Enzyme-triggered approach to reduce water bodies' contamination using peroxidase-immobilized ZnO/SnO2/alginate nanocomposite

Enzyme immobilization on solid support offers advantages over free enzymes by overcoming characteristic limitations. To synthesize new stable and hyperactive nano-biocatalysts (co-precipitation method), ginger peroxidase (GP) was surface immobilized (adsorption) on ZnO/SnO2 and ZnO/SnO2/SA nanocomposite with immobilization efficacy of 94 % and 99 %, respectively. Thereafter, catalytic and biochemical characteristics of free and immobilized GP were investigated by deploying various techniques, i.e., FTIR, PXRD, SEM, and PL. Diffraction peaks emerged at 2 theta values of 26 degrees, 33 degrees, 37 degrees, 51 degrees, 31 degrees, 34 degrees, 36 degrees, 56 degrees, indicating the formation of SnO2 and ZnO. The O-H stretching of the H2O molecules was attributed to broad peaks between 3200 and 3500 cm-1, whereas ZnO/SnO2 spikes occurred in the 1626-1637 cm-1 range. Sn-O stretching mode and Zn-O terminal vibrational patterns have been verified at corresponding wavelengths of 625 cm-1 and 560 cm-1. Enzyme entrapment onto substrate was verified via interactions between GP and ZnO/SnO2/SA as corroborated by signals beneath 1100 cm-1. GP-immobilized fractions were optimally active at pH 5, 50 degrees C, and retained maximum activity after storage of 4 weeks at-4 degrees C. Kinetic parameters were determined by using a Lineweaver-Burk plot and Vmax for free GP, ZnO/SnO2/GP and ZnO/SnO2/SA/GP with guaiacol as a substrate, were found to be 322.58, 49.01 and 11.45 (mu M/min) respectively. A decrease in values of Vmax and KM indicates strong adsorption of peroxidase on support and maximum affinity between nano support and enzyme, respectively. For environmental remediation, free ginger peroxidase (GP), ZnO/SnO2/GP and ZnO/SnO2/SA/GP fractions effectively eradicated highly intricate dye. Multiple scavengers had a significant impact on the depletion of the dye. In conclusion, ZnO/SnO2 and ZnO/SnO2/SA nanostructures comprise an ecologically acceptable and intriguing carrier for enzyme immobilization.

Automated summary

Enzyme immobilization on ZnO/SnO2 and ZnO/SnO2/SA nanocomposites was studied, and the catalytic and biochemical characteristics of the immobilized enzyme were investigated. The results showed that ZnO/SnO2 and ZnO/SnO2/SA nanostructures are suitable carriers for enzyme immobilization.