Enhancement of stability of immobilized glucose oxidase by modification of free thiols generated by reducing disulfide bonds and using additives.

Gulla, K. C. and Gouda, M. D. and Thakur, M. S. and Karanth, N. G. (2004) Enhancement of stability of immobilized glucose oxidase by modification of free thiols generated by reducing disulfide bonds and using additives. Biosensors & bioelectronics, 19 (6). pp. 621-5. ISSN 0956-5663

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Abstract

Stability of glucose oxidase (GOD) immobilized with lysozyme has been considerably enhanced by modification of free thiols generated by reducing disulfide bonds using beta-mercaptoethanol and N-ethylmaleimide in conjunction with additives like antibiotics and salts. Thermal stability of immobilized GOD was quantified by means of the transition temperature, Tm and the operational stability by half-life t1/2 at 70 degrees C. Modification of the free thiols in the enzyme coupled with the presence of kanamycin, NaCl, and K2SO4, led to increase in Tm, to 80, 82 and 84 degrees C (compared to 75 degrees C in control) and t1/2 by 7.7-, 11- and 22-fold, respectively, indicating that this method can be effectively used for enhancing the stability of enzymes.

Item Type:	Article
Uncontrolled Keywords:	Glucose oxidase; Biosensor; Thermal stability; Additives; Thiol group modification
Subjects:	600 Technology > 08 Food technology > 31 Food Additives 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions:	Fermentation Technology and Bioengineering
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	19 Aug 2008 10:14
Last Modified:	09 Apr 2018 11:07
URI:	http://ir.cftri.res.in/id/eprint/2048

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