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    A novel lanthanide-chelate based molecularly imprinted cryogel for purification of hemoglobin from blood serum: An alternative method for thalassemia diagnosis
    (Elsevier Sci Ltd, 2020) Dolak, Ibrahim; Canpolat, Gurbet; Onat, Ruken; Kecili, Rustem; Baysal, Zubeyde; Ziyadanogullari, Berrin; Ersoz, Arzu
    Purification and analyzing of proteins is an essential means for understanding their function and diseases associated with their lack or defect. In this research, a new lanthanide-chelate based molecularly imprinted polymer (MIP) was synthesized for selective separation of Hemoglobin (Hb) from human serum in the presence of various interference molecules. The Hb-imprinted polymer was prepared by using complex functional monomer N-methacryloylamido antipyrine (MAAP)-Ce(III) and 2-Hydroxyethyl methacrylate (HEMA) in accordance of cryopolymerization techniques. The nonimprinted cryogel (NIP) was also prepared at same polymerization conditions in the absence of template Hb molecule. The effects of pH, initial Hb concentration, flow rate, temperature and ionic strength on the binding capacity of both imprinted and nonimprinted cryogels was investigated. The maximum binding capacity for the MIP column was found to be as 79.41 mg g(-1) dry cryogel, that is four times higher than the NIP column under the optimum conditions (pH 5.0, flow rate: 1.0 mL min(-1), T: 25 degrees C). Moreover, selectivity experiments were performed by using two interference proteins as myoglobin (Mb) and cytochrome c (Cyt-c) and the relative selectivity coefficients (k') for Hb/Mb and Hb/Cyt-c pairs were determined as 36.59 and 37.22, respectively.
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    Development of molecular imprinting-based smart cryogels for selective recognition and separation of serum cytochrome-c as a biochemical indicator
    (Elsevier Sci Ltd, 2021) Canpolat, Gurbet; Dolak, Ibrahim; Onat, Ruken; Kecili, Rustem; Baysal, Zubeyde; Ziyadanogullari, Berrin; Ersoz, Arzu
    The recognition and detection of proteins has an important role in the fields of biochemistry and medicine in term of diagnosis and prognosis. In this study, molecularly imprinted cryogel (MIP) was synthesized for the selective recognition of Cytochrome-c (Cyt-c) by cryopolymerization techniques with the lanthanide-chelate approach using (MAAP)2-Ce(III) as complex functional monomer and Cyt-c as a template protein. The incorporation of template with monomer was characterized by near- infrared (Near-IR) spectroscopy. The binding capacity was optimized in accordance with numerous experimental parameters including pH, initial Cyt-c concentration, flow rate, temperature and ionic strength. As a result, the maximum binding capacity reached to 98.33 mg g-1 in a buffer system with a pH of 6.0. Beside of the excellent reusability performance of prepared MIP, it was successfully applied to separation of template Cyt-c in the existence of hemoglobin (Hb) and myoglobin (Mb) chosen as interfering proteins. The relative selectivity constants of the Cyt-imprinted polymer were determined as 13.84 for the Cyt/Mb pair and 16.05 for the Cyt/Hb pair. Consequently, a high selectivity, simple and cheap strategy for efficient separation of proteins was provided with this novel MIP cryogel.
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    Preconcentration with Bacillus subtilis-Immobilized Amberlite XAD-16: Determination of Cu2+ and Ni2+ in River, Soil, and Vegetable Samples
    (Taylor & Francis Inc, 2015) Okumus, Veysi; Ozdemir, Sadin; Kilinc, Ersin; Dundar, Abdurrahman; Yuksel, Uyan; Baysal, Zubeyde
    Solid-phase extraction (SPE) method was developed for the preconcentration of Cu2+ and Ni2+ before their determination by inductively coupled plasma optical emission spectrometry (ICP-OES). Bacillus subtilis-immobilized Amberlite XAD-16 was used as biosorbent. Effects of critical parameters such as pH, flow rate of samples, amount of Amberlite XAD-16 and biosorbent, sample volume, eluent type, and volume and concentration of eluent on column preconcentration of Cu2+ and Ni2+ were optimized. Applicability of the method was validated through the analysis of the certified reference tea sample (NCS ZC73014). Sensitivity of ICP-OES was improved by 36.4-fold for Cu2+ and 38.0-fold for Ni2+ by SPE-ICP-OES method. Limit of quantitation (LOQ) was found to be 0.7 and 1.1ng/ml for Cu2+ and Ni2+, respectively. Concentrations of Cu2+ and Ni2+ were determined by ICP-OES after application of developed method. Relative standard deviations (RSDs) were lower than 4.9% for Cu2+ and 7.9% for Ni2+. The Tigris River that irrigates a large agricultural part of Southeast Turkey is polluted by domestic and industrial wastes. Concentrations of Cu2+ and Ni2+ were determined in water, soil, and some edible vegetables as a biomonitor for heavy metal pollution.
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    PRODUCTION AND CHARACTERIZATION OF PARTIALLY PURIFIED EXTRACELLULAR THERMOSTABLE ?-AMYLASE BY Bacillus subtilis IN SUBMERGED FERMENTATION (SmF)
    (Taylor & Francis Inc, 2011) Ozdemir, Sadin; Matpan, Fatma; Guven, Kemal; Baysal, Zubeyde
    A Bacillus strain was isolated from soil samples from the campus area of Dicle University. Based on 16S ribosomal RNA sequencing, the microorganism was closely related to Bacillus subtilis. Effects of different culture medium, incubation time, carbon and nitrogen sources, and various starches, flours, and chemicals on alpha-amylase production were examined. Maximum enzyme production (7516 U/mL) was obtained in a basal medium A containing 0.05% Tween 40 in 24 h. Partially purified enzyme showed maximum activity at 60 degrees C with an optimum pH of 6.0. The effects of 0.2% detergents (sodium dodecyl sulfate [SDS], CHAPS [3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate], and commercial detergent Omo Matic) on partially purified enzyme activity over a period of time (15-150 min) were examined and the order of inhibition effect from the most to the least was found as SDS> Omo Matic> CHAPS. Different metal ions inhibited alpha-amylase activity at low concentrations (1.5 mM). Co2+ was a mild inhibitor and Hg2+ and Cd2+ were potent inhibitors, whereas Ca2+ and Mg2+ increased the enzyme activity. At 20 mM, Ca2+ enhanced enzyme activity, and different Ca2+ concentrations (10-300 mM) were studied.