Protein quality of chickpea ( Cicer arietinum L.) protein hydrolysates

Abstract

Chickpea protein isolate (CPI) was used as the starting material in the production of chickpea protein hydrolysates (CPHs). To obtain a highly extensive hydrolysate with a degree of hydrolysis higher than 50%, a sequential utilisation of endoprotease (Alcalase) and exoprotease (Flavourzyme) was necessary. Molecular weight patterns of CPHs were determined by gel filtration chromatography. As a result of the enzymatic activity, differences in the chromatographic pattern of CPHs were observed. Although significant ( P⩽0.05) decreases of Phe and Arg were observed after hydrolysis, adequate amounts of essential amino acids in relation to the reference pattern of FAO (FAO/WHO/ONU, 1985. Energy and requirements. Technical report series No. 724. Geneva) were found. In vitro protein digestibility of CPHs (95%) were similar to that of the starting material (CPI), and TIA was not detected in any case. A high increase of solubility in CPHs, with respect to CPI, was observed, one CPH being totally soluble over a wide pH range (2–10) when the enzymes were added sequentially. Due to their high protein quality and solubility, CPHs might be considered as potential ingredients in the food industry.