Abstract
This study examined the impact of extreme pH-cycling treatments on chickpea protein isolate (CPI). Untreated CPI, along with samples shifted to pH 2 (pH2) and pH 12 (pH12), displayed solubilities of 60.25%, 25.01%, and 75.48%, respectively. Both treatments significantly improved water and oil absorption capacities. Emulsion activity and stability for CPI at pH2 and pH12 were 125 m2/g and 110 m2/g, respectively, versus 75 m2/g for the untreated sample. Notably, the foaming capacity and stability of pH12-treated CPI increased by 3.5 and 8.8 times, respectively, compared to the untreated protein. pH12-treated CPI also demonstrated the lowest gelling concentration at 10%, compared to 14% and 18% for untreated and pH2-treated CPI, respectively. Microstructural analysis revealed partial disintegration of CPI under pH-cycling, underscoring that alkaline pH12-shifting notably enhances functional properties of CPI.
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