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Lupin protein isolates were prepared by alkaline extraction and precipitation at pH 5.1, 4.2 and 4.9 and their functional properties investigated. Solubility, emulsification capacity, swelling and gelation properties were determined under different conditions of pH, ionic strength and heat treatment. Lupin protein isolates showed better solubility than soybean isolate and a similar emulsification capacity. Swelling and gelation were found to be inferior, but when modifications in the methods of isolate preparation were introduced these properties were significantly improved. Consequently, it is possible to consider lupin proteins as a potential substitute for soybean proteins in food applications.

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