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Characterisation and functional properties of proteins of some Indian chickpea ( Cicer arietinum ) cultivars
Author(s) -
Deep Singh Gagan,
Wani Ali Abas,
Kaur Devinder,
Sogi Dalbir Singh
Publication year - 2008
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.3144
Subject(s) - glutelin , prolamin , isoelectric point , fractionation , emulsion , globulin , chemistry , albumin , food science , sugar , isoelectric focusing , molecular mass , chromatography , storage protein , biochemistry , biology , immunology , gene , enzyme
BACKGROUND: Chickpea ( Cicer arietinum L.) proteins have received attention during recent years owing to their higher biological values and better functional ingredients than oilseed proteins. In this study the composition, fractionation, electrophoretic behaviour and functional properties of five chickpea protein concentrates were determined. RESULTS: The chickpea proteins contained 15.9–54.8 g kg −1 albumin, 48.9–154.1 g kg −1 globulin, 39.2–76.5 g kg −1 glutelin and traces of prolamin. Electrophoresis of the various fractions revealed that albumin and globulin were made up of sub‐units of different molecular weights ranging from 7 to 96 kDa. Water and oil absorption of the protein concentrates varied from 1.15 to 2.75 g g −1 and from 2.60 to 5.65 g g −1 respectively. Foaming capacity and foam stability of the protein concentrates were good and improved with the addition of salt (10 g L −1 NaCl) or sugar (100 g L −1 sucrose) at both isoelectric and neutral pH. Emulsifying capacity and emulsion stability of the protein concentrates were good and excellent respectively. CONCLUSION: Protein concentrates prepared from chickpeas have potential use in food formulations owing to their good emulsifying/foaming and water/oil‐binding capacities. Copyright © 2008 Society of Chemical Industry