Protein hydrolysates wer e obtained from lupin flour and from the purified globulin α -conglutin, and their functional properties were studied. Hydrolysis with alcalase for 60 minutes yielded degrees of hydrolysis ranging from 4 % to 11 % for lupin flour, and from 4 % to 13% for α -conglutin. Protein solubility, oil absorption, foam capacity and stability, emulsifying activity, and emulsion stability of hydrolysates with 6% degree of hydrolysis were determined and compared with the properties of the original flour. The protein hydrolysates showed better functional properties than the original proteins. Most importantly, the solubility of the α -conglutin and L. angustifolius flour hydrolysates was increased by 43 % and 52 %, respectively. Thus, lupin seed protein hydrolysates have improved functional properties and could be used in the elaboration of a variety of products such as breads, cakes, and salad dressings.