- Volume 19 Issue 6
The functional properties of lupin seed protein concentrate (LPC) were examined and compared to those of soybean protein isolate (SPI) and Na-caseinate. LPC-50, of which protein level was 50%, was prepared by a two phase solvent (hexane: alcohol: water= 10:7:3) extraction method. LPC-70 was made from LPC-50 by removing the fractions solubilized by carbohydrate decomposing enzymes. The solubilities of LPC-50 and LPC-70 were similar to that of of SPI but slightly higher at pH 4-5, and less susceptible to the added salt. The apparent viscosity of LPC increased exponentially as the concentration increased over 6% level, and the change was similar to that of Na-caseinate. LPC showed strong pseudoplastic non-Newtonean flow behavior, which was similar to that of SPI The emulsifying capasity of LPC-70 was similar to that of SPI when salt was added. The foaming capacity of LPC was comparable to that of SPI. LPC showed high oil and water absorption capacities, which increased as the protein level was elevated. LPC-70 showed the highest oil absorption capacity of all the samples tested.