Structural consequences of the interaction of puroindolines with gluten proteins

• Published in: Food chemistry 2018-07, Vol.253, p.255-261
• Main Authors: Quayson, Enoch T., Marti, Alessandra, Morris, Craig F., Marengo, Mauro, Bonomi, Francesco, Seetharaman, Koushik, Iametti, Stefania
• Format: Article
• Language: English
• Subjects: Gluten aggregation; Kernel texture; Protein thiols; Puroindoline proteins
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2018.01.146

•PINs affect interactions among gluten proteins in wheat flour.•Absence of PINs enhances hydrophobic interactions.•PIN-gluten proteins interactions may occur prior to mixing. The effect of puroindolines (PINs) on structural characteristics of wheat proteins was investigated in Triticum turgidum ssp. durum (cv. Svevo) and Triticum aestivum (cv. Alpowa) and in their respective derivatives in which PIN genes were expressed (Soft Svevo) or the distal end of the short arm of chromosome 5D was deleted and PINs were not expressed (Hard Alpowa). The presence of PINs decreased the amount of cold-SDS extractable proteins and the accessibility of protein thiols to specific reagents, but resulted in facilitated solvation of gluten proteins, as detected by tryptophan fluorescence measurements carried out on minimally mixed flour/water mixtures. We propose that PINs and gluten proteins are interacting in the grain or flour prior to mixing. Hydrophobic interactions between PINs and some of the gluten proteins modify the pattern of interactions among gluten proteins, thus providing an additional mechanistic rationale for the effects of PINs on kernel hardness.