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    IMAC application of extracellular polymeric substances doped composite membranes for α-amylase immobilization and kinetic studies
    (Elsevier, 2024) Bani, Nurullah; Inanan, Tulden; Acet, Omur; Odabasi, Mehmet
    Immobilized metal affinity chromatography (IMAC), extensively utilized technique in affinity chromatography, has proven to be highly effective in purifying alpha-amylase, a crucial enzyme in industrial applications. Here, Poly (2-hydroxyethyl methacrylate) (PHEMA) based composite membranes were fabricated using the radical copolymerization technique in a petri dish. Extracellular polymeric materials (EPS) as the metal binding agent. The attachment of Cu 2+ ions to the membranes occurred through the utilization of EPSs (Cu 2+ -EPS). The membranes having Cu 2+ -EPS (Cu 2+ -EPS-PM) were subjected to various characterization techniques, including scanning electron microscopy (SEM), attenuated total reflectance-fourier transform infrared spectroscopy (ATR-FTIR), swelling tests, and surface area measurements. The investigation also encompassed the examination of various factors, including pH, initial alpha-amylase concentration, temperature, and ionic strength, that exert an influence on the adsorption of alpha-amylase from an aqueous medium. The Cu 2+ -EPS-PMs demonstrated maximum adsorption capacity with a value of 54.2 mg/g polymer (pH 5.0 sodium acetate buffer, temperature: 25 degrees C, initial alpha-amylase concentration of 2 mg/mL). Additionally, it has been observed that the enzyme is able to be used in adsorption and desorption cycles on Cu 2+ -EPS-PM many times. The investigation also focused on examining the impact of pH, temperature, storage, and operational stability over the activities of both free and immobilized alpha-amylase. The outcomes showed that immobilization had positive effects on activity.
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    Öğe
    Molecular imprinted polymers: important advances in biochemistry, biomedical and biotechnology
    (Springer, 2024) Acet, Burcu Onal; Inanan, Tulden; Salieva, Kalipa; Borkoev, Bakyt; Odabasi, Mehmet; Acet, Omur
    Molecularly imprinted polymers (MIPs) are handmade receptors that mimic the binding of natural antibodies. In other words, MIPs can selectively bind to the target molecule and qualify as bio-inspired synthetic materials. Today, MIPs are used extensively and are being developed further for biological applications. High cost and time consuming techniques are compelling factors for the field of biochemistry, biomedicine and biotechnology (3B), and there is an urgent need for an alternative, cheap, easy to produce, fast and effective method in these fields. MIPs stand out as a promising way for this purpose. MIPs have superiorities such as specific recognition specificity, excellent sensitivity selectivity and reusability. From this point of view, we examined MIP-related drug delivery studies, cell recognition, enzyme applications, in vivo applications, and applications for some important biomolecules. The aim of this review is to compile the utilizations, advantages, important developments and future expectations of MIPs for the fields of 3B.
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    Öğe
    α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors
    (Springer, 2021) Acet, Omur; Inanan, Tulden; Acet, Burcu Onal; Dikici, Emrah; Odabasi, Mehmet
    Stability of enzymes is a significant factor for their industrial feasibility. alpha-Amylase is an important enzyme for some industries, i.e., textile, food, paper, and pharmaceutics. Pumice particles (PPa) are non-toxic, natural, and low-cost alternative adsorbents with high adsorption capacity. In this study, Cu2+ ions were attached to pumice particles (Cu2+-APPa). Then, Cu2+-APPa embedded composite cryogel was synthesized (Cu2+-APPaC) via polymerization of gel-forming agents at minus temperatures. Characterization studies of the Cu2+-APPaC cryogel column were performed by X-ray fluorescence spectrometry (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) method. The experiments were carried out in a continuous column system. alpha-Amylase was adsorbed onto Cu2+-APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized alpha-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. k(cat) value of the immobilized alpha-amylase is higher than that of the free alpha-amylase while K-M value increases by immobilization. Storage and operational stabilities of the free and the immobilized alpha-amylase were determined for 35 days and for 20 runs, respectively.