Immobilization of peroxidase on textile carrier materials and their application in the bleaching of colored whey

Textiles represent promising support materials tor enzymes. The goal of the present work was to investigate the immobilization of commercial peroxidase on a polyester needle felt and the repeated use in the gentle degradation of norbixin in whey from dairy cheese as a practical application. High enzyme loads were obtained by a 2-step immobilization procedure. First, the number of functional groups on the textile surface was increased by a modification with amino-functional polyvinylamine. Second, the enzyme was immobilized by using 2 types of crosslinking agents. Due to the iron content of peroxidase, inductively coupled plasma-optical emission spectrometry was used for the quantitative determination of the enzyme load on the textile. The enzyme activity was evaluated using common 2,2'-azino-di-(3-ethylbenzthiazoline-6-sulfonic acid) assay for peroxidases. By the variation of enzyme input and crosslinker concentration, a maximal enzyme load of 80 mg/g of textile was achieved, and a maximum specific activity of 57 U/g of textile. For the visualization of the enzyme on the fiber surface, fluorescence microscopy as well as scanning probe microscopy were used. The immobilized peroxidase showed significant activity, even after 50 reuse cycles. In addition, the potential of the new support and enzyme combination hi commercial whey bleaching was demonstrated successfully on a 10-L scale.

Automated summary

Textiles are a promising support material for enzymes, with this study focusing on immobilizing commercial peroxidase on a polyester needle felt for gentle degradation of norbixin in whey. High enzyme loads were achieved through a 2-step immobilization process, allowing for visualization of the enzyme on the fiber surface. The immobilized peroxidase demonstrated significant activity and durability, showing potential for commercial whey bleaching applications.