Obtainment and physical-chemical and functional characterization of a lupin (Lupinus mutabilis Sweet ) protein hydrolyzate

A lupin protein isolate was used as substrate for the sequential enzymatic hydrolysis with papain and Flavourzyme® nutritious degree. The electrophoretic analysis revealed the presence of 4 predominant bands with molecular weights between 21 and 7.0 kDa. With the extensive hydrolysis, the dispersibility index of the protein isolate increased from 98 to 100%, the solubility increased to 93.3 % value with pH 4.5. The pH and protein concentration influenced positively on the capacity of foam formation, reaching 460% of volume increase with pH 10. However the formed foams were more unstable than those from the protein isolate. The proteolysis did not affect drastically to viscoelastic properties of the protein.