# NMR-Based Quantification of Collagen Content in Protein Hydrolysates

## TL;DR

This study developed a new NMR method to accurately measure collagen content in protein hydrolysates from poultry.

## Contribution

A validated qHNMR method using hydroxyproline as a marker for collagen content is introduced.

## Key findings

- qHNMR provides rapid, accurate, and reproducible quantification of hydroxyproline.
- QM-qHNMR outperforms conventional integration in accuracy and specificity.
- Acidic solvents' effects were analyzed using HifSA to improve method reliability.

## Abstract

Certain functional
food and dietary supplement ingredients contain
bioactive peptides whose bioactivity is determined by their chain
length, composition, and specific sequence of the amino acids. This
study investigated collagenous peptides from the valorization of poultry
side streams, which, for example, have inhibitory activities against
therapeutic targets for the management of blood pressure and blood
glucose. To overcome the specificity challenges of conventional amino
acid analysis, the aim was to establish and validate a quantitative 1H NMR (qHNMR) method for the quantification of hydroxyproline
as a marker of collagen content in poultry hydrolysates. Indeed, qHNMR
provides a rapid structure-specific quantification, and it is highly
informative, reproducible, and accurate. The effect of different acidic
solvents was investigated using quantum mechanics (QM)-based 1H iterative functionalized spin analysis (HifSA). Comparison
of conventional integration (int-) with QM-qHNMR revealed limitations
of the former approach and highlighted the increased accuracy and
specificity of QM-qHNMR.