Immobilizing Redox Enzyme on Amino Functional Group-Integrated Tailor-Made Polyester Textile: High Loading, Stability, and Application in a Bio-Fenton System

Abstract

This study reports the first approach of immobilizing a redox (glucose oxidase-GOx) enzyme on the amino functional group-integrated tailor-made textile (polyester nonwoven fabric-PF) support matrix. To achieve that, polyethylenimine if not chitosan was chemically grafted on plasma (with O2/N2gas)-activated PF before immobilizing the GOx enzyme through physical adsorption. Diverse qualitative and quantitative characterization methods were used to validate the successful activation and GOx immobilization on amino functional group-integrated tailor-made PF. Results showed that integration of amino functional groups on PF offers a great deal of favorable conditions during enzyme immobilization through covalent or ionic interaction between counter functional groups as reflected in high loading (55.46%) and good operational (78.37%) and thermal stability (∼60 °C) with excellent recyclability (60% activity/15-cycles) and poor leaching (22%) of immobilized GOx. Enzymatic reaction kinetics of free and immobilized GOx revealed the existence of relative mass transfer and diffusion limitation of immobilized GOx as apprehended in the apparent Michaelis constant (Km) and maximum velocity of the reaction (Vmax). The resultant immobilized GOx’s were studied for the first time in the removal of pollutants (10 mg L-1crystal violet) from water in a heterogeneous bio-Fenton system. Results showed as high as 88.69% pollutant removal at 1.19 × 10-2min-1following pseudo-first-order kinetic model as supported byR2values beyond 97. These results are of great importance as they provide fundamental evidence and proof of concepts regarding immobilizing biocatalysts on textiles and their potential application in a robust heterogeneous catalytic system for environmental and green chemistry applications.