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Interaction between cereal β-glucan and proteins in solution and at interfaces.

Claudia Zielke1, Yi Lu1, Romane Poinsot1

  • 1Food Technology, Engineering and Nutrition, Faculty of Engineering LTH, Lund University, PO Box 124, S-221 00 Lund, Sweden.

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Summary

Cereal beta-glucan (β-glucan) interacts with proteins like gliadin and whey protein, forming aggregates at low pH. These interactions, influenced by protein type and ratio, are crucial for understanding β-glucan

Keywords:
Asymmetric flow field-flow fractionation (AF4)Differential refractive index (dRI)Electrostatic interactionEllipsometryGliadinMulti-angle light scattering (MALS)Natural phosphatePolysaccharideTransmissionWhey protein (WP)

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Area of Science:

  • Food science and nutrition
  • Biochemistry
  • Dietary fiber research

Background:

  • Cereal beta-glucan (β-glucan) is recognized for health benefits, including cholesterol reduction and decreased heart disease risk.
  • The physiological effects of β-glucan are linked to its dissolution and aggregation during digestion.
  • Proteins may influence β-glucan's aggregation behavior and the formation of viscous slurries.

Purpose of the Study:

  • To investigate the interaction and aggregation behavior of a β-glucan isolate (OBC90) with gliadin and whey protein.
  • To examine the influence of pH, protein/β-glucan ratio, and interfaces on these interactions.
  • To elucidate the role of electrostatic interactions in β-glucan-protein aggregation.

Main Methods:

  • Solution-based studies of β-glucan and protein mixtures.
  • Investigation of aggregation kinetics under varying pH and protein/β-glucan ratios.
  • Analysis of interactions at interfaces.

Main Results:

  • Aggregates formed at low pH, with composition dependent on the protein type.
  • Phosphate presence in β-glucan contributed to a net negative charge at pH ≤ 4.
  • Evidence suggests electrostatic interactions are key to β-glucan and protein aggregation.

Conclusions:

  • The interaction between cereal β-glucan and proteins is pH-dependent, leading to aggregate formation.
  • Protein type significantly impacts the characteristics of the formed aggregates.
  • Electrostatic interactions play a critical role in mediating the aggregation of β-glucan with proteins during digestion.