Improving laccase activity and stability by HKUST-1 with cofactor via one-pot encapsulation and its application for...

Enhancing the catalytic activity and stability of enzymes is of great importance in the development of green chemical and cost-effective application, with removal of bisphenol A (BPA) as a prominent example. Engineering immobilization carriers and immobilization methods of enzymes endows great potential to achieve above goal. Until now, these reports have focused on employing the metal-organic frameworks (MOFs) to increase the stability and reusability of enzymes, an enhancement in its catalytic activity has yet to be addressed. This work introduced a biomimetic mineralization process for facile synthesis of laccase@HKUST-1 biocomposite under mild condition. By exploiting the activity of laccase@HKUST-1, we demonstrated, for the first time, that the integration of laccase and HKUST-1 containing cofactor Cu²⁺ ions leaded to 1.5-fold enhancement in the catalytic activity compared with free laccase, which was due to the synergistic enhancement of substrate oxidation. Indeed, the laccase@HKUST-1 biocomposite could function as active biocatalysts under biologically challenging conditions, such as acidic condition, high temperature, organic solvent, and continuous operation. The oxidation of phenols, such as BPA, with laccase@HKUST-1 reached higher catalytic performance than free laccase, and gave 100% degradation efficiency within 4 h. This study provides a feasible method to improve the activity and stability of laccase, which enable completely remove of BPA from the environment.