ABSTRACT
The paper presents the effect of heat treatment at 80 °C at different times (3, 5, 7, and 9 min) on the structural and functional properties of Phaseolus vulgaris L. protein (PVP, bean protein powder). Surface and structure properties of PVP after heat treatment were analyzed using a Fourier transform infrared spectrometer (FTIR), a fluorescence spectrophotometer, a visible light spectrophotometer, a laser particle size analyzer, and other equipment. The secondary structure and surface hydrophobicity (H0) of PVP changed significantly after heat treatment: the ß-sheet content decreased from 25.32 ± 0.09% to 24.66 ± 0.09%, the random coil content increased from 23.91 ± 0.11% to 25.68 ± 0.08%, and the H0 rose by 28.96-64.99%. In addition, the functional properties of PVP after heat treatment were analyzed. After heat treatment, the emulsifying activity index (EAI) of PVP increased from 78.52 ± 2.01 m2/g to 98.21 ± 1.33 m2/g, the foaming ability (FA) improved from 87.31 ± 2.56% to 95.82 ± 2.96%, and the foam stability (FS) rose from 53.23 ± 1.72% to 58.71 ± 2.18%. Finally, the degree of hydrolysis (DH) of PVP after gastrointestinal simulated digestion in vitro was detected by the Ortho-Phthal (OPA) method. Heat treatment enhanced the DH of PVP from 62.34 ± 0.31% to 73.64 ± 0.53%. It was confirmed that heat treatment changed the structural properties of PVP and improved its foamability, emulsification, and digestibility. It provides ideas for improving PVP's potential and producing new foods with rich nutrition, multiple functions, and easy absorption.
ABSTRACT
In this paper, the effects of homogenization at low pressure (1~40 MPa) on structural and functional properties of soy protein isolates (SPI) are investigated. Homogenization at low pressure increase solubility, surface hydrophobicity, emulsification activity and foaming capacity of SPIs, these all functional properties increases and then decreases with the homogenization pressure. Whereas, emulsion stability and foaming stability of SPIs treated by homogenization initially decrease and then increase with homogenization pressure. There is a dramatic decrease in hardness, springiness and cohesiveness of homogenized SPI gels. Generally, homogenization at low pressure do not change the subunit composition of SPIs. It is observed that, when the homogenization pressure is lower than 10 MPa than there is no significant impact on structural change. The content of ß-sheet decreased, while unordered structure significantly increased, when the homogenization pressure increased from 10 MPa to 20 MPa. Furthermore, the content of ß-sheet increases, when the content of the other structures decreases with the increasing homogenization pressure. The maximum emission wavelength (λmax) for SPIs increases with homogenization pressure increases from 10 Mpa to 20 Mpa, which is attributed to the gradual structural unfolding exposing more hydrophobic residues in protein surface. While, the decreased λmax of SPIs treated with 20 Mpa to 40 Mpa homogenization corresponds to the protein aggregation. It can be deduced that appropriate selection of homogenization pressure is important for improving the functional properties of SPIs.
