Effects of ionic strength and (−)-epigallocatechin gallate on physicochemical characteristics of soybean 11S and 7S proteins

Yang, Yaxuan; Wang, Qiming; Tang, Yuwan; Lei, Lin; Zhao, Jing; Zhang, Yuhao; Li, Lin; Wang, Qiang; Ming, Jian

doi:10.1016/j.foodhyd.2021.106836

Cited by 32 publications

(16 citation statements)

References 52 publications

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Section: Resultsmentioning

confidence: 99%

“…On the one hand, it is possible that the 11S subunits produced dimers during the gel process, and the dimers combined to form stronger and more stable quaternary structures. However, the amino acid residues were buried in the hydrophobic region, and the DH of amino acid was relatively small (Yang, Wang, et al, 2021). Renkema et al (2001) reported that the strength of 11S globulin thermal gel was greater than the 7S, indicating that the 11S globulin molecule contained more disulfide bonds and fewer thiol/disulfide bond exchanges.…”

Section: Changes In the Dh And Surface Hydrophobicity Of Tgase-treate...mentioning

confidence: 99%

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Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase

Huang

Sun

Zhao

et al. 2022

Food Science & Nutrition

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Section: Resultsmentioning

confidence: 99%

Section: Changes In the Dh And Surface Hydrophobicity Of Tgase-treate...mentioning

confidence: 99%

Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase

Huang

Sun

Zhao

et al. 2022

Food Science & Nutrition

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“…Turbidity enhancement of protein dispersion indicates the formation of larger particles by aggregation 26 . The salt ions shielded the surface charge and reduced the electrostatic repulsion between protein molecules, promoting an increment in turbidity 27 …”

Section: Resultsmentioning

confidence: 99%

“…26 The salt ions shielded the surface charge and reduced the electrostatic repulsion between protein molecules, promoting an increment in turbidity. 27 Under neutral and alkaline conditions, the turbidity of the ⊍and ⊍c-subunits showed opposite results. The turbidity of the ⊍-subunit was significantly lower than that of the ⊍c-subunit.…”

Section: The Effect Of the Extension Region On The Turbidity At Diffe...mentioning

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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“…Physicochemical properties of 11S and 7S proteins are affected by interactions with phenolic compounds and ionic strength, with 11S more sensitive than 7S (Y. Yang et al, 2021), which might explain the higher stability for complexes made from ANC and 11S soy protein.…”

Section: Mueller Et Al (2018)mentioning

confidence: 99%

Protein‐binding approaches for improving bioaccessibility and bioavailability of anthocyanins

Oliveira

Lila

2022

Comp Rev Food Sci Food Safe

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Color is an important characteristic of food. Over the last 15 years, more attention has been paid to natural colorants because of the rising demand for clean-label food products. Anthocyanins, which are a group of phytochemicals responsible for the purple, blue or red hues of many plants, offer a market advantage. In addition, anthocyanin-rich foods are associated with protection against cardiovascular disease, thrombosis, diabetes, cancer, microbial-based disorders, neurological disorders, and vision ailments. However, the real health value of anthocyanins, whether as a natural colorant or a functional ingredient, is dependent on the ultimate bioaccessibility and bioavailability in the human body. Many animal and human clinical studies revealed that, after intake of anthocyanin-rich foods or anthocyanin extracts, only trace amounts (< 1% of ingested content) of anthocyanins or their predicted metabolites were detected in plasma after a standard blood draw, which was indicative of low bioavailability of anthocyanins. Protein binding to anthocyanins is a strategy that has recently been reported to enhance the ultimate bioactivity, bioaccessibility, and bioavailability of anthocyanins as compared to anthocyanins delivered without a protein carrier. Therefore, in this review, we address anthocyanin properties in food processing and digestion, anthocyanin-protein complexes used in food matrices, and changes in the bioaccessibility and bioavailability of anthocyanins when bound into anthocyanin-protein complexes in foods. Finally, we summarize the challenges and prospects of this delivery system for anthocyanin pigments.

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Effects of ionic strength and (−)-epigallocatechin gallate on physicochemical characteristics of soybean 11S and 7S proteins

Cited by 32 publications

References 52 publications

Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase

Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase

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

Protein‐binding approaches for improving bioaccessibility and bioavailability of anthocyanins

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