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Bio-based Material Protein and Its Novel Applications
Published in Shakeel Ahmed, Saiqa Ikram, Suvardhan Kanchi, Krishna Bisetty, Biocomposites, 2018
Tanvir Arfin, Pooja R. Mogarkar
These are proteins carrying metal ions such as Fe, Mg, Cu, and Co or a colored compound as the prosthetic group due to which the protein appears colored. Examples include chlorophyll in plant, hemoglobin in blood, myoglobin, cytochromes (red colored), flavoproteins (yellow colored), and hemocyanin (blue colored). Metalloproteins are complexes of proteins and heavy metals. In most metalloproteins, the metal is loosely bound and can be easily removed. However, in some proteins such as hemoglobin and myoglobin, the metal iron is firmly bound to the prosthetic group. Liver and spleen contain the metalloproteins ferritin and hemosiderin with about 20% iron content. These are storage forms of iron in animals, which release iron from the proteins when required. Conalbumin from egg can form complex with iron, and it also combines with copper and zinc.
PolyHIPEs for Separations and Chemical Transformations: A Review
Published in Solvent Extraction and Ion Exchange, 2019
Kathryn M. L. Taylor-Pashow, Julia G. Pribyl
Another separations application that has seen extensive use of polyHIPE materials in recent years is the area of protein purification. Unlike the majority of the polyHIPE resins used for metal complexation or ion exchange that were primarily styrene-based foams, the majority of the polyHIPE materials used for protein purification are based on glycidyl methacrylate backbones. The earliest such report of polyHIPEs for protein purification came from Krajnc and coworkers, who prepared polyHIPE monoliths from co-polymerization of glycidyl methacrylate and ethylene glycol dimethacrylate.[28] The epoxy groups on the monomer remained unreacted during the polymerization, and they were then used to further functionalize the material through reaction with diethylamine. The amine functionalization of the material introduced weak anion-exchange groups, which were then used for the protein purification. Chromatographic evaluation was performed using a standard protein mixture containing myoglobin, conalbumin, and trypsin inhibitor. While the dispersion was slightly higher in the polyHIPE samples compared to commercially available materials, the separation was still acceptable.