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Published on: October 4, 2012
Ultrafiltration to fractionate wheat polypeptides
S Berot1, Y Popineau, J P Compoint
1Unité de Biochimie et Technologie des Protéines, INRA, Nantes, France.
Summary
Ultrafiltration effectively separated wheat gliadin polypeptides based on hydrophobicity. Hydrophobic fractions enhanced foaming properties, while hydrophilic fractions did not, offering a novel method for functional ingredient development.
Area of Science:
- Food Science
- Biochemistry
- Separation Science
Background:
- Wheat gliadins are complex proteins yielding various polypeptides upon hydrolysis.
- Fractionating these polypeptides is crucial for understanding and utilizing their functional properties, such as foaming.
Purpose of the Study:
- To investigate the efficacy of ultrafiltration for fractionating wheat gliadin hydrolysates.
- To characterize the separated polypeptide fractions based on their physicochemical properties and foaming capabilities.
Main Methods:
- Limited chymotryptic hydrolysis of wheat gliadins.
- Ultrafiltration using inorganic ZrO2-based membranes at acidic pH.
- Characterization of permeate and retentate fractions using chromatography and foaming assays.
Main Results:
- Ultrafiltration successfully separated polypeptides into hydrophilic (permeate) and hydrophobic (retentate) fractions.
- Permeate fractions were rich in hydrophilic, poorly charged polypeptides (84-90%).
- Retentate fractions contained 75-88% hydrophobic polypeptides, exhibiting significantly enhanced foaming properties compared to whole hydrolysates.
Conclusions:
- Ultrafiltration provides an effective method for fractionating wheat gliadin hydrolysates based on polypeptide hydrophobicity.
- The hydrophobic polypeptide-rich retentate fractions demonstrate superior foaming capabilities, suggesting potential applications in food formulations.
