Interaction mechanisms of condensed tannins (proanthocyanidins) with wheat gluten proteins. Academic Article

abstract

• Proanthocyanidins (PA) crosslink wheat gluten, increasing its polymer size and strength. However, mechanisms behind these interactions are unknown. This study used PA of different MW profiles (mean degree of polymerization 8.3 and 19.5) to investigate how PA polymerize gluten. The higher MW PA had greater binding affinity for both glutenins and gliadins than lower MW PA, whereas both PA precipitated glutenins more efficiently than gliadins. The PA preferentially bound the largest of the protein fractions available: high MW glutenin subunits (HMW-GS) over low MW-GS, and -gliadins over - and -gliadins. Furthermore, within the HMW-GS, PA bound more of the larger x-type than the smaller y-type. Proanthocyanidins reduced gluten solubility in urea and decreased surface hydrophobicity of glutenins, but not gliadins. The PA appear to preferentially crosslink HMW-GS via hydrophobic interactions and hydrogen bonding, whereas their interaction with gliadins is dominated by hydrogen bonding and is relatively weaker.

authors

• Awika, Joseph

published proceedings

• Food Chem

altmetric score

• 0.25

author list (cited authors)

• Girard, A. L., Bean, S. R., Tilley, M., Adrianos, S. L., & Awika, J. M.

citation count

• 56

complete list of authors

• Girard, Audrey L||Bean, Scott R||Tilley, Michael||Adrianos, Sherry L||Awika, Joseph M

publication date

• January 2018

publisher

• Elsevier  Publisher

published in

• Food Chemistry  Journal

keywords

• Condensed Tannins
• Gliadin
• Gliadins
• Glutenins
• Glutens
• Molecular Weight
• Noncovalent Gluten Crosslinking
• Proanthocyanidins
• Solubility
• Triticum
• Urea

Digital Object Identifier (DOI)

• 10.1016/j.foodchem.2017.11.054

start page

• 1154

end page

• 1162

volume

• 245

URL

• http://dx.doi.org/10.1016/j.foodchem.2017.11.054