Immobilization of Candida rugosa lipase on electrospun cellulose nanofiber membrane

被引:135
作者
Huang, Xiao-Jun [1 ]
Chen, Peng-Cheng [1 ]
Huang, Fu [1 ]
Ou, Yang [1 ]
Chen, Ming-Rui [1 ]
Xu, Zhi-Kang [1 ]
机构
[1] Zhejiang Univ, MOE Key Lab Macromol Synth & Functionalizat, Dept Polymer Sci & Engn, Hangzhou 310027, Peoples R China
基金
中国国家自然科学基金;
关键词
Cellulose; Nanofiber membrane; Enzyme immobilization; Lipase; Response surface methodology; COVALENT IMMOBILIZATION; OPTIMIZATION; CHITOSAN; ACID); ULTRAFILTRATION; HYDROLYSIS; OXIDASE; OIL;
D O I
10.1016/j.molcatb.2011.02.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A biocatalyst with high activity retention of lipase was fabricated by the covalent immobilization of Candida rugosa lipase on a cellulose nanofiber membrane. This nanofiber membrane was composed of nonwoven fibers with 200 nm nominal fiber diameter. It was prepared by electrospinning of cellulose acetate (CA) and then modified with alkaline hydrolysis to convert the nanofiber surface into regenerated cellulose (RC). The nanofiber membrane was further oxidized by NaIO4. Aldehyde groups were simultaneously generated on the nanofiber surface for coupling with lipase. Response surface methodology (RSM) was applied to model and optimize the modification conditions, namely NaIO4 content (2-10 mg/mL), reaction time (2-10 h), reaction temperature (25-35 degrees C) and reaction pH (5.5-6.5). Well-correlating models were established for the residual activity of the immobilized enzyme (R-2 = 0.9228 and 0.8950). We found an enzymatic activity of 29.6 U/g of the biocatalyst was obtained with optimum operational conditions. The immobilized lipase exhibited significantly higher thermal stability and durability than equivalent free enzyme. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:95 / 100
页数:6
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