Ultrasound treatment modified the functional mode of gallic acid on properties of fish myofibrillar protein

Ultrasonic pre-treatment modifies the pH-dependent molecular interactions between β-lactoglobulin and dietary phenolics: Conformational structures and interfacial properties

“…Ultrasound cavitation generates strong shear and mechanical forces to dissociate insoluble aggregates by disrupting the hydrogen bonds and hydrophobic interactions, thus enabling strong protein-water interactions [20] . Under both pH, the presence of EGCG/CA statistically diminished the solubility of NLG and ULG-35 ( p < 0.05), which can be explained by a less polar microenvironment and the formation of larger complex particles [5] , in line with previous reports in egg white–EGCG [5] and myofibrillar protein–GA samples [22] . With the aid of ultrasound irradiation, compared to NLG–phenolic groups, phenolic addition witnessed a 3.2%–10.1% increment in the solubility of β-LG, except for a 11.6% reduction in ULG-35–CA system at pH 2.4.…”

“…Given this, it is expected that the sonication of proteins would have a profound impact on their subsequent interactions with phenolic ingredients. To our knowledge, only a few studies have investigated the role of ultrasound on protein–phenolic binding, such as emodin–micellar casein [38] , egg white–gallic acid (GA)/EGCG [5] , and myofibrillar protein–GA systems [22] . Despite extensive research on β-LG relating phenolic addition and ultrasound alone, no studies have yet focused on the ultrasound-driven changes in the interactions between β-LG and dietary phenolics, results of which would provide greater insights into the utilization of both techniques in the dairy products.…”

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

“…In the same study, free radicals were only detected in UVA irradiated and PTE‐treated MP f and not in the control samples with only UVA or PTE, indicating that both UVA irradiation and PTE are required to generate and maintain free radicals. Similarly, ultrasonication, which produced • H, drastically increased gel storage modulus (G ' ) from 410 to 14,137 Pa in MP f treated with 5 μmol/g of gallic acid (Pan et al., 2020). MS analysis confirmed the formation of covalent adduction of oxidized GA to cysteine and lysine residues in proteins, which likely contributed to the improved gelling properties.…”

“…Several methods have been employed to introduce oxidative stress in the study of MP f –phenol interactions and consequential structure‐related functionality. They include Fenton oxidation (Cao & Xiong, 2015; Chen et al., 2016; Feng et al., 2017; Jia et al., 2017; Tang et al., 2017), enzymatic oxidation (Guo & Xiong, 2019; Vate & Benjakul, 2016a), malondialdehyde (MDA)‐mediated oxidation (Lv et al., 2019; Lv et al., 2020), and processing‐induced oxidation (Jiang et al., 2020; Pan et al., 2020). A general conclusion based on these investigations is that mild oxidation promotes gelation while strong oxidation jeopardizes the process (Figure 6).…”

Modification of myofibrillar protein functional properties prepared by various strategies: A comprehensive review

“…(2018) also indicated that the solubility, emulsifying properties, and gel properties of pork MP could be considerably enhanced after being subjected to 30 min of HIU at 300 W. Recently, HIU treatment was found to promote structural unfolding and reactive groups (SH and NH 2 ) exposure in Japanese seerfish MP molecules. Additionally, the addition of low dose (1, 5, and 25 µmol/g) gallic acid coupled with HIU treatment improved the MP gelling potential due to strengthened cross‐linking (S‐S and protein‐S‐GA‐S‐protein) (Pan et al., 2020).…”