title: Rational surface silane modification for immobilizing glucose oxidase.
abstract: Glucose oxidase (GOx) has many significant applications in biosensor and biocatalysis. In this study, we firstly quantitatively analyzed the binding efficiency of (3-aminopropyl) trimethoxysilane (APTES) modified onto the surface of GOx. It was found that the contents of the grafted silane did not significantly influence the relative activities and tertiary structures of all surface modified GOxs. Immobilization ratio and relative activity of all instances of APTES modified GOx increased, compared with those of native enzyme. However, good stability of immobilized GOx at extreme pH and high temperature could only be obtained when modified protein with low binding silane content. At pH 2.0, the immobilized GOx with low binding content showed a more than 600% activity, compared to the free enzyme. Therefore, rational surface modification would be beneficial to improving the activity and stability of immobilized enzyme as well as increasing loading amount.
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Feibao
authors.initials: F
authors.lastname: Tian
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Yi
authors.initials: Y
authors.lastname: Guo
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Feifei
authors.initials: F
authors.lastname: Lin
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Yumei
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Qipeng
authors.initials: Q
authors.lastname: Yuan
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, PR China. Electronic address: lianghao@mail.buct.edu.cn.
authors.forename: Hao
authors.initials: H
authors.lastname: Liang
mesh_terms: D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism*; D005949:Glucose Oxidase / Q000737:chemistry* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011487:Protein Conformation; D012821:Silanes / Q000737:chemistry*; D013499:Surface Properties; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D012821:Silanes; D005949:Glucose Oxidase
keywords: Glucose oxidase; Immobilization; Silane surface modification; Silica nanoparticles