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

• Published in: Journal 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
• Language: English
• 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
• ISSN: 0022-5142; 1097-0010; 1097-0010
• DOI: 10.1002/jsfa.13415

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.