Abstract
In this study, the deformation behavior of soybean protein isolate (SPI) xerogels cross-linked with different transglutaminase (TGase) concentrations was investigated. The gel properties of TGase cross-linked SPI were analyzed by rheology and texture. Results showed that 0.4% TGase completely promoted the intermolecular cross-linking, SPI molecules had more binding sites and α-helix content and less irregular curl structure. The presence of 0.4% TGase enhanced the water binding ability and thermal stability of SPI xerogel, and its denaturation temperature was up to 181.50 °C. The corresponding texture characteristics showed that hardness and elasticity were significantly increased by 182.90% and 25.00%, respectively. Results showed that SPI containing 0.4% TGase had the best 3D (three-dimension) shape change after hydration. However, excessive TGase (1.0% w/v) led to excessive lysine covalent cross-linking, which increases the porosity of the gel surface, causing the disrupted gel network. The research provides insights and new ideas for food-processing technology called 4D (four-dimension) food.
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