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

Chickpea protein isolate (CPI) was used as the starting material in the pro duction of chickpea protein hydrolysates (CPHs). To obtain a highly extensi ve hydrolysate with a degree of hydrolysis higher than 50%, a sequential ut ilisation of endoprotease (Alcalase) and exoprotease (Flavourzyme) was nece ssary. Molecular weight patterns of CPHs were determined by gel filtration chromatography. As a result of the enzymatic activity, differences in the c hromatographic pattern of CPHs were observed. Although significant (P less than or equal to 0.05) decreases of Phe and Arg were observed after hydroly sis, adequate amounts of essential amino acids in relation to the reference pattern of FAO (FAO/WHO/ONU, 1985. Energy and requirements. Technical repo rt series No. 724. Geneva) were found.: In vitro protein digestibility of C PHs (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 respe ct 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. (C) 1999 Elsevier Science Ltd. All rights reserved.