Aminated lignin mesoporous carbon as advanced support for high-performance lipase immobilization
In this study, alkali lignin (AL), a low-cost and renewable biopolymer, was innovatively selected as the precursor. Modified lignin, namely aminated lignin (AAL), sulfomethylated lignin (SML) and phosphorylated lignin (PAL), were synthesized and combined with nano-MgO to serve as a template. Subsequent carbonization of these mixtures produced mesoporous carbon (MC) carriers denoted as AL-MC, AAL-MC, SML-MC and PAL-MC. Rhizomucor miehei lipase (RML) immobilization onto these carriers was effectively achieved through physical adsorption under mild conditions. Through optimization of the preparation parameters, high-performance immobilized enzymes (IM-AL-MC, IM-AAL-MC, IM-SML-MC, IM-PAL-MC) were developed. Notably, IM-AAL-MC exhibited superior enzyme activity (0.037 U/mg immobilized lipase), loading capacity (0.145 mg protein/mg immobilized lipase) and immobilization efficiency (84.5 %). The catalytic efficiency and stability of IM-AAL-MC were comprehensively examined. Characterization of the carriers and immobilized enzymes was conducted using Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), Brunauer-Emmett-Teller surface area analysis (BET) and transmission electron microscopy (TEM). Results indicated that IM-AAL-MC displayed significantly improved stability compared to free lipase. Remarkably, IM-AAL-MC retained 99.49 % activity in n-hexane, far exceeding the free lipase (43.53 %). Additionally, IM-AAL-MC preserved 86.2 % of its relative activity after six consecutive reuse cycles.
Authors
- Yani Zhao (ORCID: https://orcid.org/0000-0002-3589-9883)
- Luyi Chen (ORCID: https://orcid.org/0000-0002-8801-9907)
- Jiaojiao Xia (ORCID: https://orcid.org/0000-0001-8007-9748)
- Bin Zou (ORCID: https://orcid.org/0000-0003-3816-8776)
- Xue Zhang (ORCID: https://orcid.org/0000-0002-2204-2346)
- Qi Lu (ORCID: https://orcid.org/0000-0001-7603-4360)
- Xing Ni
Institutions
- Jiangsu University (CN)
Publication Details
- Journal
- Colloids and Surfaces B Biointerfaces
- Published
- 2025-08-28
- DOI
- https://doi.org/10.1016/j.colsurfb.2025.115079
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Jiangsu University
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- National Key Research and Development Program of China