Textile Material Technology, Department of Textile Technology, The Swedish School of Textiles, Faculty of Textiles, Engineering and Business, University of Borås, SE-50190, Borås, Sweden.
Ecole Nationale Supérieure des Arts et Industries Textiles (ENSAIT), GEMTEX Laboratory, 2 allée Louise et Victor Champier BP 30329, 59056, Roubaix, France.
Sci Rep. 2019 Oct 31;9(1):15730. doi: 10.1038/s41598-019-52087-8.
Robust immobilization of glucose oxidase (GOx) enzyme was achieved on poly(ethylene terephthalate) nonwoven fabric (PN) after integration of favourable surface functional groups through plasma treatments [atmospheric pressure-AP or cold remote plasma-CRP (N + O)] and/or chemical grafting of hyperbranched dendrimers [poly-(ethylene glycol)-OH or poly-(amidoamine)]. Absorption, stability, catalytic behavior of immobilized enzymes and reusability of resultant fibrous bio-catalysts were comparatively studied. Full characterization of PN before and after respective modifications was carried out by various analytical, instrumental and arithmetic techniques. Results showed that modified polyester having amine terminal functional groups pledged better surface property providing up to 31% enzyme loading, and 81% active immobilized enzymes. The activity of the enzyme was measured in terms of interaction aptitude of GOx in a given time to produce hydrogen peroxide using colorimetric assay. The immobilized GOx retained 50% of its original activity after being reused six (06) times and exhibited improved stability compared with the free enzyme in relation to temperature. The reaction kinetics, loading efficiency, leaching, and reusability analysis of enzyme allowed drawing a parallel to the type of organic moiety integrated during GOx immobilization. In addition, resultant fibrous bio-catalysts showed substantial antibacterial activity against pathogenic bacteria strains (Staphylococcus epidermidis and Escherichia coli) in the presence of oxygen and glucose. These results are of great importance because they provide proof-of-concept for robust immobilization of enzymes on surface-modified fibrous polyester fabric for potential bio-industrial applications.
通过等离子体处理 [常压(AP)或冷远程等离子体(CRP)(N+O)] 和/或超支化树枝状大分子 [聚(乙二醇)-OH 或聚(酰胺胺)] 的化学接枝,在聚对苯二甲酸乙二醇酯非织造织物(PN)上实现了葡萄糖氧化酶(GOx)的稳定固定。比较研究了固定化酶的吸附、稳定性、催化行为和所得纤维状生物催化剂的可重复使用性。通过各种分析、仪器和算法技术对各自改性前后的 PN 进行了充分的表征。结果表明,具有胺端基官能团的改性聚酯具有更好的表面性能,可提供高达 31%的酶负载量和 81%的活性固定化酶。酶的活性通过比色法测量 GOx 在给定时间内与过氧化氢相互作用的能力来衡量。固定化 GOx 在重复使用六次后保留了其原始活性的 50%,并且与游离酶相比,在温度方面表现出更高的稳定性。酶的反应动力学、负载效率、浸出和可重复使用性分析允许将其与 GOx 固定化过程中整合的有机部分的类型进行平行比较。此外,在有氧和葡萄糖存在的情况下,所得纤维状生物催化剂对病原菌(表皮葡萄球菌和大肠杆菌)表现出显著的抗菌活性。这些结果非常重要,因为它们为在表面改性的纤维聚酯织物上实现酶的稳定固定提供了概念验证,这对于潜在的生物工业应用具有重要意义。