Surfactant-activated magnetic cross-linked enzyme aggregates (magnetic CLEAs) of Thermomyces lanuginosus lipase for biodiesel production

被引：48

作者：

Zhang, Wei-Wei ^{[1
]}

Yang, Xian-Ling ^{[1
]}

Jia, Jun-Qi ^{[1
]}

Wang, Na ^{[1
]}

Hu, Cheng-Li ^{[1
]}

Yu, Xiao-Qi ^{[1
]}

机构：

[1] Sichuan Univ, Coll Chem, Key Lab Green Chem & Technol, Minist Educ, Chengdu 610064, Peoples R China

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2015年 / 115卷

基金：

中国国家自然科学基金;

关键词：

Lipase; Magnetic cross-linked enzyme aggregates; Amino-functionalized magnetite; nanoparticles; Surfactant activation; Biodiesel production; CANDIDA SP 99-125; RHIZOPUS-ORYZAE; IMMOBILIZATION; PROTEIN; FEEDER; WATER; FUEL;

D O I：

10.1016/j.molcatb.2015.02.003

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：

Novel surfactant-activated magnetic cross-linked enzyme aggregates of Thermomyces lanuginosus lipase (TLL-magnetic-CLEAs) were developed and provided an efficient approach to improve the activity and stability of lipase for biodiesel production. In the methanolysis of Jatropha oil for biodiesel synthesis, the maximum yield in isopropyl ether was 88% after 48 h at 40 degrees C, representing 3.5-fold and 2.5-fold higher activity than that exhibited by free TLL and TLL CLEAs, respectively. Moreover, Tween 80-activated TLL-magnetic-CLEAs retained their activity during storage at 4 degrees C for 11 weeks and 10 cycles of repeated 48 h biodiesel reactions at 40 degrees C (over 30 days). Additionally, the surface morphology, particle size and loading of lipase aggregates were confirmed by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM). The combination of interfacial activation, high specific enzyme activity, improved stability and easy recovery of magnetic CLEAs presents an attractive process for lipase immobilization and provides a promising catalyst for biodiesel production. (C) 2015 Elsevier B.V. All rights reserved.

引用

页码：83 / 89

页数：7

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