Reduction of soybean globulin antigen by soybean protein isolate/γ-aminobutyric acid complexes: Effect of the different concentrations of γ-aminobutyric acid on the protein modification, antigen levels, and foaming properties

Abstract

Soybean flour has received increasing attention because of its unique nutritional properties. However, potential allergies to soy protein limit its application. This study aims to investigate the impact of various concentrations of γ-aminobutyric acid (GABA) on the secondary structure, foaming properties, and antigenicity of soybean protein obtained from soybean flour under thermal sterilisation. GABA increased the content of α-helix, reduced β-turn and random coil in soybean protein. The results indicated that after heating treatment, the concentration of GABA significantly affects the spatial conformation of soybean protein isolates (SPI). When the concentration of GABA was 0.40% (w/v), the particle size, zeta potential, and surface hydrophobicity of the SPI were the lowest, whereas the disulfide bond content was the highest. Multi-spectral technologies indicated that adding 0.40% GABA could assemble the system in a relatively stable manner. Moreover, the rigid structure of the protein was destroyed. This structural change significantly reduced the foaming and allergy of the protein. Adding 0.40% GABA could reduce the β-conglycinin antigen concentration from 24.26 mg/mL to 4.43 mg/mL. This study provides new insights into the production of new low-allergenic soybean flour. Additionally, it offers an assurance for the safe consumption of soybeans by individuals with allergies.