstrating 71% and 63% storage stability of the initial activity even after 28 days at 4 °C and room temperature, respectively. Together with these results, l-asparaginase was successfully immobilized upon Fe3O4/SBA-15/tannic acid magnetic nanoparticles with improved stability properties. This support holds great potential and opens up a novel perspective for growing applications.