Amino Acid Supplementation For People With Poor Digestion

Amazoniac

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Someone who hasn't been digesting protein well for a long time may end up malnourished in spite of the diet being adequate, Raj mentioned this before. Once supplementation with purified amino acids starts, the person will be switching from destruction to construction and micronutrients have to be abundant.

- Malnutrition and Trace Element Metabolism

"Whereas it is presumed that hepatic depots of copper are available at times of increased copper requirement, there is little evidence that such specific reserves exist for manganese or zinc. Thus, although adventitious release of zinc and manganese from muscle and bone may occur during states of nutritional deficiency and tissue catabolism, as soon as these processes are reversed, the organism becomes totally dependent on an adequate exogenous supply of the metals. No doubt this requirement for an additional source applies also when functional reserves of metals have become depleted during a period of deficiency."​

It's one more reason to be mindful with these.
 
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tankasnowgod

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Purified amino acids will likely induce micronutrient deficiencies, every meal had a tablet of 'VIT-formula'. Digesting protein takes longer (peptides compared to proteids), it's an opportunity for the body to make adjustments and reallocate nutrients according to what's available, perhaps measures that retard release from the stomach may be of welp. And this is considering that they're consumed in the right proportions, or else it's one additional disturbance.

Agreed, if taking Amino Acids, and Amino Acids only chronically. But if you are still eating regular protein and things like liver and oysters, this probably won't happen. There shouldn't be much danger of this using them as a protein replacement for a few meals a week, or even for all protein for a short term burst, like a week or two.

Unless I'm missing something?
 

tankasnowgod

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Someone who hasn't been digesting protein well for a long time may end up malnourished in spite of the diet being adequate, Raj mentioned this before. Once supplementation with purified amino acids starts, the person will be switching from destruction to construction and micronutrients have to be abundant.

- Malnutrition and Trace Element Metabolism

"Whereas it is presumed that hepatic depots of copper are available at times of increased copper requirement, there is little evidence that such specific reserves exist for manganese or zinc. Thus, although adventitious release of zinc and manganese from muscle and bone may occur during states of nutritional deficiency and tissue catabolism, as soon as these processes are reversed, the organism becomes totally dependent on an adequate exogenous supply of the metals. No doubt this requirement for an additional source applies also when functional reserves of metals have become depleted during a period of deficiency."​

It's one more reason to be mindful with these.

Ah! The "Burr Disease!" I'll file this under "quality problem," since it suggests that it's ramping up metabolism, and increased food intake should go with it. Still a good thing to be mindful of.
 

Amazoniac

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Agreed, if taking Amino Acids, and Amino Acids only chronically. But if you are still eating regular protein and things like liver and oysters, this probably won't happen. There shouldn't be much danger of this using them as a protein replacement for a few meals a week, or even for all protein for a short term burst, like a week or two.

Unless I'm missing something?
Ah! The "Burr Disease!" I'll file this under "quality problem," since it suggests that it's ramping up metabolism, and increased food intake should go with it. Still a good thing to be mindful of.
Yes, a few depleting meals shouldn't be a problem.

In our case it's not protein-energy malnutrition, it's more like protein-micronutrient malnutrition. Some nutrients are bound to proteins, if someone doesn't digest proteins well, part of the nutrition may be lost along.

Many of us have chronic deficiencies and this strategy is being purposed mainly for people with poor digestion (title) that need extreme measures. It's good to have options, but I would leave the protein replacement as a last resource because it's easy to mess up and not sustainable without additional support. If amino acids were present in the diet and the person couldn't use them, digestive aids, antimicrobials, and agents that normalize motility should be favored because it's a problem with digestion, not dietary deficiency.

It's likely that someone who can't digest them properly drops the intake to bear with the situation, this makes the person susceptible to amino acid imbalances, contrary to the viking that barely notices when something is off. A formula that's meant to synthesize protein is serving as a guide and evil amino acids are pieced out, I doubt that it can be maintained for long, the negligence might lead to the Rayfeeding Syndrome.

Decreasing the consumption of these foods puts them at greater risk of deficiencies for being important contributors:


The lack of phosphate in the presence of factors that lower it might eventually become an issue too. It's not just the lack of micronutrients in a malnourished state, but amino acids that are not essential yet of value.

One likely scenario is an issue at the metabolic level that would require specific amino acids to correct the imbalance, but members seek or come up with blends, where it's either a hit or miss and little to learn.

The justification that purified nutrients are digested more easily can be applied to anything in the diet, why not dextructose syrup as carbohydrate or stentic acid (C18H36O2) as fat? It's preferable to leave these as emergency measures.
 
