Structural changes induced by ultrasound improve the ability of the myofibrillar protein to bind flavor compounds from spices

Sun, X.; Yu, Yumei; Saleh, Ahmed S.M.; Yang, Xinyu; Ma, Jiale; Gao, Ziwu; Li, Wenhao; Wang, Zhenyu; Zhang, Dequan

doi:10.1016/j.ultsonch.2023.106510

Cited by 15 publications

(4 citation statements)

References 44 publications

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“…This effect c tributed to the unfolding and depolymerization of MPs, which exposed SH gro aromatic amino acids and induced a conformational transition from α-helix to β-t ditionally, this combined treatment also enhanced the adsorption capacity of MP none compounds by facilitating the formation of hydrophobic, hydrogen, and static bonding sites. In conclusion, the synergistic use of ultrasound and L-lysin a promising approach for enhancing the functionality of meat-based products, Untreated MPs (control) had a higher percentage of free ketones in the headspace, which is related to steric hindrance in the ability of MPs to bind flavour compounds [17]. Except for 2-octanone, the binding capacity of MPs at 20 min of ultrasound treatment only was significantly higher than that of the untreated group.…”

Section: Discussionmentioning

confidence: 86%

“…Except for 2-octanone, the binding capacity of MPs at 20 min of ultrasound treatment only was significantly higher than that of the untreated group. This may be due to the cavitation effects of ultrasound, which led to the unfolding of proteins, the exposure of more active sites, and the interaction of more volatiles with proteins [17]. Only the addition of L-lysine significantly increased the binding capacity of MPs for ketone compounds (p < 0.05).…”

Section: Discussionmentioning

confidence: 99%

“…MPs can bind to flavour compounds through chemical forces such as hydrogen bonds, van der Waals forces, and hydrophobic interactions [16]. The cavitation effects of ultrasonic dissociates water molecules produces highly active hydroxyl radicals and further changes and modifies the structure and intermolecular forces of MPs, thereby affecting the flavour adsorption capacity of MPs [17]. It has been reported that different ultrasound powers can enhance the binding of MPs to furan flavour compounds [18,19].…”

Section: Introductionmentioning

confidence: 99%

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Synergistic Effects of High-Intensity Ultrasound Combined with L-Lysine for the Treatment of Porcine Myofibrillar Protein Regarding Solubility and Flavour Adsorption Capacity

Xie,

Chen,

Cao

et al. 2024

Foods

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This study aimed to investigate the synergistic effects of high-intensity ultrasound (0, 5, 10, 15, and 20 min) in combination with L-lysine (15 mM) on improving the solubility and flavour adsorption capacity of myofibrillar proteins (MPs) in low-ion-strength media. The results revealed that the ultrasound treatment for 20 min or the addition of L-lysine (15 mM) significantly improved protein solubility (p < 0.05), with L-lysine (15 mM) showing a more pronounced effect (p < 0.05). The combination of ultrasound treatment and L-lysine further increased solubility, and the MPs treated with ultrasound at 20 min exhibited the best dispersion stability in water, which corresponded to the lowest turbidity, highest absolute zeta potential value, and thermal stability (p < 0.05). Based on the reactive and total sulfhydryl contents, Fourier transform infrared spectroscopy, and fluorescence spectroscopy analysis, the ultrasound treatment combined with L-lysine (15 mM) promoted the unfolding and depolymerization of MPs, resulting in a larger exposure of SH groups on the surface, aromatic amino acids in a polar environment, and a transition of protein conformation from α-helix to β-turn. Moreover, the combined treatment also increased the hydrophobic bonding sites, hydrogen-bonding sites, and electrostatic effects, thereby enhancing the adsorption capacity of MPs to bind kenone compounds. The findings from this study provide a theoretical basis for the production and flavour improvement of low-salt MP beverages and the utilisation of meat protein.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Synergistic Effects of High-Intensity Ultrasound Combined with L-Lysine for the Treatment of Porcine Myofibrillar Protein Regarding Solubility and Flavour Adsorption Capacity

Xie,

Chen,

Cao

et al. 2024

Foods

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show abstract

“…Low-amplitude ultrasound can induce specific structural changes in protein monomers, forming hydrogen-bonded β-sheet-rich structures, which serve as primary nucleation sites for protein refolding. These changes are initiated by pressure perturbations and accelerated by temperature factors [61]. Additionally, prolonged exposure to low-amplitude ultrasound enables the controlled elongation of amyloid protein nanofibrils directly from monomeric lysozyme proteins.…”

Section: Ultrasound In Protein Refoldingmentioning

confidence: 99%

Ultrasound-assisted innovations in protein processing: review

Rebezov,

Assenova,

Luneva

et al. 2024

Potr. S. J. F. Sci.

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The contemporary landscape of protein processing is witnessing a paradigm shift propelled by innovative technologies. This review unveils innovations in protein processing through the lens of an ultrasound-assisted approach. The focus was on the interplay between ultrasound waves and proteins during ultrasound extraction technology. The realm of protein extraction, where traditional methods face challenges and ultrasound emerges as a transformative force, was highlighted, as well as ultrasound's role in enhancing protein yield and quality in relationship to protein structure and function. Comparative analyses have showcased the remarkable advancements ushered in by ultrasound-assisted techniques, and this review also extends to enzymatic hydrolysis, where ultrasound catalyses reactions, unlocking new dimensions in the production of bioactive peptides and nutritionally enriched proteins. In the bio-industrial sectors, ultrasound facilitates protein refolding and revolutionises recombinant protein production, stability and bioavailability. Ultrasound has emerged as a catalyst for efficiency and bioactivity enhancement, defeating conventional limitations to the intricate optimisation strategies of refolding. This review envisages the advantages of ultrasound technology and its applications in the bio-industrial sector. The prospects of ultrasound-assisted protein processing are outlined, and roadmaps and processing techniques are offered.

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Flavor of extruded meat analogs: A review on composition, influencing factors, and analytical techniques

Jiang,

Yang,

2024

Current Research in Food Science

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Structural changes induced by ultrasound improve the ability of the myofibrillar protein to bind flavor compounds from spices

Cited by 15 publications

References 44 publications

Synergistic Effects of High-Intensity Ultrasound Combined with L-Lysine for the Treatment of Porcine Myofibrillar Protein Regarding Solubility and Flavour Adsorption Capacity

Synergistic Effects of High-Intensity Ultrasound Combined with L-Lysine for the Treatment of Porcine Myofibrillar Protein Regarding Solubility and Flavour Adsorption Capacity

Ultrasound-assisted innovations in protein processing: review

Flavor of extruded meat analogs: A review on composition, influencing factors, and analytical techniques

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