Abstract

The immobilization of enzymes is an important strategy to improve their stability and reusability. Enzyme immobilization technology has broad application prospects in biotechnology, biochemistry, environmental remediation, and other fields. In this study, composites of chitosan (CS) and sodium alginate (SA) with Cu2+ forming a double-network crosslinked structure of hydrogels were prepared and used for the immobilization of laccase. Fourier infrared spectroscopy, scanning electron microscopy, and X-ray photoelectron spectroscopy tests revealed that laccase molecules were immobilized on the composite hydrogel surface by a covalent bonding method. Compared to free laccase, the pH, temperature, and storage stability of the immobilized laccase were markedly improved. In addition, the immobilized laccase could be easily separated from the reaction system and reused, and it maintained 81.6% of its initial viability after six cycles of use. Bisphenol A (BPA) in polluted water was efficiently degraded using immobilized laccase, and the factors affecting the degradation efficiency were analyzed. Under the optimal conditions, the BPA removal was greater than 82%, and the addition of a small amount of ABTS had a significant effect on BPA degradation, with a removal rate of up to 99.1%. Experimental results indicated that immobilized laccases had enormous potential in actual industrial applications.

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