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AFAIK, there are no MAP products withouht tryptophan and histidine. So, if you want something better you'll have to buy the individual aminos yourself and supplement as needed. Unless your digestion is really compromised (like after surgery or not producing any stomach acid or pancreatic enzymes) I would use this only as a supplement, not main source of protein. The effectiveness depends on how much protein you are trying to replace, so 2 capsules is an arbitrary measure.

The MAP product I use (BodyHealth PerfectAmino) is omits the histidine but still has tryptophan and methionine in it. It kind of expensive but it seems like the real deal. I like the doctor who promotes it (Dr. David Minkoff) who's an Iron Man triathlete well into his 60's. He's not very Peaty, but I still learn a lot from him.

It tastes pretty nasty, but I deal. I take between 10-20 tablets (1g/tablet) in one dose 3-5 times per week (not daily).

One drawback is that it does make me sleepier earlier than I want to. But I read somewhere on this thread that it's a good sign of its effectiveness?
If it didn't make me so sleepy, I'd take 24 grams daily.

In any case, after reading this thread, I'm inspired to make my own powder with the 6 remaining EAA's. I supplement Glycine in a separate much larger dose daily.

I also plan on supplementing Taurine and Carnosine/Beta-Alanine separately in larger doses.
 

GAF

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Biotics Research Amino Acid Quick Sorb Liquid Formula, Highly Absorbed, Glycine, L Alanine, L Arginine HCl, L Lysine HCl, L Proline, L Histidine HCl, L Serine, L Threonine, L Valine 2 Fluid Ounces​


Fellas, I stumbled on this couple months ago and it has changed my digestion and my body. Very inexpensive. On amazon. I think it may solve the problem. Give it a try.
 

Amazoniac

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Since the content here is based on milligrams of amino acids per gram of protein, those that are not essential take up space. They could've been leftened out, but we can't ignore them and the profile remains useful for comparison; how the differences increase or decrease in each amino acid. If the worthless amino acids were excluded, it would make values go up proportionally after raydistribution.

For the references, I also distributed methionine (2/3) to cysteine (1/3) and phenylalanine (1/2) to tyrosine (1/2). Jorge's MAP had the values dropped to 40% because of the guys' claimed efficiency, but the profile isn't affected. Lines were included just to make it easier to trace.

You can compare gelatin with the references or other "foods" and think in terms of multiples of the content of an amino acid. Against references (gap until the floating lines), the shortage in branch'd-chained, sulfur-containing amino acids, tryptophan and histidine is evident, but it's not good in threonine and phenylalanine/tyrosine (distributed) either. Things get worse when it's compared only against "foods", making it clearly low on those and lysine (or everything, with the non-essential toxins that are high to blame).

It can be argued that the solution is simple: double the amount of gelatin and most of them will be covered, but then you'd have to deal with all the amino acids that occur in high amounts, the undesirable ones must limit. If those that are in excess could be oxidized without being problematic, we wouldn't witness the imbalances that this tends to cause. They might also use up nutrients in the process of degradation that gelatin is devoid of.

Rather than having amino acids floating around until they're cleared, a BCAA supplement can promote protein synthesis without making up for the rest that's missing or off, I'm not sure if extra threonine helps much. Perhaps this fast forwards the transition of gelatin from sparing to depleting/consuming, I don't expect it to be sustainable.
 
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Hgreen56

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Studies often quote numbers on protein utilization and it seems that the highest utilization from food sources is for eggs (45%), followed by milk (30%), meat (25%) all the way down to plant protein (<15%). These numbers show why plant protein is in general not a good food for most people - i.e. you spend a lot of energy to digest and get very little benefit from it.
“Clean” Protein | drbillyhealth.com
Doesn't this percentage increase when someone heat up the milk?
 

Jing

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Biotics Research Amino Acid Quick Sorb Liquid Formula, Highly Absorbed, Glycine, L Alanine, L Arginine HCl, L Lysine HCl, L Proline, L Histidine HCl, L Serine, L Threonine, L Valine 2 Fluid Ounces​


Fellas, I stumbled on this couple months ago and it has changed my digestion and my body. Very inexpensive. On amazon. I think it may solve the problem. Give it a try.
Do you take it on an empty stomach or with food? And how long does a bottle last ?
 

GAF

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Do you take it on an empty stomach or with food? And how long does a bottle last ?
I take it sometimes before and sometimes after. Not necessarily with every meal or even near a meal. Can't tell that it matters.

375 servings per bottle. Lasts up to 3 months. First bottle last 2.5 months. Using more now but can't tell that more is more beneficial.

This stuff is incredible. I will never go without it. I have 10 extra bottles , but I am not sharing.
 

