Influence of Polyols on the Stability and Kinetic Parameters of Invertase from Candida utilis: Correlation with the Conformational Stability and Activity

Mr., Gangadhara and Ramesh Kumar, P. and Prakash, V. (2008) Influence of Polyols on the Stability and Kinetic Parameters of Invertase from Candida utilis: Correlation with the Conformational Stability and Activity. Protein Journal, 27. pp. 440-449.

PDF Protein_Journal_27(7-8)_2008_440-.pdf Restricted to Registered users only Download (504kB)

Abstract

Invertase (b-D-fructofuranoside fructohydrolase- E.C. 3.2.1.26) is a sucrose hydrolyzing enzyme found in microbial, plant and animal sources. Invertase from Candida utilis is a dimeric glycoprotein composed of two identical monomer subunits with an apparent molecular mass of 150 kDa. We investigated the mechanism of stabilization of invertase with polyols (glycerol, xylitol, and sorbitol). Activity, thermodynamic and kinetic measurements of invertase were performed as a function of polyol concentration and showed that polyols act as very effective stabilizing agents. The result from the solvent-invertase interaction shows preferential exclusion of the polyols from the protein domain leading to preferential hydration of protein. Apparent thermal denaturation temperature of the protein (Tm) rose from 75 �C to a maximum of 85 �C in 30% glycerol. The stabilization has been attributed to the preferential hydration of the enzyme.

Item Type:	Article
Uncontrolled Keywords:	Invertase � Polyols � Thermal stability � pH stability � Partial specific volume � Preferential hydration
Subjects:	600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes 500 Natural Sciences and Mathematics > 10 Plants
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	16 Jun 2009 10:08
Last Modified:	16 May 2012 07:26
URI:	http://ir.cftri.res.in/id/eprint/9093

Actions (login required)

View Item