The textile industry is essential, but it is also responsible for causing environmental problems, particularly the discharge of dyes. In this context, this study aimed to immobilize a previously purified peroxidase, called MoPOX, on glutaraldehyde-activated chitosan beads in order to improve the potential for textile dye decolorization. The chitosan beads were activated with 8% glutaraldehyde for 1 h, and the immobilization was performed at 30 °C, pH 5.2 for 4 h. Scanning Electron Microscopy (SEM) analyses were used to observe the differences in the chitosan beads after immobilization. The optimum temperature dropped from 70 °C to 30 °C after immobilization, but immobilized MoPOX demonstrated excellent heat stability. The optimum pH remained 5.2, while the apparent kinetic constant value (K_m) of immobilized MoPOX (14.67 mM) was lower in comparison to free MoPOX (46.8 mM). The immobilized enzyme showed improved activity after long storage times, and it could retain 40 % of its original activity even after 5 cycles. The potential for decolorization of different textile dyes was considerably enhanced after immobilization, reaching more than 80 %. Also, MoPOX showed no toxicity towards Artemia salina. Overall, the findings point to the promising potential of using immobilized MoPOX as a biocatalyst in a variety of biotechnological applications.

纺织业是必不可少的，但它也造成了环境问题，尤其是染料的排放。在这种情况下，本研究旨在将一种先前纯化的过氧化物酶（称为Mo POX）固定在戊二醛活化的壳聚糖珠上，以提高纺织染料脱色的潜力。壳聚糖珠用 8% 戊二醛活化 1 小时，固定在 30 °C，pH 5.2 下进行 4 小时。使用扫描电子显微镜 (SEM) 分析来观察固定化后壳聚糖珠粒的差异。固定后最适温度从 70 °C 下降到 30 °C，但固定MoPOX 表现出优异的热稳定性。最佳 pH 值保持在 5.2，而固定化Mo POX (14.67 mM)的表观动力学常数值 (K _m )低于游离Mo POX (46.8 mM)。固定化酶在长时间储存​​后显示出更高的活性，即使在 5 个循环后仍可保持其原始活性的 40%。不同纺织染料的脱色潜力在固定后显着增强，达到 80% 以上。此外，Mo POX 对卤虫没有表现出毒性。总体而言，这些发现表明在各种生物技术应用中使用固定化 MoPOX 作为生物催化剂具有广阔的潜力。