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

Huang, Zhanrui; Sun, Jing Ping; Zhao, Liang; He, Weidong; Liu, Teyuan; Liu, Binbin

doi:10.1002/fsn3.2706

Cited by 26 publications

(9 citation statements)

References 55 publications

(98 reference statements)

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“…Hydrophobic interactions are the main forces that maintain the tertiary structure of proteins, and they play an important role in the stability, conformational, and functional properties of protein structures. Surface hydrophobicity is the main physical parameter for evaluating proteins and it better reflects the interaction of proteins with water and other chemical groups 30 . The ANS fluorescence probe is a classical method to evaluate the surface hydrophobicity of proteins.…”

Section: Resultsmentioning

confidence: 99%

“…Surface hydrophobicity is the main physical parameter for evaluating proteins and it better reflects the interaction of proteins with water and other chemical groups. 30 The ANS fluorescence probe is a classical method to evaluate the surface hydrophobicity of proteins. It is a reflection of the three-dimensional structure of proteins in an aqueous solution.…”

Section: Surface Hydrophobicity (H0)mentioning

confidence: 99%

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Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Sun

Wang

et al. 2023

J Sci Food Agric

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Background High‐pressure homogenization (HPH) is commonly used as a non‐thermal processing technique for soybean and soy protein products, and the preparation of soy protein gel products often requires the synergistic effect of HPH and heat treatment. The dissociative association behavior of 11 S is the key to the protein gel formation state. In this study, therefore, 11 S thermal gels were prepared by high‐pressure homogenization and co‐induction (90 °C, 30 min) (adding Ca2+ to promote gel formation before heat treatment), and the effects of different high‐pressure homogenization pressures (0–100 MPa) and co‐treatment on the dissociative association behavior of 11 S protein, gel properties, and microstructure of 11 S gels were investigated. Results The results showed that HPH at higher pressures led to the breaking of disulfide bonds of aggregates and disrupted non‐covalent interactions in protein aggregates, leading to collisions between protein aggregates and the reduction of large protein aggregates. High‐pressure homogenization treatment at 60 MPa improved the gel properties of 11 S more. The HPH combined with heating changed the binary and tertiary structure of 11 S soy globulin and enhanced the hydrophobic interaction between 11 S molecules, thus improving the gel properties of 11 S. The change in intermolecular forces reflected the positive effect of HPH treatment on the formation of denser and more homogeneous protein gels. Conclusion In conclusion, high‐pressure homogenization combined with heating can improve the properties of 11 S gels by changing the structure of 11 S protein, providing data and theoretical support for soy protein processing and its further applications. © 2022 Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 99%

Section: Surface Hydrophobicity (H0)mentioning

confidence: 99%

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Sun

Wang

et al. 2023

J Sci Food Agric

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“…The authors reported an improvement in the rheological properties and higher water‐holding capacity (>98%) for TGase‐induced gels. For TGase‐treated SPI, 7S, and 11S, sulfhydryl and surface hydrophobicity were lower; conversely, both the DH and the β‐sheets contents were increased significantly (Huang, Sun, Zhao, He, Liu, & Liu, 2022). Luo et al (2019) observed more resistance to deformation of the gels when SPI emulsions were treated with low TGase concentrations (1 and 3 U/g protein) prior to the gelation.…”

Section: Enzymatic Modificationsmentioning

confidence: 99%

“…Therefore, proteins with higher lysine and glutamine contents are potentially more favorable substrates for the TGase enzyme. These cross‐linking reactions promote the chemical bonding of adjacent protein molecules and form a new tertiary network structure, which can improve the water‐binding capacity, stability, and mechanical properties of the proteins (Huang, Sun, Zhao, He, Liu, & Liu, 2022). Glusac et al (2020) evaluated the effects of TGase on the digestibility and physical stability of chickpea protein isolate (CPI)‐stabilized o/w emulsions.…”

Section: Enzymatic Modificationsmentioning

confidence: 99%

Recent advances in legume protein‐based colloidal systems

Tarahi

Ahmed

2023

Legume Science

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Developing nature‐derived surface‐active ingredients with favorable interfacial and functional properties has recently received increasing attention in the food and pharmaceutical industries. Legume proteins are used extensively in food colloidal systems because of their small particle size, high water absorption capability, excellent functional properties (e.g., emulsification, foamability, and gelation), and film formation. There are some limitations in legume proteins, such as high water vapor permeability and fragility, as well as low stability and solubility. Various conventional and innovative processing technologies (e.g., high‐pressure homogenization, ultrasonication, and cold plasma processing) have been successfully employed in order to modify the functional and interfacial properties of legume proteins. In this review, the formation and stability of legume protein‐based colloidal systems and their applications are discussed.

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“…1A and B). The polarity of the environment surrounding the SPI was changed by the urea molecules, resulting in protein swelling, hydrogen bond breakage, and a signi cant increase in average particle size (Huang et al, 2022). Previous studies have shown that the hydrogen bonds of soy peptide nanoparticles are disrupted by urea leading to an increase in their average particle size (Zhang et al, 2018).…”

Section: Spi-sa6 Stability Analysismentioning

confidence: 99%

The antibacterial activity and Pickering emulsion stabilizing effect of a novel peptide, SA6, isolated from salted-fermented Penaeus vannamei

Shen

Dai

Juventus

et al. 2022

Preprint

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This study aimed to improve bacterial inhibition in Pickering emulsions during storage using antimicrobial peptides. A peptide (ARHQGVMVGMGQK), designated SA6, isolated from the broth of salt-fermented shrimp (Penaeus vannamei). Peptide SA6 had a minimum inhibitory concentration (MIC) of 15.6 μg/mL against Staphylococcus aureus. The mean particle size of SPI-SA6 particles (417.4 nm) was significantly smaller compared with soybean isolate protein (SPI) (463.3 nm). Moreover, the polydispersity index (PDI) decreased with increasing peptide concentration, while the particles were stabilized by hydrogen bonding. SPI-SA6 Pickering emulsions were stable for the entire storage period (7 d) and had lower creaming index and droplet size compared with SPI Pickering emulsions. Further, SPI-SA6 Pickering emulsion could effectively inhibit bacterial growth and disrupt bacterial cell membrane structure, to significantly decrease bacteria (S. aureus) numbers to 2.83 CFU/mL during storage and therefore extending the inhibition time. Collectively, peptide SA6 could stabilize Pickering emulsion while exerting antibacterial effects.

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

Abstract: This is an open access article under the terms of the Creat ive Commo ns Attri bution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

Cited by 26 publications

References 55 publications

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Recent advances in legume protein‐based colloidal systems

The antibacterial activity and Pickering emulsion stabilizing effect of a novel peptide, SA6, isolated from salted-fermented Penaeus vannamei

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

Abstract: This is an open access article under the terms of the Creat ive Commo ns Attri bution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

Cited by 26 publications

References 55 publications

Effect of high‐pressure homogenization on Ca2+‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca2+‐induced gel formation of soybean 11 S globulin

Recent advances in legume protein‐based colloidal systems

The antibacterial activity and Pickering emulsion stabilizing effect of a novel peptide, SA6, isolated from salted-fermented Penaeus vannamei

Contact Info

Product

Resources

About

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin