Improvement of functional properties of chickpea proteins by hydrolysis with immobilised Alcalase

Abstract

Limited chickpeaprotein hydrolysates ranging from 1% to 10% degree of hydrolysis were produced from chickpeaprotein isolate (CPI) using Alcalaseimmobilised on glyoxyl-agarose gels. Alcalase-glyoxyl derivative produced after 24 h of immobilisation at room temperature was 24 times more stable than soluble enzyme and presented approximately 51% of the activity of Alcalase. The chemical composition of chickpea hydrolysates were very close to that of CPI. Solubility, oil absorption, emulsifying activity and stability, and foaming capacity and stability were determined. All protein hydrolysates showed higher solubility than intact proteins, especially at pHs near isoelectric point of native chickpeaproteins. Moreover, all hydrolysates had better functionalproperties, except emulsifying activity, than the original protein isolate.