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Extraction and separation of guar seed proteins.

Nath, J. P. and Subramanian, N. and Narasinga Rao, M. S. (1978) Extraction and separation of guar seed proteins. Journal of Agricultural and Food Chemistry, 26 (5). 1243-1246, 18 ref..

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Abstract

The solubility of guar meal protein was determined in various aqueous solvents using different acids and bases. The total proteins were characterized by the techniques of gel filtration, polyacrylamide gel electrophoresis, and ultracentrifugation. They were found to consist of 3 fractions, 2 of high mol. wt. and 1 of low mol. wt. Neither the total proteins nor the fractions showed any haemagglutinin activity. Max. trypsin inhibitor and proteolytic activity was observed with the lowest mol. wt. fraction.

Item Type: Article
Uncontrolled Keywords: MEAL-; guar meal proteins, characterization of; SEEDS-; PROTEINS-VEGETABLE; TRYPSIN-; guar meal proteins, trypsin inhibitor activity in; INHIBITION-; PROTEOLYSIS-; guar meal proteins, proteolytic activity in
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 28 Dec 2016 10:09
Last Modified: 28 Dec 2016 10:09
URI: http://ir.cftri.com/id/eprint/6997

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