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- W2013130319 abstract "A poly (acrylamide-allylglycidyl ether) [p(AAm-AGE)] cryogel was prepared by radical polymerization of acrylamide (AAm) and allylglycidyl ether (AGE). Cibacron Blue F3GA (CB) was covalently attached to the p(AAm-AGE) cryogel via the reaction between the chloride groups of the reactive dyes and the epoxide groups of the AGE. The CB-attached p(AAm-AGE) cryogel was chelated with Fe3+ ions. This immobilized metal ion affinity chromatography (IMAC) cryogel carrying 25.8 ± 2.0 μmol Fe3+ ions was used in adsorption studies to interrogate the effects of pH, protein initial concentration, flow rate, temperature and ionic strength on enzyme activity. Maximum adsorption capacities were found to be 75.7 ± 1.2 mg/g for p(AAm-AGE)–CB–Fe3+ cryogels and 60.6 ± 1.0 mg/g for p(AAm-AGE)–CB cryogels, respectively. The adsorbed amounts of catalase per unit mass of cryogel reached a plateau value at about 1.5 mg/mL at pH 6.0. The Km values were found to be 0.73 ± 0.02 g/L for the free catalase and 0.18 ± 0.02 g/L for the immobilized catalase. The Vmax value of free catalase (2.0 × 103 U/mg enzyme) was found to be lower than that of the immobilized catalase (2.5 × 103 U/mg enzyme). It was also observed that the enzyme could be repeatedly adsorbed and desorbed onto the p(AAm-AGE)–CB–Fe3+ cryogel." @default.
- W2013130319 created "2016-06-24" @default.
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- W2013130319 date "2012-01-01" @default.
- W2013130319 modified "2023-10-18" @default.
- W2013130319 title "Immobilization of catalase via adsorption onto metal-chelated affinity cryogels" @default.
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- W2013130319 doi "https://doi.org/10.1016/j.procbio.2011.09.021" @default.
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