Effects of different dry heating temperatures on the spatial structure and amino acid residue side-chain oxidative modification of soybean isolated proteins

Effects of preheat treatment and syringic acid modification on the structure, functional properties, and stability of black soybean protein isolate

“…As shown in Figure 3, the solubility of BSPI declined continuously as the preheat temperature increased, reaching its minimum value (25.42%) at 100°C. This reduction in solubility may be attributed to heat treatment‐induced protein aggregation and cross‐linking, where hydrophilic groups become buried, forming hydrophobic regions (Wen et al., 2023).…”

“…As shown in Figure 3, the solubility of BSPI declined continuously as the preheat temperature increased, reaching its minimum value (25.42%) at 100 • C. This reduction in solubility may be attributed to heat treatment-induced protein aggregation and cross-linking, where hydrophilic groups become buried, forming hydrophobic regions (Wen et al, 2023). Meanwhile, the solubility of BSPI-SA25 and BSPI-SA50 significantly improved compared to the corresponding preheated BSPI, and this improvement positively correlated with the concentration of SA.…”

Protein oxidation‐induced changes in the physicochemical properties and quality of plant food

“…Important oxidised amino acids are 3,4‐dihydroxyphenylalanine and O‐and m‐tyrosine, which are derived from tyrosine and phenylalanine, as well as tryptophan oxidation products N‐formyl kynurenine, kynurenine and oxindole alanine (Fleischer & Hellwig, 2023). Tryptophan, phenylalanine and sulphur‐containing amino acids are prone to oxidative modifications such as deamidation, glycosylation and carbonylation after being attacked by oxygen free radicals (Wen et al ., 2023). For aliphatic amino acids, ROS first attacks the aliphatic amino acid side chain to form RO• derivatives, which are then subjected to β‐excision or intramolecular rearrangement to generate R• and carbonyl derivatives.…”

Improving the gel properties of salted egg white/cooked soybean protein isolate composite gels by ultrasound treatment: Study on the gelling properties and structure

“…It is often used with other constituents in food processing because of its excellent gelling properties, rich nutrition and low cost [8] , as well as used as a major ingredient for tofu and an emulsifier for imitation cheese [9] . Nevertheless, SPI possesses some problems such as poor solubility and anti-nutrient factors influencing digestibility [10] . To enhance the functional properties of SPI, it is generally modified by some physical methods or enzymatic treatment.…”

“…To enhance the functional properties of SPI, it is generally modified by some physical methods or enzymatic treatment. Thereinto, thermal treatment serves as an effective physical method for SPI modification, which unfolds the structures of the protein and exposes buried hydrophobic groups, thus influencing the functional properties of SPI [10] . Mu et al [11] found that microwave pretreatment destroyed the primitive structure of SPI and enhanced the gelling properties.…”