Gelatin Can Exarcerbate A Protein Insufficiency

[Amazoniac]

Hydrolyzed collagen (gelatin) decreases food efficiency and the bioavailability of high-quality protein in rats

"Gelatin and collagen hydrolysate have been shown to improve skin hydration, transepidermal water loss, elasticity, and skin barrier dysfunction 7, 8. Furthermore, they have been used to promote weight loss because studies have shown that gelatin can inhibit appetite and promote satiety 9, 10. However, the use of gelatin in a protein-restricted diets (like those before and after gastrointestinal tract surgery, chronic renal insufficiency treatment diets, and those aimed to promote weight loss 11, 12) could be a potential nutritional risk. Insufficient protein intake (in terms of both quantity and quality) inhibits endogenous metabolism of proteins, prolongs the inflammatory phase of the healing process, decreases fibroblast proliferation, angiogenesis and collagen synthesis, and impairs tissue repair 12. Therefore, the use of gelatin in a protein-deficient diet could slow patient recovery."

"The animals fed only gelatin as protein source lost body weight in a similar way to those fed the protein-free diet, as reported in other studies 22 , 23. This result can be explained by the low protein quality of gelatin since its deficiency in indispensable amino acids inhibits endogenous protein synthesis. Furthermore, there is evidence in the literature that rats reject diets deficient in indispensable amino acids. As a result, the food intake of the animals is lower than their energy requirements 24. This was confirmed in the present study as the G10 group rejected more than half (57.6%) of the diet offered. The low energy intake along with the deficiency in indispensable amino acids accelerated the protein malnutrition of the animals 25."

"The high protein digestibility of the diets (approximately 95%) indicates that gelatin did not influence casein digestibility. The absorption of the amino acids in gelatin is facilitated since it is a partially-hydrolyzed protein derived from collagen, and its digestibility is comparable to that of casein 3 , 21. Therefore, it can be concluded that protein digestibility did not influence the decrease in protein efficiency in the casein/gelatin mixture."

"Considering that the casein/gelatin mixture (4:1 of protein content) has sufficient indispensable amino acid content, as well as high digestibility, this mixture could be expected to have protein quality close to that of casein. However, this study showed that gelatin negatively influenced the protein quality of the casein/gelatin mixture."
?

"In the present study, using casein and gelatin mixtures of (20% of the protein content), it was observed that gelatin decreases the efficiency of a high-quality protein in protein-restricted diets. This finding suggests that in some clinical practices, mainly in situations that involve protein catabolism, gelatin, or partially-hydrolyzed collagen could eventually worsen the catabolic status and thus slow patient recovery. Moreover, in cases of high rate of catabolism, such as major burns, cancer, and malnutrition, special attention to the supplements prescription is suggested because these products can have gelatin as source of protein or amino acids."

"Gelatin interferes with protein efficiency of high-quality protein. This influence depends on the gelatin concentration in the mixtures and the amount of protein in the diet. When there is low protein intake, gelatin decreases food efficiency and the bioavailability of high-quality protein."

--
Experimental models of malnutrition and its effect on skin trophism

"The malnourished animals in the gelatin group [(5% casein + 15% gelatin) vs (20% casein)] experienced weight loss and stunted growth; their skin was thinner and more fragile; they were lethargic and experienced hair loss."

"After a 30-day period, mean epidermal thick ness in the well-nourished group was statistically similar to that of the animals in the malnourished group; however, dermal thickness was significantly lower in the malnourished group compared to the well-nouris hed group (p<0.0001) (Figures 5A and 5B). Figures 5C and 5D show this difference in dermal thickness between the two groups from a histological point of view."

"The percentage of coll agen was higher in the group of well-nourished animals and this difference was statistically significant (p<0.003) (Figure 6A). In the qual itative histological analysis, the area of coll a gen was better organized in the well-nourished group compared to the malnourished group (Figures 6B and 6C)."


@tyw, I think that this might interest you.

 

[tyw]

Gelatin is one of the only true "incomplete" proteins out there, and is absent of many amino acids. (Note that even the so-called-incomplete plant proteins have all the required amino acids; they just have reduced levels of certain ones)

What we see in these studies is completely expected given the context:

(1) in the first study, they used weanling rats -- ie: growing animals whose need for full-spectrum dietary amino acid consumption is different from a fully-grown animal. This logic applies to humans as well.

​

Sidenote: Which is also why the Protein Efficiency Ratio is not a useful measure for human adult protein consumption at all.​

(2) in the second study, the rats were put into a state of caloric restriction, which we know increases net nitrogen turnover rates, and thus dietary protein requirements.

