Isolation and Partial Characterization of Chikpea, Lupine and Lentill Seed Proteins

Alsohaimy, S. A.; Sitohy, M. Z.; El-Masry, R. A.
January 2007
World Journal of Agricultural Sciences;Jan2007, Vol. 3 Issue 1, p123
Academic Journal
Recently chickpea lupine and lentil seed proteins have been the focus of chemical and nutritional interest as a good substitute for soybean protein in the preparation of infant formulas and human foods. The purpose of the present investigation is to study the effect of different methods of protein isolation on the chemical and physical properties of the isolated proteins. Proteins were isolated in two steps: First protein was solubelized using alkaline conditions (pH 7-12) and with or without inorganic solutes (NaCl, Na2SO3 and MgCl2). Second protein was precipitated from solution by using different techniques: Isoelectric point (pI), ammonium sulfate, methanol and ethanol). Optimum pH of chickpea protein solubilization was pH 11, but for lupine and lentil seed proteins pH was 12. Ammonium sulfate and alcohols precipitated all proteins. All proteins were deficient in sulfur amino acids but sufficient in acidic amino acids. Chickpea protein isolated by alcohols registered the highest water absorption, while that recovered by isoelectric point gave medium values. On the other hand, chickpea protein obtained with ammonium sulfate showed the minimum value. The same trend of water absorption was observed in lupine and lentil seed proteins. All proteins recovered by isoelectric point achieved the highest emulsion capacity. While proteins recovered by ammonium sulfate showed the highest emulsion stability. On the other hand, foaming capacity of lentil seed protein recovered by alcohols registered the highest values. Foaming stability of chickpea recovered by ammonium sulfate and ethyl alcohol was the highest while, foaming stability of lupine and lentil seed proteins recovered by ammonium sulfate was attained the highest values. This phenomenon is a function of the agent used for protein precipitation irrespective of the protein source.


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