Isolation of lysozyme from hen egg albumen using glass fiber-based cation-exchange membranes

Poly(glycidylmethacrylate) brushes generated on poly(VBC) beads by SI-ATRP technique: Hydrazine and amino groups functionalized for invertase adsorption and purification

“…The ligand molecules have different functional groups such as -SO 3 H, -NH 2 , NH, -COOH, -OH and aromatic rings for ionic, polar and hydrophobic interactions. Hydrazine as an affinity ligand has been incorporated on different matrices (i.e., membranes, beads and silica particles) to purify various proteins with affinity interaction [29][30][31][32][33][34][35]. The hydrazine ligand offers several advantages over other ligands in terms of economy, stability and ease of immobilization [29].…”

Sulfanilic acid‐modified chitosan mini‐spheres and their application for lysozyme purification from egg white

“…In comparison with other cation exchange matrices such as alcohol‐insoluble solids from pea pod as chromatographic media, which had a yield of 71.7% using a pretreatment for albumin precipitation with ethanol, the results obtained in this work were better taking also into account that the only pretreatment was a dilution. The pretreatment of egg white solution with ethanol was also used in other cation‐exchange‐based method published by Chiu et al, working with glass fiber‐based membranes, whose yield was 72.6/68.8% depending on the flow rate used.…”

“…However, these methods present disadvantages such as low selectivity in the case of precipitation and the need of special equipment in the case of ultrafiltration and liquid chromatography. Cation exchange chromatography is one of the most effective methods for the purification of Lz from egg white because of the high isoelectric point of this protein (10.7) in comparison with the other proteins present in this source . Bayramoglu et al have published an interesting approach involving the development of chitosan based magnetic beads provided with sulphonic groups, and their utilization for Lz purification from egg white.…”

“…Cation exchange chromatography is one of the most effective methods for the purification of Lz from egg white because of the high isoelectric point of this protein (10.7) in comparison with the other proteins present in this source. 12,[17][18][19][20] Bayramoglu et al 20 have published an interesting approach involving the development of chitosan based magnetic beads provided with sulphonic groups, and their utilization for Lz purification from egg white. The sulphonic groups were incorporated after the beads were grafted with poly (glycidyl methacrylate) by the epoxy groups treatment with sodium sulfite.…”

The optimization of aqueous two‐phase extraction of lysozyme from crude hen egg white using response surface methodology

“…It has been commonly used as a natural preservative in the food industry . Different methods, such as ion exchange chromatography, gel‐filtration chromatography, dye‐binding chromatography, membrane separation, reverse micelles, magnetic cation exchange and ethanol precipitation, can be applied to separate lysozyme from hen egg white in order to prepare commercial product. However, only a few have been implemented at industrial scale.…”