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Impact of gluten separation process and transglutaminase source on gluten based dough properties

Ceresino, Elaine Berger, Kuktaite, Ramune, Sato, Hélia Harumi, Hedenqvist, Mikael S., Johansson, Eva
Food hydrocolloids 2019 v.87 pp. 661-669
crosslinking, dough, dough development, dough quality, hydrocolloids, mixing, polymerization, protein secondary structure, protein-glutamine gamma-glutamyltransferase, solubility, wheat gluten
This study evaluated the effect of the wheat gluten (WG) separation process and transglutaminase (TG) microbial source on WG dough quality, and opportunities to use these factors to tailor dough quality. Two types of gluten (harshly and mildly separated), two types of TG (commercial and novel SB6), and three TG concentrations were evaluated for effects on dough mixing properties, protein structure and solubility. Mildly separated gluten improved dough development parameters, resulting into higher values of most compared with harshly separated gluten. Despite more strongly cross-linked proteins being found in the harshly separated gluten, both gluten types showed similar levels of cross-linking at optimum mixing time, although differences in the secondary protein structure were indicated. Thus, disulfide-sulfhydryl exchange reactions were found to be promoted by mixing, although restrictions on establishment of new bonds because of prior cross-links in the material were clearly indicated. Degree of polymerization in doughs made from mildly separated gluten increased to varying extents with TG addition depending on TG source and concentration. Thus, for the first time, we show that an appropriate combination of WG separation procedure and TG source can be used to tailor gluten dough end-use properties.