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Denaturation of glycinin by urea and guanidine hydrochloride.

Suresh Chandra, B. R. and Appu Rao, A. G. and Narasinga Rao, M. S. (1986) Denaturation of glycinin by urea and guanidine hydrochloride. International Journal of Peptide and Protein Research, 27. pp. 493-500.

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Denaturation of glycinin by urea and guanidine hydrochloride (GdnHC1) has been studied at 30' by viscosity and circular dichroism (CD) measurements. The kinetics of denaturation by 8M urea at 20, 30, 40 and SOo, and by 6M GdnHCl at 20' have been measured by monitoring the increase in absorbance at 287nm as a function of time. Viscosity increased with denaturant concentration and reached maximum value of - 28 mL/g at 6M GdnHCl and 7M urea, The (negative) molar ellipticity values in the region 250-200 nm decreased with increase in denaturant concentration. Analysis of viscosity and CD data indicated that both sets of data fitted the same curve of fd (fraction of protein denatured) versus denaturant concentration. The kinetic data followed first order reaction kinetics. These suggest that denaturation of glycinin by urea/ GdnHCl is a two-state process and follows the same pattern as that of globular proteins.

Item Type: Article
Uncontrolled Keywords: denaturation; equilibrium study; glycinin; guanidine hydrochloride; kinetic study; urea
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Mar 2018 06:10
Last Modified: 14 Mar 2018 06:10
URI: http://ir.cftri.res.in/id/eprint/3693

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