Development and characterization of adhesives constructed by soy protein isolate and tea polyphenols for enhanced tensile strength in plant-protein meat applications.

The study aimed to evaluate a food adhesive developed using tea polyphenols (TPs) with soybean protein isolate (SPI) to create a cohesive bond between soy protein gel and simulated fat. Upon the addition of 5.0 % TPs, significant increases in viscosity, thermal stability, and crystallinity were noted in adhesives, suggesting the formation of a cohesive network. Furthermore, TPs effectively enhanced adhesion strength, with the optimal addition being 5.0 %. This enhancement can be attributed to hydrogen bonding, hydrophobic and electrostatic interactions between TPs and SPI molecules. TPs induced a greater expansion of the protein structure, exposing numerous buried hydrophobic groups to a more hydrophilic and polar environment. However, excessive TPs were found to diminish adhesion strength. This can be attributed to enhanced reactions between TPs and SPI, where high molecular weight SPI-TPs cooperatively aggregate to form agglomerates that eventually precipitated, rendering the adhesive network inhomogeneous, less stable, and more prone to disruption.

pH-regulated Tannic acid and soybean protein isolate adhesive for enhanced performance in plant-based meat analogues.

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.