Collagen ingestion and exercise
- Although bone collagen is responsive to feeding in the absence of exercise19, collagen in musculoskeletal tissue is non-responsive to feeding in the absence of exercise.20 Exercise is necessary to “switch-on” synthetic machinery in muscle and connective tissue 21, and may also increase the delivery of specific AAs when their availability is increased (i.e. after the consumption of protein sources), particularly in dense connective tissues which are otherwise poorly vascularised.22 Further, as it has been shown that proline is integrated into muscle collagen when dairy protein is ingested post exercise5, it is possible that protein to support muscle recovery/repair may be better consumed post exercise.
- A recent study has shown that serum obtained from individuals after the consumption of dietary collagen (gelatin) resulted in an increased collagen content, and improved tissue mechanics of an engineered ligament. Meanwhile, an in vitro arm of the same study illustrated an increased availability of collagen specific AAs within the blood, and an increase in a blood marker of collagen synthesis (Procollagen type I Intact N-Terminal) after collagen was consumed 1h prior to a 6-minute skipping exercise.17 This suggests that the increased availability of collagen specific AAs and/or peptides in combination with exercise may result in an increased collagen synthesis within connective tissue.
- Although gelatin (a partially hydrolysed form of collagen utilised predominantly in food manufacturing) has been utilised in formative research exploring the impact of collagen intake on the synthesis of collagen, it is not considered to be palatable in its raw form to consume mixed in water due to collagens gelling properties, and therefore alternative formulations may be better tolerated. Incorporation of gelatin into food sources or forms should not influence its AA availability.