Separation Of Bovine Hemoglobin Research Articles

Lotus seedpod-like molecularly imprinted polymers fabricated by MOF-808 stabilized Pickering emulsion and their specific recognition of hemoglobin

Herein, a new type of surface cellular protein imprinted polymers (MIPs) with inner macropores was fabricated via surface imprinting technology based on surface-modified Metal Organic Framework (MMOF-808) stabilized Pickering emulsion polymerization, and the MIPs were further used for selective adsorption and separation of bovine hemoglobin (BHb). For the first time, silane coupling agent modified MOF-808 particles were applied to stabilize a O/W emulsion, followed by the self-assembly of dopamine in the presence of BHb in the outer phase (PBS solution). SEM images proved that the MIPs possessed cellular structures, and the lotus seedpod-like structure could encourage more imprinted sites distributed on the surface of the polymeric materials, bringing about the imprinted sites easy accessibility. The static adsorption behaviors followed the Scatchard model with an equilibrium adsorption capacity of 406 mg g−1 and pseudo-first-order kinetics with the equilibrium adsorption time of 50 min. Moreover, the cellular polymers exhibited a prominent imprinting effect possessing the imprinting factor of 4.56. Importantly, the polymeric materials could be repeatedly used for rebinding bovine hemoglobin without significant loss in adsorption capacity. Therefore, the proposed approach we described in this work will provide a good reference in the separation and enrichment of biomacromolecules in aqueous solution.

A facile method to synthesize magnetic nanoparticles chelated with Copper(II) for selective adsorption of bovine hemoglobin

A novel and uncomplicated synthesis method of Cu2+-chelating with carboxyl groups that directly-modified NiFe2O4 magnetic microspheres (NiFe2O4-PAA-Cu2+) was fabricated for selective enrichment and separation of bovine hemoglobin (BHb). First, a carboxyl group directly-modified on NiFe2O4 magnetic microspheres was gained through a facile one-pot solvothermal method. Second, Cu2+ from CuSO4 was brought into use to react with carboxyl groups under mechanical stirring at room temperature. The resulting magnetic microspheres were characterized by distinct instruments that included transmission electron microscopy (TEM), Brunauer-Emmett-Teller (BET), Fourier transform infrared spectroscopy (FT-IR), X-ray photoelectron spectroscopy (XPS), vibrating sample magnetometer (VSM) and scanning electron microscope (SEM) to examine the size, morphology, composition and magnetization characterization. The results indicated that the NiFe2O4-PAA-Cu2+ microspheres exhibited good saturation magnetization (36.686 emu g−1), which can facilitate magnetic separation under the help of an outside magnetic field. Also, good dispersion and high adsorption ability to BHb (783.53mg g−1) can be applied to selective enrichment for bovine hemoglobin and used for selective sorption of BHb protein in bovine blood samples.

Facile synthesis of Cu2+-immobilized imprinted cotton for the selective adsorption of bovine hemoglobin

Degreasing cotton showing selectivity for the bovine hemoglobin (BHb) was developed by an imprinting procedure that is based on metal coordinate interaction. The morphological structure of the as-prepared samples was characterized by Scanning Electron Microscopy, and the chemical modification steps were characterized by Fourier Transform Infrared Spectroscopy. The results of adsorption experiments show that the maximum adsorption capacity of the Cu2+-immobilized molecularly imprinted cotton (Cu2+-MIC) and Cu2+-immobilized non-imprinted cotton (Cu2+-NIC) was 140.33 mg/g and 17.78 mg/g, respectively, at the optimum pH value of 6.2. The adsorption process followed a pseudo-second-order kinetic and the adsorption equilibrium could be achieved in 30 min. The adsorption isotherm data could be well described by a Langmuir model. Moreover, satisfactory reusability is demonstrated by five adsorption–desorption cycles with no significant decrease of the adsorption capacity. The SDS-PAGE analysis demonstrated that the Cu2+-MIC could be applied successfully in separation of BHb from the bovine blood sample. This procedure presents facile, cheap and stable fabrication strategy for efficient separation of proteins.

Separation of bovine hemoglobin using novel magnetic molecular imprinted nanoparticles.

