Protein Nanoparticles From Chickpea Albumin, Globulin, and Glutelin — the Impact of Heat Treatment on Secondary Structure, Surface Hydrophobicity, and Properties

Abstract

The potential of nanoparticles produced from chickpea protein fractions to gain enhanced functionality was studied. The effect of heat treatment temperature, time, and pH treatment on the linoleic acid binding ability and nanoparticle stability of three chickpea protein components were perceived through changes in secondary structure. Protein fractions were extracted from defatted chickpea seed using the Osbourne fractional method. Heat treatment was performed for 10 min or 20 min at 90 °C, and at pH 7 or pH 9.3. The smallest nanoparticles (~ 30 nm) were produced by heating glutelin at pH 9.3 for 10 min. Nanoparticles prepared from glutelin and albumin at pH 9.3 showed the highest surface hydrophobicity. The highest binding capacity of linoleic acid was achieved with nanoparticles from albumin fraction at both applied pH 7 and 9.3, and amounted 59% and 68%, respectively. The most stable nanoparticles were prepared from albumin at both applied pH values after 7 days of storage at 4 °C. Differences in properties of prepared nanoparticles could be attributed to different impacts of heat treatment on chickpea protein fractions due to differences in portions of the elements of secondary structure in them.