CHARACTERISTICS OF THE GLUCOSE-OXIDASE AT DIFFERENT SURFACES

Authors
Citation
Xd. Dong et al., CHARACTERISTICS OF THE GLUCOSE-OXIDASE AT DIFFERENT SURFACES, Bioelectrochemistry and bioenergetics, 42(1), 1997, pp. 63-69
Citations number
31
Categorie Soggetti
Biology
ISSN journal
03024598
Volume
42
Issue
1
Year of publication
1997
Pages
63 - 69
Database
ISI
SICI code
0302-4598(1997)42:1<63:COTGAD>2.0.ZU;2-C
Abstract
By adsorption or chemical bonding, glucose oxidase (GOD) molecules are immobilized to different surfaces, including bare Pt and Au, alkaneth iols self-assembled monolayers, and omega-carboxylic acid thiols self- assembled monolayers. Except Au and reduced Pt surfaces, GOD can be im mobilized on all the surfaces tested. The most durable immobilization is achieved by covalent bonding GOD to carboxylic terminated SAM. In m ost cases the immobilized GOD retains its native enzymatic activity. A chain length dependence of the apparent Michealis constant is found f or the GOD adsorbed at carboxylic group terminated SAM and the possibl e reasons are discussed. (C) 1997 Elsevier Science S.A.