Enzymatic Hydrolysis of a Collagen Hydrolysate Enhances Postprandial Absorption Rate-A Randomized Controlled Trial.
Level 2 - randomized trial
Individual randomized crossover trial
PubMed 31086034 · doi:10.3390/nu11051064
What was done
A randomized, blinded, crossover trial evaluated the postprandial absorption of collagen in 10 healthy male subjects across three nonconsecutive days. Participants received 35 g of enzymatically hydrolyzed collagen protein (EHC), 35 g of non-enzymatically hydrolyzed collagen protein (NC), or placebo (250 mL water). Blood samples were drawn before and up to 240 minutes following ingestion, and the blood metabolome was characterized using nuclear magnetic resonance (NMR)-based metabolomics.
What was found
A significant increase in plasma concentrations of nearly all amino acids occurred over 240 minutes for both EHC and NC. The absorption rate and bioavailability of glycine, proline, and hydroxyproline were significantly higher following EHC ingestion compared to NC (p < 0.05). Specific numerical values for pharmacokinetic metrics were not reported in the abstract.
Why it matters
Enzymatic pre-hydrolysis enhances the rate of absorption and total bioavailability of key collagen-derived amino acids. This indicates processing method directly influences circulating levels of glycine, proline, and hydroxyproline after oral ingestion.
Limits
The study had a very small sample size (n = 10) and included only healthy male participants. It evaluated acute postprandial amino acid kinetics up to 240 minutes without assessing clinical outcomes, joint health, or tissue incorporation.
Cited by
- supports Hydrolyzed collagen powder contains a significantly higher concentration of proline, glycine, and hydroxyproline than steak.