Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

被引:90
|
作者
Cao, Shi-Lin [1 ,2 ]
Huang, Yu-Mei [1 ]
Li, Xue-Hui [2 ]
Xu, Pei [1 ,3 ]
Wu, Hong [3 ]
Li, Ning [1 ]
Lou, Wen-Yong [1 ,3 ]
Zong, Min-Hua [2 ,3 ]
机构
[1] S China Univ Technol, State Key Lab Pulp & Paper Engn, Guangzhou 510640, Guangdong, Peoples R China
[2] S China Univ Technol, Sch Chem & Chem Engn, Guangzhou 510640, Guangdong, Peoples R China
[3] S China Univ Technol, Sch Food Sci & Engn, Lab Appl Biocatalysis, Guangzhou 510640, Guangdong, Peoples R China
来源
SCIENTIFIC REPORTS | 2016年 / 6卷
基金
中国国家自然科学基金;
关键词
IONIC LIQUIDS; PAPAIN; OPTIMIZATION; BIOCATALYST; HYDROLYSIS; RESOLUTION; STABILITY; CHITOSAN;
D O I
10.1038/srep20420
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading (82.2 mg enzyme/g) and activity recovery (95.9%). Compared with free PCL, PCL@MCNC exhibited significantly enhanced stability and solvent tolerance, due to the increase of enzyme structure rigidity. The observable optimum pH and temperature for PCL@MCNC were higher than those of free PCL. PCL@MCNC manifested relatively higher enzyme-substrate affinity and catalytic efficiency. Moreover, PCL@MCNC was capable of effectively catalyzing asymmetric hydrolysis of ketoprofenethyl ester with high yield of 43.4% and product e.e. of 83.5%. Besides, immobilization allowed PCL@MCNC reuse for at least 6 consecutive cycles retaining over 66% of its initial activity. PCL@MCNC was readily recycled by magnetic forces. Remarkably, the as-prepared nanobiocatalyst PCL@MCNC is promising for biocatalysis.
引用
收藏
页数:12
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