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Immobilization of Glucose Oxidase on Ordered Macroporous Silicas Functionalized with Amino Group
Author(s) -
Wu Quanzhou,
He Jianfeng,
Zhang Jingjia,
Ou Jiming
Publication year - 2012
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201180482
Subject(s) - glucose oxidase , chemistry , immobilized enzyme , fourier transform infrared spectroscopy , colloidal crystal , covalent bond , chemical engineering , thermal stability , hybrid material , oxidase test , enzyme , polymer chemistry , nuclear chemistry , colloid , organic chemistry , engineering
A novel glucose oxidase immobilized on three‐dimensionally ordered macroporous (3DOM) material has been prepared by firstly preparation of hybrid 3DOM SiO 2 ‐NH 2 materials using colloidal crystal method, and following covalent immobilization of glucose oxidase on the pore walls of the 3DOM materials. The materials were characterized by SEM, FTIR, DSC and BET techniques. SEM observation shows that the macropores are highly ordered and are interconnected by small windows. FTIR measurement shows that there are amino and organic groups in the pore walls. The surface area of the 3DOM SiO 2 ‐NH 2 material is about 10.2 m 2 /g. The loaded amount of enzyme is increased with amino content in the materials. The immobilized enzyme has high activity, thermal stability and can be reused.