TY - JOUR
T1 - Immobilization of Candida antarctic Lipase B on Functionalized Ionic Liquid Modified MWNTs
AU - Wan, Xiaomei
AU - Tang, Susu
AU - Xiang, Xinran
AU - Huang, He
AU - Hu, Yi
N1 - Publisher Copyright:
© 2017, Springer Science+Business Media New York.
PY - 2017/11/1
Y1 - 2017/11/1
N2 - Multiwalled carbon nanotubes (MWNTs) were modified by imidazole-based ionic liquids with different alkyl groups. The modified support samples were characterized by scanning transmission electron microscopy, Raman spectra, thermogravimetric analyses, and X-ray photoelectron spectroscopy. The samples were used to immobilize Candida antarctic lipase (CALB) and the influence of alkyl chain length of ionic liquids on enzymatic properties was investigated by the hydrolysis reaction of triacetin. The results revealed that functionalized ionic liquids modification did not destroy the structure of MWNTs. Compared with the immobilized CALB on MWNTs, the immobilized CALB on novel carriers all exhibited higher activity, thermal stability, and reusability. Especially, the activity of MWNTs-IL (8C)-CALB improved 15.23-folds than MWNTs-CALB, meanwhile, after incubation at 70 °C for 20 min, residual enzyme activity of MWNTs-IL (8C)-CALB was 46% of the initial activity, while MWNTs-CALB already lost all activity. Besides, MWNTs-IL (8C)-CALB retained 64.5% of its initial activity after 4 cycles, while MWNTs-CALB retained only 2.12%.
AB - Multiwalled carbon nanotubes (MWNTs) were modified by imidazole-based ionic liquids with different alkyl groups. The modified support samples were characterized by scanning transmission electron microscopy, Raman spectra, thermogravimetric analyses, and X-ray photoelectron spectroscopy. The samples were used to immobilize Candida antarctic lipase (CALB) and the influence of alkyl chain length of ionic liquids on enzymatic properties was investigated by the hydrolysis reaction of triacetin. The results revealed that functionalized ionic liquids modification did not destroy the structure of MWNTs. Compared with the immobilized CALB on MWNTs, the immobilized CALB on novel carriers all exhibited higher activity, thermal stability, and reusability. Especially, the activity of MWNTs-IL (8C)-CALB improved 15.23-folds than MWNTs-CALB, meanwhile, after incubation at 70 °C for 20 min, residual enzyme activity of MWNTs-IL (8C)-CALB was 46% of the initial activity, while MWNTs-CALB already lost all activity. Besides, MWNTs-IL (8C)-CALB retained 64.5% of its initial activity after 4 cycles, while MWNTs-CALB retained only 2.12%.
KW - Candida antarctic lipase B
KW - Carbon nanotubes
KW - Enzyme immobilization
KW - Ionic liquids
KW - Modification
UR - http://www.scopus.com/inward/record.url?scp=85016115849&partnerID=8YFLogxK
U2 - 10.1007/s12010-017-2465-9
DO - 10.1007/s12010-017-2465-9
M3 - 文章
C2 - 28353043
AN - SCOPUS:85016115849
SN - 0273-2289
VL - 183
SP - 807
EP - 819
JO - Applied Biochemistry and Biotechnology
JF - Applied Biochemistry and Biotechnology
IS - 3
ER -