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Effect of acidic pH on the protein carmin from safflower seed (Carthamus tinctorius).

Rao, K. S. and Prakash, V. (1989) Effect of acidic pH on the protein carmin from safflower seed (Carthamus tinctorius). Journal of Protein Chemistry, 8 (4). pp. 529-48. ISSN 0277-8033

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The effect of a decrease in pH on the structural integrity of carmin has been monitored by a variety of biophysical techniques. The protein undergoes initial dissociation up to pH 3.5-4.0 without any significant denaturation. Below this pH the process of dissociation and denaturation appears to be simultaneous. Further, in the pH range of 2.5-1.6 the protein reassociates to probably a different polymer resulting from possibly, an entropically driven hydrophobic interaction. The process of dissociation appears to be reversible to a large extent. The process of denaturation appears to be governed by the kinetic path that the denatured protein molecule follows either by a sudden decrease in pH or through a gradual decrease in pH. These results are interpreted while keeping in view the oligomeric and globular structure of carmin at neutral pH. The results would help in understanding of structure-function relationship of the protein and its role in hydrogen ion binding in vivo.

Item Type: Article
Uncontrolled Keywords: carmin; association-dissociation; denaturation; reaggregation; kinetics; reversibility; hydrophobic interaction
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 20 Mar 2018 08:41
Last Modified: 20 Mar 2018 08:41
URI: http://ir.cftri.com/id/eprint/2356

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