Effect of Non-Covalent Interactions on Arabinoxylan–Protein Cross-Linking and Gluten-Free Batter Stability
Ulrich Sukop, Katharina Feist, Katharina Hoefler, Stefano D’Amico, Mario Jekle, Regine Schoenlechner, Konrad J. Domig, Philipp L. Fuhrmann, Denisse Bender

TL;DR
This study explores how non-covalent interactions affect the stability of gluten-free batters made with maize arabinoxylans and proteins.
Contribution
The study reveals how different non-covalent forces influence the cross-linking and stability of gluten-free batter systems.
Findings
AX-based batters rely on H-bonds and electrostatic interactions for stability.
Enzymatic coupling strengthens AX–protein networks when H and electrostatic forces are present.
Gas retention in batters is influenced by the balance of non-covalent interactions.
Abstract
Maize arabinoxylans (AX) and proteins (maize gluten meal, MGM) can partially replace gluten in gluten-free (GF) breads by forming polymer networks. This study investigated how non-covalent interactions (hydrophobic, electrostatic, or hydrogen (H) forces) influenced viscoelasticity, gas retention and enzymatic AX–protein cross-linking in simplified GF model batters using two maize AX extracts (commercial MAX; xylanase-extracted M-XEAX). Batter stability strongly depended on AX structure and formulation type. MGM-only controls were mainly governed by hydrophobic and electrostatic forces, while AX-based batters relied primarily on H-bonds and electrostatic interactions. Combining MGM and AX increased batter stiffness, dominated by electrostatic and H-interactions. Enzymatic coupling reinforced the AX–protein network when both H and electrostatic forces were present, whereas hydrophobic…
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Taxonomy
TopicsFood composition and properties · Nanocomposite Films for Food Packaging · biodegradable polymer synthesis and properties
