Immobilization of glucose oxidase for various industrial applications: advances, challenges, and future perspective towards sustainable development goals

Glucose oxidase is a flavin-containing enzyme widely used in biotechnology and biomedical research due to its versatile applications, particularly in cancer and diabetes treatments. As one of the significant enzymes, glucose oxidase possesses properties such as high specificity, stability under various conditions, and the ability to catalyse reactions efficiently, making it an invaluable asset in fields such as biosensing, bioconversion, and bioremediation. However, the free form of glucose oxidase faces challenges related to its reusability, prompting the use of various immobilization techniques including adsorption, covalent attachment, entrapment, and cross-linking to enhance enzyme recycling. The recovery efficiency of the immobilized glucose oxidase was determined to be ranging from 70% to 98%. A biosensor with immobilized glucose oxidase detecting glucose levels achieved a success rate of 90% even after 8 months and increased the power density from 9.6 μW cm–2 to 5.7 mW cm−2. Similarly, immobilized glucose oxidase able to remove the various organic contaminants to be ranging from 81% to 93% in the waste water. The novelty of this review lies in its mechanistic and comparative assessment of immobilization approaches, establishing direct correlations between enzyme – support interactions, electron-transfer pathways, microenvironmental control, and application-specific performance outcomes. Collectively, these insights highlight the critical role of rational immobilization design in realizing the full catalytic and commercial potential of glucose oxidase and in driving the development of sustainable biotechnological solutions that align with five United Nations Sustainable Development Goals.