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Chickpea protein isolates and the protease alcalase were used for the production of protein hydrolysates that inhibit angiotensin I-converting enzyme (ACE). The highest degree of inhibition was found in a hydrolysate obtained by 30 min of treatment with alcalase. This hydrolysate was used as starting material for the puri®cation of ACE-inhibitory peptides. After Biogel P2 gel ®ltration chromatography and HPLC C 18 reverse phase chromatography, four peptides with ACE-inhibitory activity were puri®ed. Two of them were competitive inhibitors of ACE, while the other two were uncompetitive inhibitors. These results show that chickpea proteins are a good source of ACEinhibitory peptides when hydrolysed with the protease alcalase.

Limited rapeseed protein hydrolysates ranging from 3.1 to 7.7% hydrolysis were produced from isoelectric-precipitated protein isolate. Water absorption, oil absorption, whippability, foam capacity and stability, emulsifying activity, and emulsion stability of the hydrolysates were determined. All protein hydrolysates showed better functional properties than the original protein isolate. Foam and emulsion stability decreased as the degree of hydrolysis increased. The hydrolysate with the lowest degree of hydrolysis showed the best functional properties. These improved functional properties make rapeseed protein hydrolysates a useful product to be used in foods such as breads, cakes, ice creams, meat products, desserts, and salad dressings.