# Effect of Non-Covalent Interactions on Arabinoxylan–Protein Cross-Linking and Gluten-Free Batter Stability

**Authors:** Ulrich Sukop, Katharina Feist, Katharina Hoefler, Stefano D’Amico, Mario Jekle, Regine Schoenlechner, Konrad J. Domig, Philipp L. Fuhrmann, Denisse Bender

PMC · DOI: 10.3390/foods15040768 · 2026-02-20

## 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.

## Key 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 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.

## Linked entities

- **Proteins:** Muc5ac (mucin 5, subtypes A and C, tracheobronchial/gastric)
- **Chemicals:** AX (PubChem CID 33613)

## Full-text entities

- **Diseases:** injury to (MESH:D014947)
- **Chemicals:** H (MESH:D006859), AX (MESH:C085118), sucrose (MESH:D013395), arabinose (MESH:D001089), xylose (MESH:D014994), Urea (MESH:D014508), starch (MESH:D013213), M-XEAX-MGM (-), dextran (MESH:D003911), SDS (MESH:D012967), Water (MESH:D014867), silicone oil (MESH:D012827), ferulic acid (MESH:C004999), phenolic acid (MESH:C017616), polysaccharide (MESH:D011134), polymer (MESH:D011108), NaCl (MESH:D012965)
- **Species:** Homo sapiens (human, species) [taxon 9606], Leuconostoc mesenteroides (species) [taxon 1245], Aspergillus niger (species) [taxon 5061], Saccharomyces cerevisiae (baker's yeast, species) [taxon 4932]

## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12939721/full.md

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Source: https://tomesphere.com/paper/PMC12939721