Gluten proteins are highly impacting the quality of various gluten-based products, and transglutaminases (TGs) are used to influence the protein cross-linking. In this study we monitored the interplay of “harsh” and “mild” gluten processing for dough mixing and pasta-like sheet production and TGs from a commercial and newly sourced bacteria (SB6). Despite the harshly separated gluten presenting strongly cross-linked proteins in the beginning of the mixing, similar levels of polymerization were achieved at the optimum mixing time but with differences in the secondary protein structure. TG addition increased polymerization in wheat doughs, possibly as a result of increased glutenin polymerization, while gliadins become more soluble with SB6. This enzyme also dramatically increased polymerization in mild gluten. These results show that an adequate investigation when using TGs and gluten from various origins is necessary to adequately predict the quality in various gluten-based products, thus, of great relevance to the food industry.

Industrial relevance

Currently, there is a mounting trend towards the modification of gluten proteins to improve technological features and functionality. In breadmaking, when weak flour (low protein content) is used or general stabilization is desired for technological purposes, additives can be used to stabilize the gluten protein matrix. The use of transglutaminase (TG) has grown in popularity as they promote specific cross-linking between residues of glutamine and lysine in proteins. Another way of improving dough functionality is by increasing the oxidation of disulfide groups by adding gluten which is a co-product of the starch industry. Industrial production of gluten includes the use of heating and shear forces, which may impact gluten dough-forming ability. Thus, increased understanding of the interplay of gluten processing and the impact of choice of the TG origin in gluten dough quality is highly applicable in food industry.

中文翻译：

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加工条件和转谷氨酰胺酶源可“驱动”小麦面筋面团的质量

面筋蛋白在很大程度上影响各种面筋产品的质量，转谷氨酰胺酶（TGs）用于影响蛋白质的交联。在这项研究中，我们监测了“搅和”和“温和”面筋加工在面团混合和面食类薄片生产以及来自商业和新来源细菌（SB6）的TGs之间的相互作用。尽管在混合开始时，面筋的分离度很强，但蛋白质却具有很强的交联性，但在最佳混合时间，聚合度却达到了相似的水平，但是二级蛋白质的结构却有所不同。TG的添加增加了小麦面团中的聚合，这可能是谷蛋白的聚合增加的结果，而麦醇溶蛋白则更易溶于SB6。该酶还显着增加了轻质面筋中的聚合。

行业相关性

当前，对面筋蛋白进行修饰以改善技术特征和功能性的趋势日益明显。在面包制作中，当使用弱面粉（低蛋白含量）或出于技术目的需要常规稳定化处理时，可以使用添加剂来稳定面筋蛋白基质。转谷氨酰胺酶（TG）的使用已日益普及，因为它们促进蛋白质中谷氨酰胺和赖氨酸残基之间的特定交联。改善面团功能的另一种方法是通过添加麸质增加二硫键的氧化，而麸质是淀粉工业的副产品。面筋的工业生产包括使用加热力和剪切力，这可能会影响面筋面团的形成能力。从而，