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pH-regulated Tannic acid and soybean protein isolate adhesive for enhanced performance in plant-based meat analogues.
Xue, Zixi; Zhang, Minghao; Wang, Junting; Wang, Shengnan; Han, Shuyin; Huang, Xueying; Liu, He.
Afiliación
  • Xue Z; College of Food Science and Technology, Bohai University, Jinzhou 121013, China.
  • Zhang M; College of Food Science and Technology, Bohai University, Jinzhou 121013, China.
  • Wang J; College of Food Science and Technology, Bohai University, Jinzhou 121013, China.
  • Wang S; College of Food Science and Technology, Bohai University, Jinzhou 121013, China; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou 121013, China. Electronic address: wsnname@163.com.
  • Han S; College of Food Science and Technology, Bohai University, Jinzhou 121013, China.
  • Huang X; College of Food Science and Technology, Bohai University, Jinzhou 121013, China.
  • Liu H; College of Food Science and Technology, Bohai University, Jinzhou 121013, China; Grain and Cereal Food Bio-efficient Transformation Engineering Research Center of Liaoning Province, Jinzhou 121013, China.
Food Res Int ; 185: 114289, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38658073
ABSTRACT
A food adhesive comprising tannic acid (TA) and soybean protein isolate (SPI) was developed to establish a cohesive bond between soy protein gel and simulated fat. The impact of varying TA concentrations and pH levels on the adhesive's rheology, thermal stability, chemical structure, and tensile strength were investigated. Rheological results revealed a gradual decrease in adhesive viscosity with increasing TA content. Differential scanning calorimetry (DSC) and thermal gravimetric (TG) results indicated that the stability of the adhesive improved with higher TA concentrations, reaching its peak at 0.50% TA addition. The incorporation of TA resulted in the cross-linking of amino group in unfolded SPI molecules, forming a mesh structure. However, under alkaline conditions (pH 9), adhesive viscosity and stability increased compared to the original pH. This shift was due to the disruption of the SPI colloidal charge structure, an increase in the stretching of functional groups, further unfolding of the structure, and an enhanced binding of SPI to TA. Under the initial pH conditions, SPI reacted with TA's active site to form covalent crosslinked networks and hydrogen bonds. In alkaline condition, beyond hydrogen and ionic bonding, the catechol structure was oxidized, forming an ortho-quinone that crosslinked SPI and created a denser structure. Tensile strength measurements and freeze-thaw experiments revealed that the adhesive exhibited maximum tensile strength and optimal adhesion with 0.75% TA at pH 9, providing the best overall performance. This study provides a new formulation and approach for developing plant-based meat analogues adhesives.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Reología / Taninos / Resistencia a la Tracción / Proteínas de Soja / Polifenoles Idioma: En Revista: Food Res Int Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Canadá
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Reología / Taninos / Resistencia a la Tracción / Proteínas de Soja / Polifenoles Idioma: En Revista: Food Res Int Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Canadá