High-intensity ultrasound improved the physicochemical and gelling properties of Litopenaeus vannamei myofibrillar protein

Li, Na; Zhang, Kexin; Du, Jia‐Yi; Tan, Zhifeng; Xu, Yunpeng; Liu, Xiaoyang; Zhou, Da‐Yong; Li, De-Yang

doi:10.1016/j.ultsonch.2022.106217

Cited by 39 publications

(49 citation statements)

References 35 publications

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“…For example, the carbonyl content reached a maximum ( p < 0.05) when the ultrasound power was increased to 600 W, which was approximately 11.45 times higher than that of the control group. Generally speaking, the carbonylation of proteins is mainly attributed to the oxidation of amino acid side chains and the aldehydes produced by lipid oxidation can also bind to amino acid side chain groups to form Schiff bases thereby increasing the carbonyl content [2] . In this study, ultrasound led to the increase of carbonyl groups in N. taihuensis MP, which might be due to the fact that the secondary structure of N. taihuensis MP contained many loose and disordered random curl structures.…”

Section: Resultsmentioning

confidence: 99%

“…Li et al [9] showed that the MP emulsification behavior was significantly improved after ultrasound, and a more stable emulsion could be obtained from the MP. Similarly, Li et al [2] also reported that ultrasound treatment improved the functional properties of shrimp MP and its gel properties. At present, there are few literatures on the effects of processing technology on the N. taihuensis MP and its related surimi products, mainly focusing on squid, shrimp and poultry meat.…”

Section: Introductionmentioning

confidence: 84%

“…The ultrasound treatment of N. taihuensis MP was performed with a reference of our previous method [2] . An ultrasonic cell disruptor (SCIENTZ-II D, Ningbo, China) was used to treat MP solution.…”

Section: Methodsmentioning

confidence: 99%

“…MP contributes to more than 90% of the development of the emulsifying capability of aquatic muscle food. It could be adsorbed to form an interfacial protein membrane on the surface of fat globules/oil droplets in the emulsified meat system [2] , [3] , [4] . In addition, MPs are easily digestible and rich in all essential amino acids, which make them popular functional ingredients in food formulations and allowing the preparation of stable emulsions as nutrient delivery systems.…”

Section: Introductionmentioning

confidence: 99%

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High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability

Deng

Han

et al. 2023

Ultrasonics Sonochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 84%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability

Deng

Han

et al. 2023

Ultrasonics Sonochemistry

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“…The sample concentration of whey protein solution to be measured was 0.25. The acquisition interval was 1 nm [ 20 ]. The control group was untreated WPI.…”

Section: Methodsmentioning

confidence: 99%

Investigation of the Structure and Allergic Potential of Whey Protein by Both Heating Sterilization and Simulation with Molecular Dynamics

Zhang

et al. 2022

Foods

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As the main allergens in milk, whey proteins are heat-sensitive proteins and are widespread in dairy products and items in which milk proteins are involved as food additives. The present work sought to investigate the effect of heating sterilization on the allergenicity of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG), the main composite and allergen in whey protein isolate (WPI), by combining molecular dynamics with experimental techniques for detecting the spatial structure and IgE binding capacity. The structure of WPI was basically destroyed at heat sterilization conditions of 95 °C for 5 min and 65 °C for 30 min by SDS-PAGE analysis and spectroscopic analysis. In addition, α-lactalbumin (α-LA) may be more sensitive to temperature, resulting in exposure to allergic epitopes and increasing the allergic potential, while the binding capacity of β-lactoglobulin (β-LG) to IgE was reduced under 65 °C for 30 min. By the radius of gyration (Rg) and root-mean-square deviation (RMSD) plots calculated in molecular dynamics simulations, α-LA was less structurally stable at 368 K, while β-LG remained stable at higher temperatures, indicating that α-LA was more thermally sensitive. In addition, we observed that the regions significantly affected by temperatures were associated with the capacity of allergic epitopes (α-LA 80–101 and β-LG 82–93, 105–121) to bind IgE through root-mean-standard fluctuation (RMSF) plots, which may influence the two major allergens. We inferred that these regions are susceptible to structural changes after sterilization, thus affecting the allergenicity of allergens.

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Investigation of Soy Protein Isolate-Konjac Glucomannan Sodium Salt Hydrogel: Molecular Docking, Microstructure, Rheological Properties, and 3D Printing Characteristics

Zhang,

Li,

Tan

et al. 2024

Food Bioprocess Technol

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High-intensity ultrasound improved the physicochemical and gelling properties of Litopenaeus vannamei myofibrillar protein

Cited by 39 publications

References 35 publications

High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability

High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability

Investigation of the Structure and Allergic Potential of Whey Protein by Both Heating Sterilization and Simulation with Molecular Dynamics

Investigation of Soy Protein Isolate-Konjac Glucomannan Sodium Salt Hydrogel: Molecular Docking, Microstructure, Rheological Properties, and 3D Printing Characteristics

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