[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Stabilization of immobilized glucose oxidase against thermal inactivation by silanization for biosensor applications.

Sarath Babu, V. R. and Kumar, M. A. and Karanth, N. G. and Thakur, M. S. (2004) Stabilization of immobilized glucose oxidase against thermal inactivation by silanization for biosensor applications. Biosensors and Bioelectronics, 19 (10). pp. 1337-41. ISSN 0956-5663

[img] PDF
Biosensors_and_Bioelectronics_19_(2004)_1337-1341.pdf
Restricted to Registered users only

Download (84kB)

Abstract

An important requirement of immobilized enzyme based biosensors is the thermal stability of the enzyme. Studies were carried out to increase thermal stability of glucose oxidase (GOD) for biosensor applications. Immobilization of the enzyme was carried out using glass beads as support and the effect of silane concentration (in the range 1-10%) during the silanization step on the thermal stability of GOD has been investigated. Upon incubation at 70 degrees C for 3h, the activity retention with 1% silane was only 23%, which increased with silane concentration to reach a maximum up to 250% of the initial activity with 4% silane. Above this concentration the activity decreased. The increased stability of the enzyme in the presence of high silane concentrations may be attributed to the increase in the surface hydrophobicity of the support. The decrease in the enzyme stability for silane concentrations above 4% was apparently due to the uneven deposition of the silane layer on the glass bead support. Further work on thermal stability above 70 degrees C was carried out by using 4% silane and it was found that the enzyme was stable up to 75 degrees C with an increased activity of 180% after 3-h incubation. Although silanization has been used for the modification of the supports for immobilization of enzymes, the use of higher concentrations to stabilize immobilized enzymes is being reported for the first time.

Item Type: Article
Uncontrolled Keywords: Glucose oxidase; Controlled pore glass; �-Aminopropyl triethoxysilane; Hydrophobic interactions; Thermal stability; Flow injection analysis; Thermal denaturation; Transition temperature; Half-life
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 02 Engineering & allied operations
Divisions: Central Instrumentation Facility Services
Fermentation Technology and Bioengineering
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 19 Aug 2008 10:32
Last Modified: 03 Jul 2015 08:07
URI: http://ir.cftri.res.in/id/eprint/2040

Actions (login required)

View Item View Item