2022
DOI: 10.1016/j.foodchem.2022.133296
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Effects of phosphorylation pretreatment and subsequent transglutaminase cross-linking on physicochemical, structural, and gel properties of wheat gluten

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Cited by 36 publications
(9 citation statements)
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“…The surface structures of freeze-fractured SPI gels under optimum gelation conditions are presented in Figure 5a,b. The three-dimensional structure of the SPI gel made in the presence of both TGase and salt is denser and more uniform, compared to the SPI gel made with TGase or salt alone, regardless of protein concentration which is confirmed by Zou et al (2022), stating more homogeneous and denser threedimensional network structure of gel using TGase cross-linking of wheat gluten (Zou et al, 2022). Also, adding CaCl 2 contributed to the formation of a compact gel phase.…”
Section: Microstructurementioning
confidence: 78%
“…The surface structures of freeze-fractured SPI gels under optimum gelation conditions are presented in Figure 5a,b. The three-dimensional structure of the SPI gel made in the presence of both TGase and salt is denser and more uniform, compared to the SPI gel made with TGase or salt alone, regardless of protein concentration which is confirmed by Zou et al (2022), stating more homogeneous and denser threedimensional network structure of gel using TGase cross-linking of wheat gluten (Zou et al, 2022). Also, adding CaCl 2 contributed to the formation of a compact gel phase.…”
Section: Microstructurementioning
confidence: 78%
“…As the cross‐linking time increased, the number of pores gradually decreased, the surface gradually became smooth and the gel network structure was relatively tight. On the one hand, the TG cross‐linking reaction can promote the formation of protein aggregates, which were compact and uniform gel microstructures (Zou et al., 2022), on the other hand, oil droplets could be used as active fillers to be embedded or integrated into the gel network, resulting in the improvement of gel strength and gel‐like rheological properties.…”
Section: Resultsmentioning
confidence: 99%
“…Under high-moisture extrusion conditions, the low-protein content can also achieve fibrosis by interacting with wheat gluten proteins. This is due to the fact that wheat gluten protein has a stronger ability to unwind its molecular chains and easily bind to other molecules compared with other proteins and can generate solid disulfide bonds, which in turn promote protein rearrangement and the formation of fibrous structures with a weblike structure [ 19 ]. Meanwhile, studies have been reported on wheat gluten in the field of extrusion histochemistry, suggesting that the addition of gluten improves the fibrous reticulation of the protein and helps to improve the quality of the extruded product [ 18 , 20 , 21 ].…”
Section: Types Of Plant-based Protein Products As Alternatives To Ani...mentioning
confidence: 99%