Effects of low‐frequency magnetic field on solubility, structural and functional properties of soy 11S globulin

BACKGROUND Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the low‐frequency magnetic field (LF‐MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical p...

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Published inJournal of the science of food and agriculture Vol. 104; no. 10; pp. 5944 - 5954
Main Authors Kang, Zhuang‐Li, Yao, Peng‐Lei, Xie, Jing‐jie, Li, Yan‐ping, Ma, Han‐Jun
Format Journal Article
LanguageEnglish
Published Chichester, UK John Wiley & Sons, Ltd 15.08.2024
John Wiley and Sons, Limited
Subjects
agriculture
Disulfide bonds
disulfides
Foaming
foaming capacity
Food industry
gel strength
gels
Globulins
Globulins - chemistry
Globulins - metabolism
Glycine max - chemistry
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
low‐frequency magnetic field
Magnetic Fields
Magnetic properties
Physicochemical properties
Protein Conformation
Protein folding
Protein structure
Proteins
Rheological properties
rheological property
Rheology
Solubility
soy 11S globulin
Soybean Proteins - chemistry
Soybean Proteins - metabolism
Soybeans
Structure-function relationships
sulfhydryl content
Surface properties
Thermal stability
Viscosity
water holding capacity
Zeta potential
sulfhydryl content
foaming capacity
low‐frequency magnetic field
rheological property
soy 11S globulin
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Abstract BACKGROUND Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the low‐frequency magnetic field (LF‐MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin. RESULTS Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water‐holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF‐MF treatment. The LF‐MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF‐MF modification time being 90 min. CONCLUSION LF‐MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant‐based proteins in the food industry. © 2024 Society of Chemical Industry.
AbstractList BACKGROUND: Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the low‐frequency magnetic field (LF‐MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin. RESULTS: Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water‐holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF‐MF treatment. The LF‐MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF‐MF modification time being 90 min. CONCLUSION: LF‐MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant‐based proteins in the food industry. © 2024 Society of Chemical Industry.
BACKGROUND Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the low‐frequency magnetic field (LF‐MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin. RESULTS Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water‐holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF‐MF treatment. The LF‐MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF‐MF modification time being 90 min. CONCLUSION LF‐MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant‐based proteins in the food industry. © 2024 Society of Chemical Industry.
BACKGROUNDSoy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the low‐frequency magnetic field (LF‐MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin.RESULTSCompared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water‐holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF‐MF treatment. The LF‐MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF‐MF modification time being 90 min.CONCLUSIONLF‐MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant‐based proteins in the food industry. © 2024 Society of Chemical Industry.
Soy 11S globulin has high thermal stability, limiting its application in the production of low-temperature gel foods. In this study, the low-frequency magnetic field (LF-MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin. Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water-holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF-MF treatment. The LF-MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF-MF modification time being 90 min. LF-MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant-based proteins in the food industry. © 2024 Society of Chemical Industry.
Soy 11S globulin has high thermal stability, limiting its application in the production of low-temperature gel foods. In this study, the low-frequency magnetic field (LF-MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin.BACKGROUNDSoy 11S globulin has high thermal stability, limiting its application in the production of low-temperature gel foods. In this study, the low-frequency magnetic field (LF-MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin.Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water-holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF-MF treatment. The LF-MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF-MF modification time being 90 min.RESULTSCompared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water-holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF-MF treatment. The LF-MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF-MF modification time being 90 min.LF-MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant-based proteins in the food industry. © 2024 Society of Chemical Industry.CONCLUSIONLF-MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant-based proteins in the food industry. © 2024 Society of Chemical Industry.
Author Yao, Peng‐Lei
Li, Yan‐ping
Kang, Zhuang‐Li
Xie, Jing‐jie
Ma, Han‐Jun
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Keywords sulfhydryl content
foaming capacity
low‐frequency magnetic field
rheological property
soy 11S globulin
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Snippet BACKGROUND Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the...
Soy 11S globulin has high thermal stability, limiting its application in the production of low-temperature gel foods. In this study, the low-frequency magnetic...
BACKGROUNDSoy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the...
BACKGROUND: Soy 11S globulin has high thermal stability, limiting its application in the production of low‐temperature gel foods. In this study, the...
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SubjectTerms agriculture
Disulfide bonds
disulfides
Foaming
foaming capacity
Food industry
gel strength
gels
Globulins
Globulins - chemistry
Globulins - metabolism
Glycine max - chemistry
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
low‐frequency magnetic field
Magnetic Fields
Magnetic properties
Physicochemical properties
Protein Conformation
Protein folding
Protein structure
Proteins
Rheological properties
rheological property
Rheology
Solubility
soy 11S globulin
Soybean Proteins - chemistry
Soybean Proteins - metabolism
Soybeans
Structure-function relationships
sulfhydryl content
Surface properties
Thermal stability
Viscosity
water holding capacity
Zeta potential
Title Effects of low‐frequency magnetic field on solubility, structural and functional properties of soy 11S globulin
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjsfa.13415
https://www.ncbi.nlm.nih.gov/pubmed/38415770
https://www.proquest.com/docview/3068993658
https://www.proquest.com/docview/2932940196
https://www.proquest.com/docview/3153621310
Volume 104
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