Enhancing enzymatic catalysis efficiency: Immobilizing laccase on HHSS for synergistic bisphenol A adsorption and biodegradation through optimized external surface utilization

Laccase, a prominent enzyme biomacromolecule, exhibits promising catalytic efficiency in degrading phenolic compounds like bisphenol A (BPA). The laccase immobilized on conventional materials frequently demonstrates restricted loading and suboptimal catalytic performance. Hence, there is a pressing...

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Veröffentlicht in:International journal of biological macromolecules 2024-10, Vol.278 (Pt 1), p.134586, Article 134586
Hauptverfasser: Yu, Hongxia, Feng, Lijun, Abbas, Mohamed, Liang, Xue, Zhang, Tianjing, Yang, Guiping, Liu, Yong, Xu, Meisong, An, Yan, Yang, Wanliang
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Sprache:eng
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Zusammenfassung:Laccase, a prominent enzyme biomacromolecule, exhibits promising catalytic efficiency in degrading phenolic compounds like bisphenol A (BPA). The laccase immobilized on conventional materials frequently demonstrates restricted loading and suboptimal catalytic performance. Hence, there is a pressing need to optimized external surface utilization to enhance catalytic performance. Herein, we synthesized amino-functionalized modified silica particles with a hierarchical hollow silica spherical (HHSS) structure for laccase immobilization via crosslinking, resulting in HHSS-LE biocatalysts. Through Box-Behnken design (BBD) and response surface methodology (RSM), we achieved a remarkably high enzyme loading of up to 213.102 mg/g. The synergistic effect of adsorption by HHSS and degradation by laccase facilitated efficient removal of BPA. The HHSS-LE demonstrated superior BPA removal capabilities, with efficiencies exceeding 100 % in the 50–200 mg/L BPA concentration range. Compared to MCM-41 and solid silica spheres (SSS), HHSS showed the highest enzyme loading capacity and catalytic activity, underscoring its superior external surface utilization rate per unit mass. Remarkably, the HHSS-LE biocatalyst exhibited remarkable recyclability even after 11 successive cycles of reuse. By preparing high immobilization rate with efficient external surface utilization, this study lays the foundation for the design of universally applicable and efficient enzyme immobilization catalysts. High enzyme-loading of HHSS-LE refers to laccase immobilized on amino-functionalized modified silica particles with hierarchical hollow silica microsphere structures, this configuration facilitates synergistic adsorption and biodegradation of BPA. [Display omitted] •Maximizing the utilization of the outer surface of the carrier to achieve efficient enzyme catalysis.•Laccase was efficiently immobilized onto HHSS with a loading capacity of 213.102 mg/g.•The laccase immobilization procedure was optimized using BBD-RSM model.•The stability of the immobilized laccase was significantly enhanced.•The HHSS-LE achieved adsorption-biodegradation synergistic degradation of BPA.
ISSN:0141-8130
1879-0003
1879-0003
DOI:10.1016/j.ijbiomac.2024.134586