A comprehensive study on structures and characterizations of 7S protein treated by high intensity ultrasound at different pH and ionic strengths

Geng, Mengjie; Liu, Jian; Hu, Hao; Qin, Lang; Taha, Ahmed; Zhang, Zhuo

doi:10.1016/j.foodchem.2021.131378

Cited by 18 publications

(10 citation statements)

References 47 publications

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“…6b. Under acidic conditions, both subunits showed positive ζ, because they were protonated and carried positive charges 40 . The ζ of the α ‐subunit was lower under low ionic strength conditions because the extension region contains more negatively amino acids 8 .…”

Section: Resultsmentioning

confidence: 99%

The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength

Yuan

et al. 2022

J Sci Food Agric

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BACKGROUND To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutral or alkaline conditions (pH 4.0, 7.0, and 8.0) and high or low ionic strength (μ = 0.05 and 0.5), respectively. RESULTS The results showed that the extension region contributed to increasing thermal stability, especially at low ionic strength under acidic and neutral conditions. The extension region stabilized the α‐subunit with high solubility, low turbidity, and small particle size under neutral and alkaline conditions, whereas these impacts were suppressed at a high ionic strength and acidic conditions. Surface hydrophobicity of the α‐subunit decreased under acidic and alkaline conditions without being interfered with by ionic strength. CONCLUSION It can be concluded that the extension region played different roles under different pH and ionic strength conditions. These factors should be specified carefully and speculated individually to explore the more detailed and profound nature of β‐conglycinin at the submolecular level. The results could benefit a better understanding of the relationship between domain structure and functions of soybean protein. © 2022 Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 99%

The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength

Yuan

et al. 2022

J Sci Food Agric

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“…Rennetability of milk (raw form) might be less impacted by PEF and mild heat treatment using low electric field strength and temperatures (≤30 kV/cm, ≤50 C) combinations. The present information shows that PEF could be an alternative to pasteurization for cheese production.8 | THE IMPORTANCE OF PH AND WATER ACTIVITY IN NONTHERMAL MODIFICATION OF PROTEINEnvironmental factors such as pH and water activity are of great importance in nonthermal processing, reference to the effects on food protein functionalities Geng et al (2021). investigated the effect of HIUS (40 min, 20 kHz, room temperature) on soy 7S proteins at various pH (3.0 and 7.0) and ionic strengths (I = 0.1, 0.3, and 0.5).…”

mentioning

confidence: 82%

“…Environmental factors such as pH and water activity are of great importance in nonthermal processing, reference to the effects on food protein functionalities. Geng et al (2021) investigated the effect of HIUS (40 min, 20 kHz, room temperature) on soy 7S proteins at various pH (3.0 and 7.0) and ionic strengths ( I = 0.1, 0.3, and 0.5). When dissolved at pH 7.0 and low ionic strength ( I = 0.1), 7S proteins formed aggregates, whereas large aggregates dissociated at increased ionic strengths ( I = 0.3 or 0.5) after the HIU treatments.…”

Section: The Importance Of Ph and Water Activity In Nonthermal Modifi...mentioning

confidence: 99%

Effects of nonthermal physical processing technologies on functional, structural properties and digestibility of food protein: A review

Pan

Zhang

Mintah

et al. 2022

J Food Process Engineering

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This review assesses the nonthermal physical processing technologies for protein modification. The review also discusses the structural, functional, and digestibility attributes of protein following nonthermal physical processing. Applications of ultrasonication, ultrahigh pressure, and pulsed electric field (PEF) can induce the conformational changes of protein via the creation of free radicals and/or larger/smaller protein molecules, damaging the primary, secondary, tertiary, and quaternary structure of protein, and thus influence the functional properties. Some key achievements in using nonthermal physical technologies to process protein‐rich foods include improved enzymatic hydrolysis, solubility, emulsification, foaming, gelatinization, digestion properties, and reduced allergenicity. Therefore, nonthermal physical technologies are useful methods to modify food protein structure and functionality for the food industry. Practical Application The demand for protein with desirable functional properties and nutritional value makes it imperative to find suitable processing technologies that could conserve or yield high quality proteins from both conventional and nonconventional sources. Since thermal processing (including microwave, radiofrequency heating, etc.) could possibly reduce the quality attributes of proteins, many researchers have focused their investigations on nonthermal physical processing to improve the functional properties of proteins. To this regard, this review discusses nonthermal techniques, including ultrasonication, high‐pressure processing, PEFs, cold plasma, and ultraviolet.

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“…Not only animal-derived proteins but similar phenomena were also seen in the effects of HIU on the structure of amaranth isolates and chickpea isolates studied by Tomé Constantino & Garcia-Rojas [37] and Xu et al [38] , respectively. Further, a recent study found that the surface hydrophobicity of soybean 7S proteins with higher ionic strength was significantly higher than that of soybean 7S proteins with lower ionic strength after HIU treatment at pH = 7.0 [39] . However, they also found that increasing the ionic strength did not significantly improve the hydrophobicity of the protein surface under the HIU field at pH = 3.0.…”

Section: Changes Of the Structure Of Proteins By Hiumentioning

confidence: 93%

Recent advances in modified food proteins by high intensity ultrasound for enhancing functionality: Potential mechanisms, combination with other methods, equipment innovations and future directions

Chen

Wang

2022

Ultrasonics Sonochemistry

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A comprehensive study on structures and characterizations of 7S protein treated by high intensity ultrasound at different pH and ionic strengths

Cited by 18 publications

References 47 publications

The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength

The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength

Effects of nonthermal physical processing technologies on functional, structural properties and digestibility of food protein: A review

Recent advances in modified food proteins by high intensity ultrasound for enhancing functionality: Potential mechanisms, combination with other methods, equipment innovations and future directions

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