As said before, gelatin is a poor primary protein source, and the results were predictable.

If we really want to get into more speculation, we can take about how excessive proline and glycine could have specific effects on free Amino Acid pool during caloric restriction, and where there may be potential negative consequences, but the main trigger is still the context of protein under-nourishment given the circumstances (either fast growth in youth, or caloric restriction)

If there is already sufficient protein in the diet (and note that the amount that defines "sufficient protein" is defined by caloric intake), then the issues above do not come about. That is what we see in the real world of people eating gelatin as a by-product of regular food (eg: tendinous cuts of meat)

NOTE: this says nothing about the consumption of isolated gelatin, whether it be in the form of bone broth, or powdered / sheet preparations. Some people have reported issues with those, and those issues are most likely caused by other factors.​

....

 

[jaa]

If we really want to get into more speculation, we can take about how excessive proline and glycine could have specific effects on free Amino Acid pool during caloric restriction, and where there may be potential negative consequences, but the main trigger is still the context of protein under-nourishment given the circumstances (either fast growth in youth, or caloric restriction)

If there is already sufficient protein in the diet (and note that the amount that defines "sufficient protein" is defined by caloric intake), then the issues above do not come about. That is what we see in the real world of people eating gelatin as a by-product of regular food (eg: tendinous cuts of meat)

....

I wouldn't mind hearing about that speculation.

I eat a lot of gelatin. Between 40-60g /day. I also eat about 60g of protein from a mix of liver, heart, muscle meat, cheese, milk, oysters, mussels, and scallops. I don't feel like I experience any negative effects from gelatin, but do you think I could causing a little harm in the long run?

 

[tara]

The experimental animals were getting 3/5 of their protein from gelatin, right? So in addition to being young growing creatures in need of all the amino acids, they were also eating a higher proportion of gelatin than Peat or anyone round here recommends even for adults, right?

 

[jyb]

See glycine causing grey hair by reducing absorption efficiency of other proteins Association Of Potassium Caproyl Tyrosine, L-phenylalanine And Taurine And Use Thereof To Prevent An

 

[Amazoniac]

Gelatin is one of the only true "incomplete" proteins out there, and is absent of many amino acids. (Note that even the so-called-incomplete plant proteins have all the required amino acids; they just have reduced levels of certain ones)

What we see in these studies is completely expected given the context:

(1) in the first study, they used weanling rats -- ie: growing animals whose need for full-spectrum dietary amino acid consumption is different from a fully-grown animal. This logic applies to humans as well.

​

Sidenote: Which is also why the Protein Efficiency Ratio is not a useful measure for human adult protein consumption at all.​

(2) in the second study, the rats were put into a state of caloric restriction, which we know increases net nitrogen turnover rates, and thus dietary protein requirements.

As said before, gelatin is a poor primary protein source, and the results were predictable.

If we really want to get into more speculation, we can take about how excessive proline and glycine could have specific effects on free Amino Acid pool during caloric restriction, and where there may be potential negative consequences, but the main trigger is still the context of protein under-nourishment given the circumstances (either fast growth in youth, or caloric restriction)

If there is already sufficient protein in the diet (and note that the amount that defines "sufficient protein" is defined by caloric intake), then the issues above do not come about. That is what we see in the real world of people eating gelatin as a by-product of regular food (eg: tendinous cuts of meat)

NOTE: this says nothing about the consumption of isolated gelatin, whether it be in the form of bone broth, or powdered / sheet preparations. Some people have reported issues with those, and those issues are most likely caused by other factors.​

....

Good points as always!
The unexpected thing (at least for me) is that in diets low in "indispensable" proteins the gelatin made the outcome worse, instead of sparing protein and easing the insufficiency.

But regarding (2), the second model of malnourishment was just giving them gelatin in place of some casein. As far as I can tell, they were given enough calories, but they could be eating less for the reasons mentioned above.

Like jaa, I'm also interested if you can elaborate on that part..

 

[Amazoniac]

The experimental animals were getting 3/5 of their protein from gelatin, right? So in addition to being young growing creatures in need of all the amino acids, they were also eating a higher proportion of gelatin than Peat or anyone round here recommends even for adults, right?

On the first: 1/5 of proteins
"The rats were treated with protein-restricted diets (10.0 and 12.5%) containing casein (control diets), casein with gelatin mixtures (4:1 of protein content), and gelatin as sources of protein."

On the second, much more: 3/4 of proteins

 

[Makrosky]

@Amazoniac, @tyw,

So I understand the problem (if any) would be using gelatin/collagen as your ONLY protein source ?

Maybe adding some burtlancasterone to the gelation would mitigate some of those effects ?

 

[Amazoniac]

@Makrosky
As far as I can tell, it's not an issue as long as you are eating enough of the "indispensable" amino acids.
And the proportion alone doesn't mean much, same thing for PUFA intake; the proportion only matters if the total intake falls into the desired range.

For me it was relatively easy to suspect that using gelatin on a low-protein diet causes problems because I experienced that. However it took me some time to be certain because it's counter-intuitive. I could never imagine that additional protein, in the form of gelatin, can have that effect of exacerbating a protein insufficiency.

 

[raypeatclips]

For me it was relatively easy to suspect that using gelatin on a low-protein diet causes problems because I experienced that..

What problems did you experience? Have you tried eating gelatin from foods, as in oxtail and chicken feet that Peat has mentioned before?

 

[Amazoniac]

What problems did you experience? Have you tried eating gelatin from foods, as in oxtail and chicken feet that Peat has mentioned before?

The same clues that I use as indicators that I'm not eating enough protein: hair starts to lose its shine, skin gets drier and rougher, nails (and also hair) grow slower, digestion is not as smooth and hypoburtlancastenemia, mostly.
And it's not something related to impurities, or toxins, because at this point I think that I can distinguish the reaction.

 

[Makrosky]

@Makrosky
As far as I can tell, it's not an issue as long as you are eating enough of the "indispensable" amino acids.
And the proportion alone doesn't mean much, same thing for PUFA intake; the proportion only matters if the total intake falls into the desired range.

For me it was relatively easy to suspect that using gelatin on a low-protein diet causes problems because I experienced that. However it took me some time to be certain because it's counter-intuitive. I could never imagine that additional protein, in the form of gelatin, can have that effect of exacerbating a protein insufficiency.

This reminds me one of the Mula Nasrudin tales... (I'm paraphrasing)

"The Mula Nasrudin wasn't feeling very well... He decided to go to the doctor to see if he could help. Upon examination of the Mula, the doctor prescribed a bleeding with leeches. He didn't like the diagnosis so he went to a second doctor. The second doctor examined Nasrudin and prescribed immediate surgery. The Mula was very afraid so he went to a third doctor. After a deep examination, he prescribed some purgative herbs and told him he would get well. Nasrudin went back home thinking about it... Upon arrival, his relatives asked : So, Mula, what did the doctor tell you ? and he replied : I went to three doctors. The first one prescribed surgery, the second one a bleeding, and the third one an herbal medicine. "So what are you gonna do then, Mula ?" and he replied : I've decided to do 1/3 of the surgery, 1/3 of the bleeding, and take 1/3 of the herbs."

 

[tyw]

Good points as always!
The unexpected thing (at least for me) is that in diets low in "indispensable" proteins the gelatin made the outcome worse, instead of sparing protein and easing the insufficiency.

But regarding (2), the second model of malnourishment was just giving them gelatin in place of some casein. As far as I can tell, they were given enough calories, but they could be eating less for the reasons mentioned above.

Like jaa, I'm also interested if you can elaborate on that part..

I'm pretty sure that in the second study, it was the case where:

- Properly nourished => Rats were OK
- Malnourished with "balanced protein" => Rats suffered
- Malnourished with "incomplete protein" (gelatin) => Rats suffered more

The primary factor was energetic intake, and not protein composition.

----

It is useful here to go back to basics of protein metabolism. Below is a chart from Lyle McDonald's "Protein Book" -- The Protein Book : Bodyrecomposition (I like all of Lyle's work, and as usual, recommend his stuff)

Note the huge role that the liver plays in all of this. All dietary amino acids must go through the liver, which then decides whether or not to push it through to the Free Amino Acid Pool, or to get rid of some of these amino acids.

Sidenote: which is also why liver metabolism, and therefore pre-existing liver dysfunction, is going to tremendously affect the ability to process protein. I have no recommendations here, but I've seen many cases where reducing overall protein (and fat) intake was the correct thing to do during particular illnesses.​

This Free Amino Acid Pool is under tight regulation, which practically means that we have no clue how a particular person's body will exactly decide to regulate this pool.

Also, what can arguably be said to be the 2 primary amino acids in Gelatin -- Proline and Glycine -- are considered "Conditionally Essential":

- Proline and hydroxyproline metabolism: implications for animal and human nutrition
- https://www.researchgate.net/profil...and_health/links/5648089e08aef646e6cfda41.pdf

ie: They can be synthesized from other amino acids, but their need is so great under certain condition (eg: in infancy) that dietary supplementation is ideally used.

