NMR-Based Quantification of Collagen Content in Protein Hydrolysates

Area of Science:

• Food Chemistry
• Analytical Chemistry
• Biotechnology

Background:

• Bioactive peptides in functional foods and supplements derive their activity from specific amino acid sequences.
• Poultry side streams are a source of collagenous peptides with potential health benefits, including blood pressure and glucose management.
• Accurate quantification of collagen content is crucial for assessing the bioactivity and quality of these peptides.

Purpose of the Study:

• To establish and validate a quantitative 1H NMR (qHNMR) method for hydroxyproline quantification in poultry hydrolysates.
• To use hydroxyproline as a specific marker for collagen content.
• To overcome limitations of conventional amino acid analysis for complex peptide mixtures.

Main Methods:

• Investigated collagenous peptides derived from poultry side streams.
• Employed quantitative 1H NMR (qHNMR) for hydroxyproline quantification.
• Utilized quantum mechanics (QM)-based 1H iterative functionalized spin analysis (HifSA) to study the effect of acidic solvents and improve accuracy.

Main Results:

• Successfully established and validated a qHNMR method for hydroxyproline quantification.
• Demonstrated the high accuracy, specificity, reproducibility, and speed of qHNMR.
• QM-qHNMR analysis revealed limitations of conventional integration methods, showing superior accuracy and specificity.

Conclusions:

• The developed QM-qHNMR method provides a robust tool for precise collagen quantification in poultry hydrolysates.
• This method enhances the characterization of bioactive peptides from food industry byproducts.
• Accurate collagen measurement using qHNMR supports the development of functional foods and dietary supplements.