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Effects of low-frequency magnetic field on solubility, structural and functional properties of soy 11S globulin.
Kang, Zhuang-Li; Yao, Peng-Lei; Xie, Jing-Jie; Li, Yan-Ping; Ma, Han-Jun.
Affiliation
  • Kang ZL; School of Tourism and Cuisine, Industrial Engineering Center for Huaiyang Cuisin of Jiangsu Province, Yangzhou University, Yangzhou, China.
  • Yao PL; School of Food Science, Henan Institute of Science and Technology, Xinxiang, China.
  • Xie JJ; Key Laboratory of Chinese Cuisine Intangible Cultural Heritage Technology Inheritance, Ministry of Culture and Tourism, Yangzhou, China.
  • Li YP; School of Food Science, Henan Institute of Science and Technology, Xinxiang, China.
  • Ma HJ; School of Food Science, Henan Institute of Science and Technology, Xinxiang, China.
J Sci Food Agric ; 104(10): 5944-5954, 2024 Aug 15.
Article in En | MEDLINE | ID: mdl-38415770
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Rheology / Solubility / Glycine max / Soybean Proteins / Hydrophobic and Hydrophilic Interactions / Magnetic Fields / Globulins Language: En Journal: J Sci Food Agric Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Rheology / Solubility / Glycine max / Soybean Proteins / Hydrophobic and Hydrophilic Interactions / Magnetic Fields / Globulins Language: En Journal: J Sci Food Agric Year: 2024 Document type: Article