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Molecular regulation of rapeseed protein for improving its techno-functional properties.
Shao, Feng; Zhang, Yuanlong; Wan, Xia; Duan, Yuqing; Cai, Meihong; Hu, Kai; Zhang, Haihui.
Afiliación
  • Shao F; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
  • Zhang Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
  • Wan X; Oil Crops Research Institute, Chinese Academy of Agricultural Sciences, Wuhan 430062, China.
  • Duan Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Institute of Food Physical Processing, Jiangsu University, Zhenjiang 212013, China. Electronic address: dyq101@ujs.edu.cn.
  • Cai M; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
  • Hu K; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
  • Zhang H; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China. Electronic address: dyq101@ujs.edu.cn.
Int J Biol Macromol ; 275(Pt 1): 133441, 2024 Aug.
Article en En | MEDLINE | ID: mdl-38955302
ABSTRACT
To improve the techno-functional properties of rapeseed protein (RP), this work tried to regulate the molecular structure of RP via inducing the co-assembly of RP with zein and whey protein (WP). The results showed that WP and zein mainly regulate the folding process of RP through hydrophobic and disulfide bonds, thereby altering the structural conformation and forming stable complex RP (CRP). WP addition not only increased the number of surface charges and hydrophilicity of proteins, but also decreased their sizes, improved the water solubility, as well as the availability of active groups. These changes significantly increased the foaming capacity (from 60 % to 147 %) and in vitro gastric digestion rate (from 10 % to 60 %) of CRP. Besides, WP also contributed to the formation of gels and the regulation of their textural profiles. Comparatively, zein improved the hydrophobicity of CRP and balanced degree of intermolecular forces, which effectively increased the emulsifying activity index of CRP from 22 m2/g to 90 m2/g. Zein decreased the hardness, springiness and water-holding capacity of gel, but increased its gumminess and chewiness. Overall, both WP and zein effectively changed the structural conformation of RP, and improved its techno-functional properties, which provides an effective strategy to modify protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Solubilidad / Zeína / Brassica rapa / Interacciones Hidrofóbicas e Hidrofílicas / Proteína de Suero de Leche Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Solubilidad / Zeína / Brassica rapa / Interacciones Hidrofóbicas e Hidrofílicas / Proteína de Suero de Leche Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos