“Can you cook with collagen?”
We get asked this question a lot, and we love answering it, why? Because it really adds extra credit where credit is due for the durability and flexibility of collagen protein peptides. So, to answer that question in short, yes you can cook with our collagen protein, and here is why…
I thought protein denatured when heated?
Yes, it can, however, there is more to it than that. Protein as we have spoken about in detail in a few of our recent articles is comprised of amino acids, aligned in a formation, like that of a stranded nature that provides the building blocks to areas of the body that require growth, recovery, and function. Dietary protein therefore as a whole is essential for life. That being said, protein can be fragile in design, when it is heated, even to just the temperature of our own body it starts to lose grip on its structural integrity.
To better picture this, imagine a small spring tightly bound, apply some heat and it starts to unravel and depending on the heat level applied, straightens out and doesn’t hold that tightly bound structure anymore. The same can happen with proteins, many denaturing assets can denature the hydrogen bonds of proteins, these include:
- Heavy Metals .
- Acids and bases .
- Heat .
- Alcohol .
- Reducing agents (although these are often intentionally used to cleave the bonds between cysteine amino acids in protein).
How does the denaturing process work?
The denaturing of protein is actually a natural process, it is actually happening in our gut when we eat protein! We mentioned above that acids and bases, for example, break the hydrogen bonds of a protein structure down into smaller peptides and amino acids to later be distributed by the body. This acids and bases component accounts for the environment in our digestion also, acidic environments/ low PH is enough to break down these linkages in protein. Our gut sits at around a PH of 2 and severe breakdown of protein structure outside of our stomach can be measured to occur at a PH of 2.5.
If we take a look at the study conducted on WPI (Whey Protein Isolate) and its outcomes when exposed to elements known to denature proteins. (Effect of heat, pH, ultrasonication, and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra) Food Chem 2017. We see that this form of the protein was sensitive to denaturing when exposed to the following:
- Heat denaturation occurred at temperatures of 90 degrees celsius.
- PH environment level of 2.5
- Ethanol exposure to the WPI at a range of 20-50% denatured the protein by up to 80%
External factors from various areas, as we can see, are liabilities for the structural integrity of the protein.
Does this mean the denatured protein is bad for us?
No, not necessarily – with dietary proteins, most are denatured in a way, during the process of digestion to free up amino acids and provide the building blocks the body needs to still build and repair. The cost of denatured protein being negative only really comes in the form of two things:
When you are cooking with various forms of protein that are sensitive to heat and do become less stable in their makeup, you can find that it can give a bit of an ‘off taste’ to your cooking and or your recipe where you are using a whey protein isolate in for example may not be as predictable in the final outcome of consistency and flavour.
The concept of denatured protein has in the past and even currently still been a favoured go-to for many in the fitness industry who want to opt for a whey protein hydrolysate. The hydrolysate aspect of this form means that the protein has gone through a hydrolysis process to break apart the protein structure into much smaller individual peptide bonds and free up amino acids that may make it easier to digest if you are getting more of it in during the day and want It to be a bit gentler on the stomach.
Now, the only other downside to this is that if you have a protein designed to be providing a specific function, the process of denaturation may inhibit the predictability of that, but nutritionally the value of the protein doesn’t change that much at all.
What about cooking with collagen?
The answer you have been waiting for… yes cooking with collagen is totally fine. We spoke on the hydrolysis process above be used to extract peptides from protein in a very efficient cleaving-like manner, these peptides provide a specific function intent, like a key in a lock. We recently covered this in more detail in our “what is a peptide” article piece which you might enjoy.
Collagen and the process of extraction not just collagen itself from sources, but the peptides especially, is done through an exceedingly high-temperature range of hydrolysis to break apart the bonds and section out specific peptides to be used for specific functions in the body – think of the slight variation between collagen that makes up bone, tendons, ligaments, cartilage, skin and connective tissue as a whole in the body – they are all collagen forms, just different in structure.
Because these peptides are extremely heat-stable due to their process that is undergone for extraction – it is very difficult to denature these through heat alone. These peptides are useful beyond digestion in order to provide their intended function for this reason. To put this in a perspective and wrap up, the process at which collagen peptides are extracted is at temperatures of up to 300 degrees – meaning that if you are planning on making some pancakes or muffins with any of the Noway range… go for it; your results will be predictable and the flavour profile will be consistent each time.
To find more of the recipes in which we use the Noway collagen range – head to our recipe page to see all our delicious creations!
- Tamás, M. J., Sharma, S. K., Ibstedt, S., Jacobson, T., & Christen, P. (2014). Heavy metals and metalloids as a cause for protein misfolding and aggregation. Biomolecules, 4(1), 252–267. https://doi.org/10.3390/biom4010252
- O’Brien, E. P., Brooks, B. R., & Thirumalai, D. (2012). Effects of pH on proteins: predictions for ensemble and single-molecule pulling experiments. Journal of the American Chemical Society, 134(2), 979–987. https://doi.org/10.1021/ja206557y
- Schön, A., Clarkson, B. R., Jaime, M., & Freire, E. (2017). Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry. Proteins, 85(11), 2009–2016. https://doi.org/10.1002/prot.25354
- Nikolaidis A, Andreadis M, Moschakis T. Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra. Food Chem. 2017 Oct 1;232:425-433. doi: 10.1016/j.foodchem.2017.04.022. Epub 2017 Apr 6. PMID: 28490093.
- León-López, A., Morales-Peñaloza, A., Martínez-Juárez, V. M., Vargas-Torres, A., Zeugolis, D. I., & Aguirre-Álvarez, G. (2019). Hydrolyzed Collagen-Sources and Applications. Molecules (Basel, Switzerland), 24(22), 4031. https://doi.org/10.3390/molecules24224031