Modification of Silica Xerogels with Polydopamine for Lipase B from Candida antarctica Immobilization

• Published in: Catalysts
• Main Authors: Honghai Wang, Wenda Yue, Shuling Zhang, Yu Zhang, Chunli Li, Weiyi Su
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2021
• Subjects: Candida antarctica lipase B; silica xerogel; enzyme immobilization; polydopamine; modification; Chemical technology; TP1-1185; Chemistry; QD1-999; Antarc*; Antarctica
• Online Access: https://doi.org/10.3390/catal11121463; https://doaj.org/article/9c2e69c3803240bab1aff6a824bb68b2

Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effective strategy for stabilizing enzymes embedded inside silica xerogels by a polydopamine (PDA) coating through in-situ polymerization. The modified silica xerogels were characterized by scanning and transmission electron microscopy, Fourier tranform infrared spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy and pore structure analyses. When the PDA-modified silica xerogels were used to immobilize enzymes of Candida antarctica lipase B (CALB), they exhibited a high loading ability of 45.6 mg/g support , which was higher than that of immobilized CALB in silica xerogels (28.5 mg/g support ). The immobilized CALB of the PDA-modified silica xerogels retained 71.4% of their initial activities after 90 days of storage, whereas the free CALB retained only 30.2%. Moreover, compared with the immobilization of enzymes in silica xerogels, the mechanical properties, thermal stability and reusability of enzymes immobilized in PDA-modified silica xerogels were also improved significantly. These advantages indicate that the new hybrid material can be used as a low-cost and effective immobilized-enzyme support.