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Investigating the impact of ultrasound-assisted treatment on the crafting of mulberry leaf protein and whey isolate complex: A comprehensive analysis of structure and functionality.
Wang, Xipeng; Wang, Cunfang; Ma, Mengjia; Li, Zhenghao; Zhang, Xiaoning; Jiang, Hua; Yuan, Cunzhong.
Afiliação
  • Wang X; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: 894228055@qq.com.
  • Wang C; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: cunfangwang@163.com.
  • Ma M; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: aa665_0525@163.com.
  • Li Z; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: lzh08240034@163.com.
  • Zhang X; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: xiaoningzhang@126.com.
  • Jiang H; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Science), Jinan 250353, China. Electronic address: jhmengyou@163.com.
  • Yuan C; Shenzhen Research Institute of Shandong University, Shenzhen 518057, China. Electronic address: yuancunzhong@sdu.edu.cn.
Ultrason Sonochem ; 108: 106983, 2024 Aug.
Article em En | MEDLINE | ID: mdl-39002225
ABSTRACT
Mulberry leaf protein (MLP) is a nutrient-rich protein, but its applicability is limited because of its poor solubility. To address this issue, this study combines MLP with whey protein isolates (WPI), known for the high nutritional value, and subsequently forms composite protein nanoparticles using the ultrasound-assisted pH shifting method. Microscopic observation and SDS-PAGE confirmed the binding between these two proteins. Fluorescence spectra and Fourier Transform infrared spectroscopy (FTIR) analysis supported the involvement of electrostatic interactions, hydrophobic attractions, and hydrogen bonding in the formation of stable complex nanoparticles. The interactions between the proteins became stronger after ultrasound-assisted pH-shifting treatment. Solubility, emulsification capacity, foaming, and antioxidant activity, among other indicators, demonstrate that the prepared composite nanoparticles exhibit favorable functional properties. The study successfully illustrates the creation of protein-based complex nanoparticles through the ultrasound-assisted pH shifting method, with potential applications in the delivery of bioactive compounds.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Folhas de Planta / Morus / Proteínas do Soro do Leite Idioma: En Revista: Ultrason Sonochem Assunto da revista: DIAGNOSTICO POR IMAGEM Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Folhas de Planta / Morus / Proteínas do Soro do Leite Idioma: En Revista: Ultrason Sonochem Assunto da revista: DIAGNOSTICO POR IMAGEM Ano de publicação: 2024 Tipo de documento: Article
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