Functional properties were investigated on chickpea proteins acetylated at 6 and 49% of the -amino groups of lysine. In water and in 0.25M NaCl solutions, acetylated chickpea proteins (ACP) were more soluble at high pH (pHϾ8), but less soluble at low pH (pH 2-7), than native chickpea protein (NCP). The solubility of ACP and NCP was reduced in 0.25-0.75M CaCl 2 solutions. Acetylation increased the water and oil absorption capacity of ACP. ACP also had higher emulsion capacity than that of NCP, but acetylation made emulsions of chickpea protein dispersions less stable.These improvements were attributed to the conformational changes in the protein molecules. The related changes in functionality are affected by the extent of acetylation. Extensive acetylation increased hydrophobicity of glycinin while moderately acetylated glycinin showed low hydrophobicity (Kim and Rhee, 1989). The viscosity of field bean and fat absorption of winged bean were related to the degree of acetylation (Schmidt and Schmandke, 1987, Narayana andNarasinga Rao, 1984). Barman et al. (1977) showed that the effect of acetylation could be predicted and the functional properties of soy protein could be altered by varying degrees of acetylation. Thus, acetylation provides a means of improving the functionality of chickpea proteins and may enable further understanding of their behavior in food systems. Our objective was to investigate the effects of acetylation on the functional properties of chickpea proteins.

Flow properties of aqueous chickpea protein dispersions were investigated. The dispersions had Newtonian flow behavior at concentrations up to 4%. Flow behavior became progressively less Newtonian as concentration increased above 4%. The apparent viscosity of the dispersions was pH and concentration dependent, being higher at the protein's most soluble pHs (pH 2 and 9) and lower at the isoelectric point (pH 4-5). Within the investigated temperatures (15, 25, 35 and 55ЊC), power law constants were unchanged up to 35ЊC but the flow behavior became non-Newtonian at 55ЊC. Denaturation by urea and sodium dodecyl sulphate (SDS) increased the consistency index (m), casson yield stress and apparent viscosities, and the flow became more pseudoplastic with a decrease in the flow index (n).Howell and Lawrie, 1987). Our objective was to determine quantitative flow properties of chickpea protein dispersions and the relevant factors affecting their behavior.