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Boosting catalytic efficiency of lipase by regulating amphiphilic microenvironment through reversible addition-fragmentation chain transfer polymerized modifications on polyacrylonitrile fiber  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Boosting catalytic efficiency of lipase by regulating amphiphilic microenvironment through reversible addition-fragmentation chain transfer polymerized modifications on polyacrylonitrile fiber

作者:Ying, Anguo[1,2];Bai, Linsheng[1];Jiang, Xubao[1];Shen, Runpu[2];Liu, Yujing[1];Liu, Zhongqiu[1]

机构:[1]Qufu Normal Univ, Dept Chem & Chem Engn, Qufu 273100, Shandong, Peoples R China;[2]Shaoxing Univ, Zhejiang Engn Res Ctr Fat Soluble Vitamin, Shaoxing 312000, Zhejiang, Peoples R China

年份:2024

卷号:277

外文期刊名:INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录:SCI-EXPANDED(收录号:WOS:001284366700001)、、EI(收录号:20243116772305)、Scopus(收录号:2-s2.0-85199535909)、WOS

基金:This work was financially supported by the National Natural Science Foundation of China (Grant 22278243, 21978154, 22108156, 42306235) and the Youth Innovation Team Project of Shandong Pro-vincial College (No. 2022KJ180) .

语种:英文

外文关键词:Polyacrylonitrile fiber; Hydrophobic modification; Lipase immobilization; Transesterification; Biodiesel

外文摘要:Lipases are increasingly attracting attention in green and sustainable biodiesel production. Currently, the research emphasis lies in immobilizing unstable lipase onto carriers to enhance its performance. Polyacrylonitrile fiber (PANF) is considered to be a promising material for lipase immobilization due to its excellent properties. In this study, functional carriers with regulated surface hydrophobicity were obtained by loading functional groups on PANF via reversible addition-fragmentation chain transfer (RAFT) polymerized modification, and Candida rugosa lipase (CRL) was covalently immobilized on the carrier with glutaraldehyde as a linker. By employing this optimized biocatalyst PANF@BMA&2VImBr-NH2-CRL &2VImBr-NH 2-CRL in the transesterification process, the yield of biodiesel derived from soybean oil reached an impressive 92.7 %. The outstanding performance can be attributed to the activation of lipase interface induced by hydrophobic microenvironment derived from alkyl ester on the carrier skeleton. Moreover, the stability and storage performance of immobilized lipase were significantly improved. The immobilized lipase exhibited facile recovery and maintained a consistent biodiesel yield of 80.9% even after undergoing 5 cycles of reuse, thereby highlighting its potential for sustainable production. To sum up, our research demonstrates that the designed and prepared process of PANF-supported lipase offers a promising approach for enzyme immobilization, thereby presenting extensive potential applications in the field of biotechnology.

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