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Metal affinity immobilization of cellulase on Fe3O4 nanoparticles with copper as ligand for biocatalytic applications
- Abbaszadeh, Mohaddeseh, Hejazi, Parisa
- Food chemistry 2019 v.290 pp. 47-55
- carboxymethylcellulose, copper, copper nanoparticles, endo-1,4-beta-glucanase, enzyme activity, hydrolysis, immobilized enzymes, industry, iron oxides, ligands, magnetism, pH, storage temperature, working conditions
- The immobilization of cellulase on amine-functionalized Fe3O4 magnetic nanoparticles (MNPs), via metal affinity immobilization, as a nano-biocatalyst was investigated. Copper was chosen as ligand and loaded onto MNPs in a buffering environment without adding any intermediates. Immobilization conditions were optimized by a 23 full factorial design method. Under optimized working conditions (Cu/MNPs = 1, E/MNPs = 0.11, pH = 6), the relative enzyme activity and the amount of enzyme immobilization were 91% and 164 (mg enzyme/g MNPs), respectively. The immobilized cellulase (tested by carboxymethyl cellulose hydrolysis at 1% concentration) was found to be more stable than the free enzyme. Also, the immobilized enzyme still retained 73% of its initial activity after five cycles of usage. Furthermore, the free and immobilized cellulases retained 70 and 84% of their initial activity after eight days storage at 4 °C, respectively. Immobilization of enzymes, using this method, could be a good and economic option for various industries.