Another sidenote: It is well known that both Proline and Hydroxyproline cannot be transamidated in the liver. Transamidation is considered a catabolic pathway used to both derive energy substrate from amino acids, as well as to regulate amino acid levels.

What is not well known, is how a sudden imbalance in liver amino acid influx is going to affect downstream metabolism. For example, if you eat a lot of gelatin, and thus proline, does this send a signal to the liver and thus the rest of the body, that "protein input is high, and thus protein degradation should be increased as a result"?

And for those unaware, yes, nitrogen turnover rates increase when you increase protein intake -- the more protein you eat, the body your body decides to recycle its own proteins. If amino acid intake is "balanced", and if there is other anabolic stimulus (eg: resistance training), then net protein accumulation in the body increases, and the higher recycling rate increases the rate of accumulation.

This adaptation takes places within days of shifting to a higher protein intake. Therefore, what happens if you can forcibly increase protein turnover, but yet provide the body with a mostly incomplete protein source like gelatin? Dunno, but there is room for speculation here.

Athletes usually just overcome this by eating more protein than the body needs. IMO, this is the right approach, and the commonly recommended 1g / lbs_bodyweight up to 1.5 g / lbs_bodyweight seems to be a good place for such people.​

As far as normal recommendations are concerned, I personally have no clue how to make any recommendations outside of saying "eat enough protein". People who have read some of my older posts also know that I habitually follow a relatively low protein intake, because that is what tests best given my circumstances.

Therefore, no recommendations from me, except to say that supplementing extra gelatin is not the magic that some people on the Internet make it out to be.

....

 

[Travis]

Just to make it clear in case anyone doesn't know, Ray Peat, IIRC, recommends collagen/gelatin mainly to balance out the active amino acids in muscle-meats. If you eat the entire animal this becomes less of an issue.

If a person eats a large serving of meat, it's probably helpful to have 5 or 10 grams of gelatin at approximately the same time, so that the amino acids enter the blood stream in balance.

Gelatin, stress, longevity

Gelatin is made up of the neutral and non-reactive amino acids in connective tissue and skin. Muscle, and other functional proteins, needs amino acids with reactive side-chains in order to exchange cations and anions during contraction (see Gilbert Ling). The neutral amino acids are the safest amino acids, and Ray Peat found that the negative effects of super-high protein diets was attributed to cysteine and tryptophan.

Restricting only tryptophan, or only cysteine, produces a greater extension of the life span than achieved in most of the studies of caloric restriction...Both tryptophan and cysteine inhibit thyroid function and mitochondrial energy production, and have other effects that decrease the ability to withstand stress. Tryptophan is the precursor to serotonin, which causes inflammation, immunodepression, and generally the same changes seen in aging.

So as long as you get the bare minimum of the potentially dangerous ones, a bit of extra gelatin should be helpful.

Here is a compound bar graph of the total amino acid contents of beef vs whole egg. I think that it is fair to consider egg as completely balanced since it has all of the amino acids in the correct proportion for a baby chicken. You will notice that there are large relative differences among cysteine, glycine, serine, and tryptophan. The so-called "perfect amino acid ratio" is obviously up for debate. Whole egg seems like a fair enough standard, but perhaps adults require different ratios than embryonic birds.

Maybe eating something like 50% RDA for cysteine and tryptophan and 125% for glycine, proline, and serine would be good for longevity and skin; but cysteine (glutathione) can be helpful for removing lead, mercury and arsenic from the body, as the sulfhydryl group binds strongly to these metals.

 

[DaveFoster]

I would love a source for burtlancasterone.

 

[Amazoniac]

I'm pretty sure that in the second study, it was the case where:

- Properly nourished => Rats were OK
- Malnourished with "balanced protein" => Rats suffered
- Malnourished with "incomplete protein" (gelatin) => Rats suffered more

The primary factor was energetic intake, and not protein composition.

?
Marasmus model: normal vs half of the needed calories
Gelatin model: (x) normal with only casein vs (y) normal with less casein and completed with gelatin

"After a 30-day period, mean epidermal thick ness in the well-nourished group [x] was statistically similar to that of the animals in the malnourished group [y]; however, dermal thickness was significantly lower in the malnourished group compared to the well-nourished group (p<0.0001) (Figures 5A and 5B). Figures 5C and 5D show this difference in dermal thickness between the two groups from a histological point of view."

