Improved catalytic properties of Candida antarctica lipase B immobilized on cetyl chloroformate-modified cellulose nanocrystals
文献类型： 外文期刊
作者： Shi, Xue 1 ; Qin, Xiaoli 1 ; Dai, Yunxiang 1 ; Liu, Xiong 1 ; Wang, Weifei 3 ; Zhong, Jinfeng 1 ;
作者机构： 1.Southwest Univ, Coll Food Sci, Chongqing 400715, Peoples R China
2.Chongqing Key Lab Special Food Cobuilt Sichuan & C, Chongqing 400715, Peoples R China
3.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Guangzhou 510610, Peoples R China
关键词： Lipase; Immobilization; Cellulose nanocrystals; Hydrophobic modification; Interaction; Catalytic activity
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.025； 五年影响因子：7.626 ）
ISSN： 0141-8130
年卷期： 2022 年 220 卷
页码：
收录情况： SCI
摘要： The catalytic activity of Candida antarctica lipase B (CALB) immobilized on modified cellulose nanocrystals (CNC) with different hydrophobicity was investigated using experimental and theoretical approaches. Firstly, the modified CNC were characterized by multi-spectroscopic methods, water contact angle, scanning electron mi-croscopy and thermogravimetric analysis. Moderately hydrophobic CNC were found to be an optimal support for CALB immobilization. Secondly, model systems contained a CALB molecule and different numbers of modified CNC molecules (CALB@3CNC-C16, CALB@10CNC-C16 and CALB@15CNC-C16) were prepared for molecular dynamics (MD) simulation. Root-mean-square fluctuation values (0.61-2.61 angstrom) of lid region were relatively high in CALB@10CNC-C16, indicating that modified CNC with moderate hydrophobicity favored forming a lid-open conformation of CALB. Finally, the esterification of oleic acid catalyzed by the immobilized CALB showed higher conversion (54.68 %) than free CALB (12.98 %). Insights into modified CNC with tunable properties provided by this study may be a potential support for improving the catalytic performance of lipases.
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