6 Characteristics of an Effective Collagen Powder

For the “collagen powder”, or more accurately, “Collagen Peptides” to actually work effectively; you need the following characteristics:

It has to be sourced from a reputable manufacturer,
It has to be safe for human use,
It has to be of impeccable quality,
It has to have evidence-based efficacy,
It has to have clinically proven bioavailability of at least 90%,
And most importantly, for collagen powder, peptides or hydrolysed collagen not to be just another protein powder, it has to have adequate amounts of targeted di-peptides and tri-peptides specifically for the purpose of building new collagen fibres.

1. Reputable Manufacturer

There are hundreds of suppliers for collagen peptides popping up across the world, each one offering better collagen than its competitors.

Lots of promises;

Small molecular weight molecules,
Sourced from “Pasture Raised” cattle,
Sourced from “Grass-fed Cows”,
Organic collagen,
Sustainable source,
No fillers were added,
Pure collagen powder,
GMP Manufacturing facility,
FDA Approved facility

and tens more claims and promises.

The best practice is to do some research and select one of the manufacturers with a proven reputation.

Or if you want to buy inexpensive collagen with lots of promises, send a request to the brand for legitimate (Verified) certification for each of their claims.

2. Safe for Human use.

This goes without saying, make sure your collagen comes from a reputable source. The top brand will be able to supply you with a “Human Safety Study” for their collagen peptides.

All collagen powders are derived from Animals, it is animal protein. The most popular and affordable collagen powders are derived from Bovine, mostly cow split hide.

The more expensive collagen powders are derived from fish skin or scale and in some cases both.

In the case of bovine collagen, you could ingest some of the following depending health of the animal, the feed of the animal and the possible medication and vaccination of the animals.

1. Herbicides,

2. Pesticides,

3. Hormones,

4. Antibiotics,
5. Other veterinary products,

And very important, it must be certified FREE from;

BSE (Bovine Spongiform Encephalopathy) and
TSE (Transmissible Spongiform Encephalopathy).

In the case of fish or marine collagen, you have to make sure the products were tested for heavy metal contamination and specifically mercury. Marine fish, especially the ones higher up in the food chain can have high levels of retained mercury.

Other considerations are microbial contamination like Salmonella or E. coli.

It is also important to check, if possible if the products were irradiated. This is normally done to extend shelf life after manufacturing. The process is not common for capsule or powdered collagen peptide products but it might be the case for liquid collagen products.

3. Quality

This is one of the main considerations in the manufacturing process.

High-quality source,
High-quality processing,
High-quality manufacturing,
GMP – Good Manufacturing Process,
Total Quality Management

Once again forms part of the reputable manufacturer selection.

4. Efficacy

And then the whole reason for your research, “Does the product work?”.

The only way to determine the efficacy of a product is through studies and human clinical trials.

How well were the collagen peptides absorbed, what is the bio-availability, and have the peptides been used as collagen fibre building blocks? Is there any clinical evidence of increased activity of fibroblast or osteoblast?

Ultimately, have the consumer experienced any improvement in skin, joint or bone condition? Was there any visible change in skin condition or wrinkles?

Consumers read about the benefits of collagen (Collagen peptides) but rarely understand that 90% of the benefits are not visible or you can’t necessarily feel or experience any gratification.

Most of the results take time, it builds up little by little over time. A few months later you stop using the supplement and then you experience the negative effect of using this important supplement.

43 Studies and Scientific evidence > Click Here

5. Proven Bioavailability & Bioactivity

It is very important that the collagen you use is both bioavailable and has efficient bioactivity.

Bioavailability in this case refers to the accessibility of the collagen peptide as a nutrient within the powder and the ability of the body to absorb the peptides into the bloodstream.

Bioactivity refers to the ability of a small molecule to modulate a biological function of a target cell and/or tissue. In this case, di-peptides and tri-peptides are specific to humans.

Bioactivity is what makes a nutrient beneficial.

6. Di-peptides and Tri-Peptides

As mentioned above, “Bio-activity is what makes the nutrient beneficial”.

The bioactive peptides of collagen are the Di-peptides and Tri-peptides.

It is therefore very important to use collagen peptide products with a high density of di-peptides and tripeptides for the best value for money and results,

The two most abundant dipeptides in collagen supplements are hydroxyproline-glycine (Hyp-Gly) and proline-hydroxyproline (Pro-Hyp), well-known for their bioactivity.

Evenly important is the easy-to-absorb, tripeptide format Gly-X-Y, where X and Y most commonly include proline, hydroxyproline and alanine.

References:

[1] Kleinnijenhuis, A.J., 2019. Non-targeted and targeted analysis of collagen hydrolysates during the course of digestion and absorption. Anal Bioanal Chem. 2019 Dec 24. doi: 10.1007/s00216-019-02323-x.

[2] Ohara, H., et al., 2010. Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts. The Journal of Dermatology, 37(4), 330–338. doi: 10.1111/j.1346-8138.2010.00827.x

[3] Asai, T. T. et al., 2019. Food-Derived Collagen Peptides, Prolyl-Hydroxyproline (Pro-Hyp), and Hydroxyprolyl-Glycine (Hyp-Gly) Enhance Growth of Primary Cultured Mouse Skin Fibroblast Using Fetal Bovine Serum Free from Hydroxyprolyl Peptide. International Journal of Molecular Sciences, 21(1), 229. doi: 10.3390/ijms21010229