Enhanced pulse protein-proanthocyanidin interactions through electron beam irradiation

Area of Science:

• Food Science
• Protein Chemistry
• Biotechnology

Background:

• Proanthocyanidins (PA) are known to enhance pulse protein networks.
• The globular structure of pulse proteins limits the effectiveness of PA interactions.
• Electron beam irradiation (EBI) can modify protein structures to potentially improve these interactions.

Purpose of the Study:

• To investigate the effects of EBI on soy and pulse protein-PA interactions.
• To determine optimal EBI doses for enhancing protein-PA cross-linking.
• To evaluate changes in protein solubility, molecular weight, and thermal stability.

Main Methods:

• Soy, pea, faba, and lentil proteins were treated with EBI (0-10 kGy) in the presence of PA (25 mg/g protein).
• Protein solubility, surface hydrophobicity, molecular weight (Mw), and thermal stability were analyzed.
• Denaturation enthalpy was measured to confirm cross-linking extent.

Main Results:

• EBI at 2-5 kGy significantly enhanced protein-PA cross-linking, increasing complex Mw by 1.7-5.7 fold.
• Surface hydrophobicity decreased by 9-47% following EBI treatment.
• Faba proteins, with high proline content, exhibited the most extensive PA cross-linking, forming larger soluble complexes.

Conclusions:

• EBI is an effective method for improving proanthocyanidin-protein interactions in pulse proteins.
• Faba proteins show enhanced cross-linking with PA under EBI due to proline content and structural flexibility.
• This approach offers potential for modifying pulse protein functionality in food systems.