Gluten proteins: Enzymatic modification, functional and therapeutic properties

Area of Science:

• Biochemistry
• Food Science
• Pharmacology

Background:

• Gluten proteins possess complex covalent network structures.
• Protease inhibitors can influence gluten's functional and technological properties.
• Allergic peptide sequences in gluten may be depleted enzymatically.

Purpose of the Study:

• To explore the multifunctional therapeutic effects of gluten proteins.
• To investigate how covalent network structures impact gluten's properties.
• To assess the potential of enzymatic modification for enhanced gluten functionalities.

Main Methods:

• Enzymatic digestion of gluten proteins using proteolytic enzymes.
• Analysis of structural changes in gluten networks.
• Evaluation of functional properties like gelatinization, gelation, and pasting.
• Assessment of bioactive peptide generation and their properties.

Main Results:

• Enzymatic treatment can deplete allergenic peptide sequences.
• Modified gluten yields active peptides with osmoregulation and surface activity.
• Enhanced bioactive surfaces, gelatinization, gelation, and pasting properties observed.
• Therapeutic activities include immunoregulatory, antithrombin, and opioidal effects.

Conclusions:

• Gluten modification via enzymatic processes enhances technological and therapeutic applications.
• Active peptides derived from gluten show potential in managing free radicals, diabetes, and cardiovascular diseases.
• Further research into gluten's bioactive peptides can unlock novel health and technological solutions.