Lipid-Induced Oxidative Modifications Decrease the Bioactivities of Collagen Hydrolysates from Fish Skin: The...

Area of Science:

• Biochemistry
• Food Science

Background:

• Collagen peptides possess valuable bioactivities like antioxidation and ACE inhibition.
• Oxidative deterioration during storage diminishes these bioactivities.
• The degradation pathways of bioactive peptides during oxidation are not well understood.

Purpose of the Study:

• To investigate the oxidative levels and bioactivities of collagen peptides during lipid-accelerated oxidative storage.
• To elucidate the dynamic changes in collagen peptide oxidation and their impact on bioactivity.
• To identify specific amino acids susceptible to oxidation and their modification types.

Main Methods:

• Inducing oxidation in collagen peptides using lipids.
• Monitoring oxidative markers such as carbonyl content, Schiff base, and dityrosine.
• Assessing bioactivities including antioxidation and Angiotensin-Converting Enzyme (ACE) inhibition.
• Performing amino acid and proteomic analyses to identify oxidized residues.

Main Results:

• Collagen peptide oxidation occurred in three distinct stages.
• Early-stage oxidation (increased carbonyl content) strongly correlated with decreased antioxidation and ACE inhibition.
• Later-stage oxidation (increased Schiff base and dityrosine) also correlated with reduced bioactivities.
• Methionine, Lysine, and Arginine were identified as oxidation-susceptible amino acids.

Conclusions:

• Oxidative modifications dynamically alter collagen peptide bioactivities.
• Understanding these oxidative changes is crucial for preserving peptide function during storage.
• This study provides insights into the specific oxidative modifications affecting collagen peptide bioactivity.