Collagen as a nutritional supplement is a billion-dollar industry. All this information often gives rise to many collagen myths.

Let’s debunk some common collagen myths!

Myth #1: COLLAGEN IS NOT A GOOD PROTEIN SOURCE, ESPECIALLY FOR SPORTS NUTRITION

Two decades ago, our focus was on combating malnutrition and prolonging life expectancy. 

We achieved this by promoting the consumption of proteins that could provide all the needed essential amino acids. 

Collagen displays a low essential amino acid profile. As such it was viewed as a less than ideal protein source. 

Nowadays, this focus has shifted significantly.

We now focus more on regulating food metabolism for optimal long-term health benefits and addressing specific needs posed by ageing and exercise.

When collagen is consumed in the form of bioactive collagen peptides, the metabolism of target cells is stimulated more effectively.

The result?

More effective production of matrix proteins in both normal and healing collagen-rich tissues such as bones, tendons, ligaments, skin & cartilage. 

Conclusion: Collagen is an excellent protein supplement.

Myth #2: CERTAIN COLLAGEN TYPES ARE BETTER THAN OTHERS

To date, there are over 28 types of known collagen. They are numbered in the order they were discovered. The most common types on the market are Type I & II. 

Type I: Makes up 90% of the body’s collagen. Found in our bones, ligaments, tendons, skin & fibrous cartilage.

Type II: Found in our hyaline cartilage. Most commonly, in our ribs, nose, larynx and trachea.

Collagen is broken down into the needed bioactive collagen peptide in the body, regardless of the original collagen type. 

Conclusion: There is no difference. 

Myth #3: BIOACTIVE COLLAGEN PEPTIDES DO NOT SURVIVE ENZYMATIC DIGESTION 

Body bioavailability depends on two factors: enzymatic digestion & gut absorption.

Enzymatic digestion. 

Does enzymatic digestion destroy bioactive collagen peptides?

The short answer. No. 

Collagen peptides are remarkably rich in proline – 25% of total collagen peptides is proline. 

So, why is proline unique? 

Proline when compared to other amino acids, have stronger peptide bonds. This makes it harder for enzymes to break them down.

Absorption

Collagen peptides have a unique peptide chain structure which makes them narrower & stiffer than globular proteins (helix-shaped).

This needle-like structure appears to allow for easier absorption across the gut barrier even when not completely broken down into amino acids. 

Recent evidence shows that high-molecular-weight peptides and even small proteins can be absorbed to an extent. 

10% of bioactive collagen peptides remains intact after digestion, making them more bioavailable for absorption and the stimulation of connective tissue cell metabolism. 

The other 90% is digested into amino acids. As we all know, are the building blocks of protein in our body.

Conclusion: Bioactive collagen peptides may have higher bioavailability in the body than globular proteins.
Even after the digestive process.