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Association of proteins in acidic solutions - a case study with beta-globulin.

Rajendran, S. and Prakash, V. (1992) Association of proteins in acidic solutions - a case study with beta-globulin. International Journal of Biological Macromolecules, 14 (6). 298-304, 32 ref..

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Abstract

The investigation of the effect of acid pH on the structure of fi-globulin indicated several transitions as a function of pH. Upon reducing the pH from 7.0, the fl-globulin molecule underwent an expansion due to hydration up to pH 5.0, and a further increase in H + concentration resulted in unfolding. This' is a single step cooperative denaturation as indicated by the viscosity profile. At extreme acid pH values (below pH 2.0) the protein associates or folds to a different conformational motif as shown by blue shift of ultraviolet fluorescence emission maximum and decrease in reduced viscosity values by more than 30% due to an entropically driven hydrophobic interaction. The conformational analysis of fl-globulin showed a decrease up to pH 3.0, followed by an increase in the ordered structure at low pH values indicatin 9 that the low pH values stabilized this new conformation. These results are discussed in view of the molten globule structure of proteins.

Item Type: Article
Uncontrolled Keywords: Sesame seed protein ; fl-globulin ; acid pH ; denaturation ; swelling and hydration ; folding; molten globule state
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 19 Mar 2018 05:34
Last Modified: 19 Mar 2018 05:34
URI: http://ir.cftri.com/id/eprint/2661

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