在这项研究中,研究了基于纹理小麦蛋白(TWP)的肉类类似物在挤压过程中添加三聚磷酸钠的影响。制备了5个TWP(TWP-C0,TWP-C0.10,TWP-C0.25,TWP-C0.50和TWP-C0.75),0.10%,0.25%,0.50%,和0.75%,分别。通过确定TWP的纹理特性来分析TWP的纤维结构,纹理化程度,微观结构,和蛋白质键。当磷酸钠的浓度从0%增加到0.75%时,TWP中的纤维变得更规则和更细,毛孔更小,质构化程度从2.10±0.09增加到2.73±0.07,疏水键和二硫键断裂的增溶蛋白比例从2.06±0.14%和1.38±0.11%增加到3.42±0.12%和1.74±0.05%,分别。粒度的结果,可溶性氮含量,消化过程中样品的游离氨基酸表明,TWPs的崩解速率和蛋白质消化率随着三磷酸钠浓度的增加而增加。胃肠消化后,TWP-C0,TWP-C0.10,TWP-C0.25,TWP-C0.50和TWP-C0.75中释放的总游离氨基酸分别为391.5±2.2,403.9±1.5,430.0±3.6,473.8±2.9和485.3±5.73mg/10g消化物,分别。通过形成具有更解折叠的蛋白质结构和更多的疏水性基团暴露于酶的更精细的纤维结构,三磷酸钠可以改善TWP的蛋白质消化率。
In this study, the effects of adding sodium tripolyphosphate during the extrusion of textured wheat protein (TWP)-based meat analogs were investigated. Five TWPs (TWP-C0, TWP-C0.10, TWP-C0.25, TWP-C0.50, and TWP-C0.75) were prepared with sodium tripolyphosphate concentrations of 0%, 0.10%, 0.25%, 0.50%, and 0.75%, respectively. The fibrous structure of TWPs was analyzed by determining their textural properties, degree of texturization, microstructure, and protein bonds. When the concentration of sodium tripolyphosphate increased from 0% to 0.75%, the fibers in TWPs became more regular and finer with smaller pores, the degree of texturization increased from 2.10 ± 0.09 to 2.73 ± 0.07, and the proportions of solubilized protein from the breaking of hydrophobic bonds and disulfide bonds increased from 2.06 ± 0.14% and 1.38 ± 0.11% to 3.42 ± 0.12% and 1.74 ± 0.05%, respectively. The results of particle size, soluble nitrogen content, and free amino acids of samples during digestion indicated that the disintegration rate and protein digestibility of TWPs increased with the increase in the concentration of sodium tripolyphosphate. After gastrointestinal digestion, the total free amino acids released in TWP-C0, TWP-C0.10, TWP-C0.25, TWP-C0.50, and TWP-C0.75 were 391.5 ± 2.2, 403.9 ± 1.5, 430.0 ± 3.6, 473.8 ± 2.9 and 485.3 ± 5.73 mg/10 g digesta, respectively. Sodium tripolyphosphate may improve the protein digestibility of TWPs by forming a finer fibrous structure with a more unfolded protein structure and more hydrophobic groups being exposed to enzymes.