Fuente: Foods - Revista científica (MDPI) Foods, Vol. 15, Pages 768: Effect of Non-Covalent Interactions on Arabinoxylan–Protein Cross-Linking and Gluten-Free Batter Stability
Foods doi: 10.3390/foods15040768
Authors:
Ulrich Sukop
Katharina Feist
Katharina Hoefler
Stefano D’Amico
Mario Jekle
Regine Schoenlechner
Konrad J. Domig
Philipp L. Fuhrmann
Denisse Bender

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 interactions partly hindered these associations. Changes in viscoelasticity (G′) did not fully align with gas retention behaviour. In MGM-containing batters, gas retention was predominantly governed by H and electrostatic interactions. AX-based batters showed extract-dependent responses: electrostatic or H-interactions hindered gas stabilisation in M-XEAX, while their suppression supported gas-holding in enzyme-treated MAX batters. AX-MGM systems generally showed reduced gas expansion, indicating the contribution of multiple non-covalent interactions. Overall, batter stability strongly depended on AX structure, MGM addition, the balance of non-covalent interactions and the resulting network strength.