Dye-affinity functionalized magnetic nanoparticles enable direct immobilization of cellulase from cell-free microbial culture medium
Year: 2026
Type: article
Abstract: Enzyme recovery and purification remain major challenges for the economical application of enzymes. In this study, one-step separation and immobilization of cellulase from fermentation medium of Trichoderma reesei was investigated using dye-affinity-functionalized Fe₃O₄ magnetic nanoparticles (MNPs), with multi-covalent coupling proposed as a possible immobilization mechanism. This approach achieved a selective enzyme immobilization with a loading capacity of 70.29 ± 0.99 mg Protein g Support −1 and immobilization yield of 33.16 ± 0.83%. Evaluations of the catalytic activities of the immobilized biocatalyst showed the endoglucanase, exoglucanase, and β -glucosidase activities of about 143.3, 62.9, and 63.1% in comparison with the original free cellulase, respectively. The immobilized cellulase was stable in repeated saccharification cycles of carboxymethylcellulose and sustained 70.12% of the original activity after six cycles. Also, the immobilized biocatalysts retained 100% activity after being stored at 4 °C for 180 days. Further evaluation of the immobilized biocatalyst was performed on the hydrolysis of paper waste at different initial concentrations. The Michaelis-Menten model with observable constants of K m = 4.142 ± 0.700 mg mL − 1 and V max = 0.043 ± 0.003 µmol Glucose mg Protein −1 h − 1 well-described this hydrolysis reaction. Therefore, the developed biocatalyst shows promising potential for the enzymatic conversion of paper waste into value-added products.
Source: Scientific Reports
Authors: Malihe Hadadi, Alireza Habibi
Institution: Razi University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,690
OpenAlex ID: W7220436770