What is not well known, is how a sudden imbalance in liver amino acid influx is going to affect downstream metabolism. For example, if you eat a lot of gelatin, and thus proline, does this send a signal to the liver and thus the rest of the body, that "protein input is high, and thus protein degradation should be increased as a result"?

This adaptation takes places within days of shifting to a higher protein intake. Therefore, what happens if you can forcibly increase protein turnover, but yet provide the body with a mostly incomplete protein source like gelatin? Dunno, but there is room for speculation here.

This is the concerning part.
Thank you for the tips as to where to start looking for more details.

And for those unaware, yes, nitrogen turnover rates increase when you increase protein intake -- the more protein you eat, the body your body decides to recycle its own proteins. If amino acid intake is "balanced", and if there is other anabolic stimulus (eg: resistance training), then net protein accumulation in the body increases, and the higher recycling rate increases the rate of accumulation.

I didn't know that, I expected the opposite if I had to guess..

 

[Amazoniac]

Oh, and perhaps it would be great to change the title of the thread mainly to a more sensationalist but also more indexable/findable one for those that google it in the future.
Like: Gelatin can exarcerbate a protein insufficiency
If there are any objections, let me know; if not, dear charlie's angel that moved that egg thread to the egg section stealthily, could you please change it?

 

[superhuman]

@tyw lyle recommends a very high amount of protein, esp for people that workout. Like 3-4g/kg, that seems like a ton and you will get a ton of bad aminos with that? Ray says 100-150g a day is enough for athletes

 

[tyw]

?
Marasmus model: normal vs half of the needed calories
Gelatin model: (x) normal with only casein vs (y) normal with less casein and completed with gelatin

"After a 30-day period, mean epidermal thick ness in the well-nourished group [x] was statistically similar to that of the animals in the malnourished group [y]; however, dermal thickness was significantly lower in the malnourished group compared to the well-nourished group (p<0.0001) (Figures 5A and 5B). Figures 5C and 5D show this difference in dermal thickness between the two groups from a histological point of view."

Yes, but I took that to mean that Both groups suffered the malnourishment, regardless of protein consumption, as the author state:

The results shown in the two models of malnutrition were similar irrespective of the model used, showing the negative effect of malnutrition on skin trophism in these animals, an effect that was confirmed histologically by the reduction in dermal thickness and consequent decrease in the percentage of collagen, which may result in delays in the skin healing process, as has been already described by various authors. 6, 11, 14, 15, 26, 27​

@tyw lyle recommends a very high amount of protein, esp for people that workout. Like 3-4g/kg, that seems like a ton and you will get a ton of bad aminos with that? Ray says 100-150g a day is enough for athletes

"Too much" of a particular amino acid is a very subjective amount. The liver will have gatekeeping authority over how much, and which amino acids to keep. This gets into the territory of huge individual variation, where some people will be able to produce a "full spectrum, balanced" Amino Acid pool in the face of high protein intake from relatively complete sources (even if they are all muscle meats), and some people who will keel over and have amino acid imbalances.

Lyle's take is simple -- for athletic performance gains, 2g/kg_bodyweight is a baseline caloric intake, with no obvious negative side effects at 4g/kg_bodyweight. He is talking about Athletes, not what the majority of people think of "people who workout".

I obviously don't agree with all the recommendations he will make, but this one, given the qualified context, is perfectly inline. The recommendation for Lyle's work is with regard to the body of knowledge which he brings to the table, which involves at both of basic physiology plus added insight. Knowing that foundational knowledge clears up many common questions seen on this forum.

For non-athletes, the general recommendation on this forum -- to start at a moderate 1g/kg_bodyweight intake, and seek to have some balance in the amino acid profile -- is probably a good starting point. From there, you adjust based on real world results. One thing for sure, that "protein requirements" is going to be highly variable given a particular individual and their present-day context.

....

 

[Amazoniac]

Yes, but I took that to mean that Both groups suffered the malnourishment, regardless of protein consumption, as the author state:

The results shown in the two models of malnutrition were similar irrespective of the model used, showing the negative effect of malnutrition on skin trophism in these animals, an effect that was confirmed histologically by the reduction in dermal thickness and consequent decrease in the percentage of collagen, which may result in delays in the skin healing process, as has been already described by various authors. 6, 11, 14, 15, 26, 27​

As far as I understood, the controls from both models were fine and eating enough, which were referred to as well-nourished groups.
I remember that you mentioned some time ago that you eat a somewhat low-protein diet, have you experienced something in this regard?

--
Thank you for changing the title, kind invisible entity.