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/N2 gas)-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–1 crystal violet) from water in a heterogeneous bio-Fenton system. Results showed as high as 88.69% pollutant removal at 1.19 × 10–2 min–1 following pseudo-first-order kinetic model as supported by R2 values 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.
Highlights
Enzymes are naturally occurring biocatalysts capable of catalyzing complex reactions in many areas ranging from food industry,[1,2] cosmetics,[3] medical,[4,5] environmental remediation,[6−8] and so on
Results of this study have been presented in three parts: (1) the validation related to activation and surface modification of polyester nonwoven fabrics (PFs); (2) quantitative analysis of glucose oxidase (GOx) immobilization on PF in terms of enzyme loading, leaching, and their stability; and (3) the concept related to heterogeneous bio-Fenton system using biocatalyst-immobilized textiles for the removal of water pollutants
Enzyme immobilization via physical adsorption maintained a part of enzymatic activity after immobilization, since not all free enzymes would be immobilized successfully, and all immobilized enzymes do not necessarily maintain their catalytic activity after the immobilization process, yet the lowermost amount of immobilized active enzymes maintained their catalytic activity after immobilization even after successive uses
Summary
Enzymes are naturally occurring biocatalysts capable of catalyzing complex reactions in many areas ranging from food industry,[1,2] cosmetics,[3] medical,[4,5] environmental remediation,[6−8] and so on. In a typical enzymatic system, it requires additional efforts to separate enzymes from the reaction system, which increases the cost and hinders largescale production. Immobilization or fixing of enzymes to or within solid supports provides high stability, enhances reactivity, and increases the operational half-life, while offering better reaction control and easy recovery of the catalyst from the reaction products and ensuring continuous reusability.[9−11]. A wide variety of materials from inorganic and organic sources have been suggested as a suitable support material for enzyme immobilization including mesoporous materials,[12] nanotubes,[13,14] inorganic nanoparticles,[15,16] organic matrix (synthetic materials and biopolymers),[17,18] and textiles.[19,20]. A perfect support material for immobilization of all enzymes is nonexistent, choosing one is highly subjected to the desired application of immobilized enzyme.[21,22] there are some general characteristics of support materials that are primarily necessary in any application, namely, strength, inexpensiveness, flexibility, durability, versatility, broad accessibility, inertness to the surrounding stimuli, and concentrated decisive affinity toward the desired enzyme.[23,24] Availability of all the abovementioned general characteristics in a naturally available support material is very unlikely; most of the support matrix reported in various literature studies
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