Processing Enhances Coix Seed Prolamins Structure and Releases Functional Peptides after Digestion: In Silico and In...

Area of Science:

• Food Science
• Biochemistry
• Nutraceuticals

Background:

• Dipeptidyl peptidase-IV (DPP-IV) is a crucial enzyme targeted for type 2 diabetes mellitus management.
• Coix seed prolamins (CSP) are a potential source of bioactive peptides, but their DPP-IV inhibitory capacity is unexplored.

Purpose of the Study:

• To investigate the potential of coix seed prolamins (CSP) to yield DPP-IV inhibitory peptides.
• To assess the impact of thermal processing on CSP structure and the subsequent release of bioactive peptides.

Main Methods:

• In silico digestion of CSP to predict peptide bioactivity, absorption, transport, toxicity, and allergenicity.
• Analysis of amino acid composition and structural properties of CSP before and after thermal processing.
• Assessment of DPP-IV inhibitory activity of peptides derived from processed and unprocessed CSP.

Main Results:

• In silico analysis predicted 47 non-toxic bioactive peptides from CSP, with 64.58% showing potential DPP-IV inhibitory activity.
• Thermal processing altered CSP's amino acid profile and shifted its structure from ordered to disordered.
• Processing significantly increased peptide content (19.89-30.91%) and DPP-IV inhibitory activity (36.84-42.02%) of derived peptides.

Conclusions:

• Thermal processing enhances the release of DPP-IV inhibitory peptides from coix seed prolamins.
• Processing modifies CSP structure, increasing bioactive peptide yield and inhibitory potential.
• Findings support the development of coix seed-derived bioactive peptides for type 2 diabetes management and advanced coix seed processing.