Processing conditions and transglutaminase sources to "drive" the wheat gluten dough quality

被引:10
作者
Ceresino, Elaine Berger [1 ]
Kuktaite, Ramune [1 ]
Hedenqvist, Mikael S. [3 ]
Sato, Helia Harumi [2 ]
Johansson, Eva [1 ]
机构
[1] Swedish Univ Agr Sci, Dept Plant Breeding, Box 101, SE-23053 Alnarp, Sweden
[2] Univ Estadual Campinas, Sch Food Engn, Dept Food Sci, Campinas, Brazil
[3] KTH Royal Inst Technol, Sch Engn Sci Chem Biotechnol & Hlth, Fibre & Polymer Technol, SE-10044 Stockholm, Sweden
关键词
Gluten separation; Transglutaminase; Polymerization; Protein-rich; Dough; Film; Crosslinking; MICROBIAL TRANSGLUTAMINASE; RHEOLOGICAL PROPERTIES; PROTEIN POLYMERIZATION; GLIADIN; GRAIN; FLOUR; IMPACT; FILMS; GLIADIN/GLUTENIN; FUNCTIONALITY;
D O I
10.1016/j.ifset.2020.102439
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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 Hour (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.
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页数:7
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