The characteristics of soybean protein isolate obtained by synergistic modification of high hydrostatic pressure and phospholipids as a promising replacement of milk in ice cream

High Hydrostatic Pressure: Influences on Allergenicity, Bioactivities, and Structural and Functional Properties of Proteins from Diverse Food Sources

“…In the context of functional properties, emulsion properties have been a focal point in discussions due to the impact of HHP. Indices such as EAI and ESI in various legumes, including kidney beans [ 36 ], peas [ 37 ], soybeans [ 47 , 48 ], walnuts [ 41 ], lentils, and faba beans [ 38 ], were notably influenced by HHP ( Table 1 ). An increase in EAI occurred due to protein unfolding under HHP, leading to an augmented hydrophobic exposure [ 47 ].…”

“…The heightened hydrophobic regions exposed under increased pressure facilitated interaction with oil droplets, resulting in smaller emulsified particles [ 37 ]. Similarly, the increased hydrophobic sites revealed by higher pressure promoted greater surface hydrophobicity in legume proteins from peanuts [ 39 ], soybeans [ 47 , 48 , 49 ], and walnuts [ 41 ]. This increment in surface hydrophobicity further enhanced the foaming capacity and stability of kidney beans [ 36 ], soybeans [ 48 ], walnuts [ 41 ], and pulse proteins [ 38 ].…”

“…Similarly, the increased hydrophobic sites revealed by higher pressure promoted greater surface hydrophobicity in legume proteins from peanuts [ 39 ], soybeans [ 47 , 48 , 49 ], and walnuts [ 41 ]. This increment in surface hydrophobicity further enhanced the foaming capacity and stability of kidney beans [ 36 ], soybeans [ 48 ], walnuts [ 41 ], and pulse proteins [ 38 ]. Moreover, changes in conformation, such as a reduction in β-sheet content, were associated with improved emulsifying and foaming properties.…”

“…Moreover, changes in conformation, such as a reduction in β-sheet content, were associated with improved emulsifying and foaming properties. Yan et al [ 48 ] reported that decreased β-sheet content can enhance these properties of soy protein isolates. These improved properties support the application of proteins modified by HHP.…”

“…Conversely, the solubility of proteins treated by HHP displayed inconsistency. The solubility of proteins from almonds [ 30 ], cowpeas [ 32 ], peas, lentils, and faba beans [ 38 ] decreased, while that of proteins from soybeans [ 47 , 48 , 49 ] and walnuts [ 41 ] increased. These different outcomes were likely a result of the degree of denaturation.…”