Immobilization of Glucose Oxidase and 2-Hydroxybiphenyl 3-Monooxygenase in Mesoporous Silica: Characterization Studies and Construction of an Amperometric Glucose Biosensor

Author: Stefanakis Dimitrios   Margellou Asimina   Psarouli Aimilia   Chaniotakis Nikolaos   Ghanotakis Demetrios  

Publisher: Taylor & Francis Ltd

ISSN: 0003-2719

Source: Analytical Letters, Vol.43, Iss.16, 2010-01, pp. : 2582-2597

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Abstract

Immobilization techniques that preserve the activity of biomolecules have many potential applications. Mesoporous silica has been used to encapsulate a wide variety of biomolecules. In this particular work, MCM-41 silica has been used as a matrix for the immobilization of two important enzymes, HpbA and GOx. The enzyme 2-hydroxybiphenyl 3-monooxygenase (HpbA) is involved in the microbial degradation of 2-hydroxy and 2,2'-dihydroxybiphenyl, which occurs during the desulfurization of coal and petroleum, while Glucose oxidase (GOx) catalyzes the oxidation of β-D-glucose to δ-gluconolactone. The silica-enzyme hybrids were extensively characterized and the one with GOx was used for the construction of a biosensor.

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