Physicochemical properties and storage stability of soybean protein nanoemulsions prepared by ultra-high pressure homogenization

Abstract

This study investigated the effects of the ultrahigh pressure homogenization (pressure, protein concentration, oil phase fraction, pH, temperature, and ionic strength) and storage on the properties of nanoemulsions (100-500nm range), which were stabilized by laboratory-prepared soybean protein isolate (SPI), β-conglycinin (7S) and glycinin (11S). The nanoemulsions made with SPI, 7S and 11S proteins exhibited considerable stability over various ionic strengths (0-500mM NaCl), pH (<4 or >7), thermal treatments (30-60°C) and storage (0-45days). The far-UV spectra of SPI, 7S, 11S dispersions, and SPI-, 7S-, 11S protein-stabilized nanoemulsions were analyzed for the protein structural changes following lipid removal. The ultra-high pressure homogenization changed the secondary structure of SPI, 7S, 11S proteins in the nanoemulsions, and enhanced their stability. This study demonstrated that SPI, 7S, and 11S proteins can be used as effective emulsifiers in nanoemulsions prepared by ultra-high pressure homogenization.

Keywords: 8-Anilino-1-naphthalenesulphonic acid (PubChem CID: 1369); Acetone (PubChem CID: 180); Disodium hydrogen phosphate (PubChem CID: 24203); Glycinin; Hydrochloric acid (PubChem CID: 313); Monosodium phosphate (PubChem CID: 23672064); Nanoemulsions; Sodium azide (PubChem CID: 33557); Sodium chloride (PubChem CID: 5234); Sodium dodecyl sulfate (PubChem CID: 3423265); Sodium hydroxide (PubChem CID: 14798); Soybean protein isolate; Storage stability; Ultra-high pressure homogenization; β-Conglycinin.