Physico-chemical properties of low molecular weight gliadin and its structural similarity with other wheat proteins.

Prasada Rao, U. J. S. and Prasad, K. V. S. and Nigam, S. N. (2002) Physico-chemical properties of low molecular weight gliadin and its structural similarity with other wheat proteins. Journal of Food Science and Technology, 39 (6). pp. 623-628.

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Abstract

From a mixture of gliadins, extracted from wheat gluten using 70% ethanol, a low mol. wt. gliadin was purified to apparent homogeneity using gel filtration followed by electroelution methods. The viscoelastic property of this protein was less than other gliadins and the mol. wt. was estimated to be 14 000. This low mol. wt. protein which was rich in cysteine and basic amino acids, differed considerably in amino acid composition from other gliadins and other reported low mol. wt. wheat proteins. Immunoblot studies showed that this protein shared common epitopes with 30 000 and 45 000 mol. wt. proteins which were present in albumins, globulins and gliadin fractions. Limited proteolytic studies suggested the existence of common domains among 14 000, 30 000 and 45 000 mol. wt. proteins of wheat flour. Results indicate that classification of wheat proteins based on solubility behaviour may be misleading.

Item Type:	Article
Uncontrolled Keywords:	GLIADINS-; GLUTEN-; PHYSICAL-PROPERTIES; WHEAT-; MOL.-WT.; WHEAT-GLUTEN
Subjects:	600 Technology > 08 Food technology > 14 Physical properties 600 Technology > 08 Food technology > 21 Cereals > 04 Wheat
Divisions:	Dept. of Biochemistry
Depositing User:	Somashekar K.S
Date Deposited:	16 Jun 2011 11:05
Last Modified:	16 Jun 2011 11:05
URI:	http://ir.cftri.res.in/id/eprint/7585

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