Abstract

Over the past few decades, enzyme-based green and sustainable chemistry has attracted extensive research attention, which provides a promising alternative to the conventional treatment methods of recalcitrant micropollutants. However, enzyme denaturation and stability loss remain critical challenges for its potential applications in industrial wastewater treatment. In this study, laccase from Trametes versicolor (laccase T.) was cross-linked immobilized by ultraporous alumina (UPA) for the sustainable biodegradation of Remazol Brilliant Blue R (RBBR). Through sequential use of an aminosilane coupling agent (3-aminopropyl)triethoxysilane (APTES) and bifunctional cross-linker glutaraldehyde (GA), the synthesized biocatalysts showed better immobilization performances (about 4-fold to physical adsorption). The GA concentration considerably affected the laccase T. cross-linking degree, while the GA post-treatment protocol showed the highest laccase T. immobilization yield with lower activity recovery. Moreover, the biocatalyst stabilities including pH stability, thermal stability, storage stability, and reusability were also studied. Tolerance to broader pH and temperature ranges, better storage stability, good reusability of laccase T. cross-linked UPA(γ) biocatalysts, and their continuous RBRR biodegradation efficiency highlight the potentials of enzyme-based inorganic materials in industrial wastewater treatment, which can broaden our understanding of their practical applications in environmental fields.

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