Magnetic molecular imprinted nanoparticles (MMIPs), combining the progressiveness of magnetic nanoparticles and surface molecular imprinting technology, have attracted increasing attention because of the high efficiency and specificity in isolation and enrichment of the target protein. This study focused on the preparation of bovine hemoglobin MMIPs with bovine hemoglobin (BHb) as the template protein and the molecular imprinted polymer covering the functional magnetic nanoparticles modified with silane and acrylic groups. The physicochemical characteristics as well as the dynamics and isothermal adsorption properties of the generated nanoparticles were investigated to determine their efficiency and specificity in the adsorption of target protein. The maximum adsorption of the target protein was 169.29 mg g−1 at a specific pH, which was much larger than those obtained in some other research reports. MMIPs showed favorable selectivity towards BHb in a mixture of three different proteins. The results indicated the significant effects and broad prospects of MMIPs in the isolation and enrichment of specific proteins in the field of food, medicine and biological research.

Magnetic deep eutectic solvents molecularly imprinted polymers for the selective recognition and separation of protein

A novel and facile magnetic deep eutectic solvents (DES) molecularly imprinted polymers (MIPs) for the selective recognition and separation of Bovine hemoglobin (BHb) was prepared. The new-type DES was adopted as the functional monomer which would bring molecular imprinted technology to a new direction. The amounts of DES were optimized. The obtained magnetic DES-MIPs were characterized with fourier transform infrared spectrometry (FT-IR), thermogravimetric analysis (TGA), field emission scanning electron microscope (FESEM), dynamic light scattering (DLS), elemental analysis and vibrating sample magnetometer (VSM). The results suggested that the imprinted polymers were successfully formed and possessed a charming magnetism. The maximum adsorption capability (Qmax) and dissociation constant (KL) were analyzed by Langmuir isotherms (R2 = 0.9983) and the value were estimated to be 175.44 mg/g and 0.035 mg/mL for the imprinted particles. And the imprinted particles showed a high imprinting factor of 4.77. In addition, the magnetic DES-MIPs presented outstanding recognition specificity and selectivity so that it can be utilized to separate template protein from the mixture of proteins and real samples. Last but not least, the combination of deep eutectic solvents and molecular imprinted technology in this paper provides a new perspective for the recognition and separation of proteins.

Polydopamine-based molecular imprinting on silica-modified magnetic nanoparticles for recognition and separation of bovine hemoglobin

Surface molecular imprinting, especially on the surface of silica-modified magnetic nanoparticles, has been proposed as a promising strategy for protein recognition and separation. Inspired by the self-polymerization of dopamine, we synthesized a polydopamine-based molecular imprinted film coating on silica-Fe(3)O(4) nanoparticles for recognition and separation of bovine hemoglobin (BHb). Magnetic molecularly imprinted nanoparticles (about 860 nm) possess a core-shell structure. Magnetic molecularly imprinted nanoparticles (MMIP) show a relatively high adsorption capacity (4.65 ± 0.38 mg g(-1)) and excellent selectivity towards BHb with a separation factor of 2.19. MMIP with high saturation magnetization (10.33 emu g(-1)) makes it easy to separate the target protein from solution by an external magnetic field. After three continuous adsorption and elution processes, the adsorption capacity of MMIP remained at 4.30 mg g(-1). Our results suggest that MMIPs are suitable for the removal of high abundance of protein and the enrichment of low abundance of protein in proteomics.

Free‐flow electrophoresis in solutions of borax and mannitol

AbstractFree‐flow electrophoresis of proteins in solutions of borax and mannitol was investigated. The borax solution represents an equimolar boric acid‐NaOH buffer with a pH of 9.2. On addition of mannitol the pH of the buffer decreases, with increasing polyol concentration, accompanied by a slight decrease in conductivity. Using a 2.5 mM borax solution, buffers with pH from 9.2 to 4.5 can be obtained. Under the influence of the electric field the pH and conductivities of these buffers change in the near‐membrane regions of the separation chamber. Despite the changes the buffers are suitable for electrophoresis of proteins in a free‐flow apparatus. The separation of bovine hemoglobin as well as a mixture of bovine hemoglobin, human serum albumin and cytochrome C in borax‐mannitol solutions is demonstrated at 80–100 mA constant current and a residence time of only 2.0–2.6 min.