Structural stability of beta-globulin, the low molecular weight protein fraction from sesame seed (Sesamum indicum L.) in alkaline solution.

Rajendran, S. and Prakash, V. (1993) Structural stability of beta-globulin, the low molecular weight protein fraction from sesame seed (Sesamum indicum L.) in alkaline solution. Indian Journal of Biochemistry & Biophysics, 30 (1). pp. 15-20. ISSN 0301-1208

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Abstract

Beta-globulin, a single polypeptide chain of molecular weight 15,000 +/- 1,000, undergoes denaturation in alkaline pH (7.0-13.0), thereby affecting the hydrodynamic properties of the protein, viz. a decrease in sedimentation coefficient from a value of 2.0s to 1.4s at pH 11.3, an increase in reduced viscosity from 0.042 dl/g to 0.158 dl/g at pH 12.6 and a decrease in partial specific volume resulting in a volume change of 6.3 +/- 1.0 ml/mole residue at pH 11.7. The perturbation of tryptophanyl residues and ionization of tyrosyl residues are preceded by alteration in conformational status of the protein. The fluorescence emission measurements indicate initial unfolding of the protein molecule which exposes the tryptophan and tyrosyl residues to the solvent. The tyrosyl phenolic group ionization is anomalous having a pKint value of 11.2. The reduced viscosity value reaches a plateau region at pH 12.5.

Item Type:	Article
Uncontrolled Keywords:	sesame seed, beta-globulin, proteins
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:	15 Nov 2021 04:30
Last Modified:	15 Nov 2021 04:30
URI:	http://ir.cftri.res.in/id/eprint/2293

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