Summary A study on the emulsifying capacity and water binding capacity of lupin protein (isolates and concentrates) using various isolation procedures was carried out. These procedures included protein extraction in single or double step in alkaline or acid conditions by the use of a wet or dry milling technique. Different ion conditions were also used. For comparison, soya bean and lupin protein were extracted through a co‐precipitation procedure. Protein extraction by wet milling and then precipitation and drying at isoelectric pH promoted water binding capacity, while dry milling and alkaline extraction enhanced the emulsifying capacity. Protein co‐precipitation and ion environmental conditions are other factors influencing the emulsifying capacity and water binding capacity. The proper choice of these parameters will determine the optimum conditions for emulsifying and water binding capacity of a protein isolate or concentrate.