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

Institutions

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

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Aminated lignin mesoporous carbon as advanced support for high-performance lipase immobilization

Yani Zhao, Luyi Chen, Jiaojiao Xia, Bin Zou et al.
Colloids and Surfaces B Biointerfaces
Enzyme Catalysis and Immobilization
article

Aminated lignin mesoporous carbon as advanced support for high-performance lipase immobilization

Yani Zhao, Luyi Chen, Jiaojiao Xia, Bin Zou, Xue Zhang, Qi Lu, Xing Ni
article en

Abstract

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.

Colloids and Surfaces B BiointerfacesVol. 256(Pt 2)
Jiangsu University (CN)
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
Openalex Percentile: Top 80%
Enzyme Catalysis and Immobilization
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.