TY - JOUR
T1 - Covalent immobilization of Burkholderia cepacia lipase on amine functionalized ionic liquid modified SBA-15
AU - Hu, Yi
AU - Yang, Jiao
AU - Tang, Su Su
AU - Chu, Xu Ming
AU - Zou, Bin
AU - Huang, He
PY - 2013/5
Y1 - 2013/5
N2 - The (3-aminopropyl)trimethoxysilane and amine functionalized ionic liquid modified mesoporous silica SBA-15 (NH2-SBA, NH2-IL-SBA) were synthesized, and NH2-IL-SBA was activated by glutaraldehyde (CA-NH2-IL-SBA). Physical and chemical properties of the materials were characterized by elemental analysis, nitrogen adsorption-desorption, small-angle X-ray diffraction and Fourier transform infrared spectroscopy. The prepared materials were used as novel carrier systems to immobilize Burkholderia cepacia lipase (BCL) by physical adsorption, conventional covalent attachment and enzyme-aggregate coating methods. Enzymatic properties, including activity, optimum reaction condition and stability were investigated in the triacetin hydrolysis reaction. The results showed that the modification and activation did not destroy the structure of SBA-15. Compared with the immobilized BCL on NH2-SBA and parent SBA-15 (BCL-NH2-SBA, BCL-SBA-15), the immobilized BCL on novel carriers were more resistant to temperature and low pH changes and possessed both higher activity and stability. Especially, the BCL prepared by enzyme-aggregate coating method exhibited highest immobilization efficiency and stability, which improved 4.0 and 2.0 folds of thermal stability and reusability than BCL-SBA-15, respectively.
AB - The (3-aminopropyl)trimethoxysilane and amine functionalized ionic liquid modified mesoporous silica SBA-15 (NH2-SBA, NH2-IL-SBA) were synthesized, and NH2-IL-SBA was activated by glutaraldehyde (CA-NH2-IL-SBA). Physical and chemical properties of the materials were characterized by elemental analysis, nitrogen adsorption-desorption, small-angle X-ray diffraction and Fourier transform infrared spectroscopy. The prepared materials were used as novel carrier systems to immobilize Burkholderia cepacia lipase (BCL) by physical adsorption, conventional covalent attachment and enzyme-aggregate coating methods. Enzymatic properties, including activity, optimum reaction condition and stability were investigated in the triacetin hydrolysis reaction. The results showed that the modification and activation did not destroy the structure of SBA-15. Compared with the immobilized BCL on NH2-SBA and parent SBA-15 (BCL-NH2-SBA, BCL-SBA-15), the immobilized BCL on novel carriers were more resistant to temperature and low pH changes and possessed both higher activity and stability. Especially, the BCL prepared by enzyme-aggregate coating method exhibited highest immobilization efficiency and stability, which improved 4.0 and 2.0 folds of thermal stability and reusability than BCL-SBA-15, respectively.
KW - Burkholderia cepacia lipase
KW - Immobilization
KW - Ionic liquid
KW - Mesoporous material
KW - Modification
UR - http://www.scopus.com/inward/record.url?scp=84878912908&partnerID=8YFLogxK
U2 - 10.7503/cjcu20120951
DO - 10.7503/cjcu20120951
M3 - 文章
AN - SCOPUS:84878912908
SN - 0251-0790
VL - 34
SP - 1195
EP - 1202
JO - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities
JF - Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universities
IS - 5
ER -