FitnessMike

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FitnessMike

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I take it sometimes before and sometimes after. Not necessarily with every meal or even near a meal. Can't tell that it matters.

375 servings per bottle. Lasts up to 3 months. First bottle last 2.5 months. Using more now but can't tell that more is more beneficial.

This stuff is incredible. I will never go without it. I have 10 extra bottles , but I am not sharing.
Can you say a bit more about how did it help your digestion? i don't understand how such a small amount of amino acids would be better than a powdered version in a higher amount? Also, any idea where can you get these from? looks like you can get them only thru the practitioner.
 
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Amazoniac

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As mentioned by Jorge (can be confirmed here), collagen is relatively low in threonine. This may become an issue:

- Specific roles of threonine in intestinal mucosal integrity and barrier function

"Small intestinal integrity, which is most commonly evaluated by histological measurements of villus height, villus surface area, and crypt depth (16). The intestinal mucus covers the mucosa with a semisolid gel to function as a diffusion barrier for the solutes with low molecular weight and as a physical barrier for microorganisms and their toxins (17). The actual mucus production can hardly be measured directly. However, it can be estimated indirectly by numbers of goblet cells (16). Transepithelial permeability can be determined using passive diffusion of a marker or Ussing chambers (18, 19). The increase in transepithelial permeability can decrease the intestinal mucosal integrity. As a result, pathogens and toxins may cross the mucosal epithelial barrier. The activities of brush border enzymes (including sucrase, lactase, maltase, and isomaltase) are also the indicators of intestinal mucosal integrity and function. In addition, the mass of intestine and mucosae, as well as their daily gain, can be indicative of intestinal mucosal integrity (16)."

"The mucus gel layer may protect the intestinal mucosa against digestive secretions, pathogens and physico-chemical damage (32-34). The mucus has the viscoelastic and polymer-like properties that are derived from the major gelforming glycoprotein components, namely mucins. Mucins are secreted by intestinal goblet cells and can be broadly classified into neutral and acidic subtypes. Acidic mucins are further divided into sulfated (sulfomucins) or nonsulfated (sialamucins) groups (35, 36). Because of the analogs between the mucins and the glycoprotein of the enterocyte membrane, they can act as competitors to the binding of many foreign antigens (37, 38). In 2006, Ven der Sluis et al. (39) reported that the deficiency of MUC2, a kind of mucins containing high levels of threonine, could lead to colon inflammation in MUC2 knockout mice. Additionally, the mucus gel layer participates in filtering luminal nutrients and can affect the digestion and absorption of nutrients. Furthermore, the mucosa can produce a broad spectrum of antimicrobial agents, such as antimicrobial peptides, to maintain mucosal integrity (40, 41)."

"Studies with both humans and pigs have shown that 20-70% of the first-pass metabolism of dietary essential amino acids is consumed by the portal-drained viscera (PDV), including the intestines, pancreas, spleen, and stomach (42, 43). Recent studies showed that large amounts (40-60%) of dietary threonine were extracted by the PDV (dominated by the intestine) in first pass metabolism, while the values for other essential amino acids were 30-60% (42, 44-46). In infant studies involving dual stable-isotope tracer techniques, the intestinal first-pass threonine metabolism was 82% and 70% for partial enteral feeding and full enteral feeding, respectively (47). These values might have been overestimated possibly due to methodological problems, because the efficiency of utilization of dietary threonine for protein accretion in neonates is approximately 60-70%. Dawson et al. demonstrated that threonine uptake by the colonic mucosa of humans with carcinoma was higher than that in the normal mucosa (48). In addition, intestinal inflammation enhanced gastrointestinal threonine uptake in enterally fed mini-pigs (49). Likewise, the study conducted by Bertolo et al. indicated that the whole-body threonine requirement was decreased by 60% in piglets receiving total parenteral nutrition (TPN) compared with that in piglets receiving enteral nutrition (50). Furthermore, dietary threonine deficiency caused a decrease in intestinal goblet cell numbers and mucin content, which cannot be reversed by intravenous administration of threonine (10). These data indicate that the intestine takes up a large amount of threonine from the lumen but not from arterial blood."

"The intestine is the major site of amino acid utilization and plays an active role in amino acid metabolism (51-53). The amino acids taken up by the intestine can be utilized for protein synthesis, or oxidation into CO2 for ATP production, or conversion into other amino acids and metabolic substrates (54). Threonine has two metabolic fates in the intestine: (a) incorporation into mucosal proteins [including mucosal cellular proteins and secretary proteins (e.g. mucins)); and (b) catabolism (e.g., oxidation to CO2) by luminal bacteria (42, 45, 55, 56). Schaart et al. (2005) observed that intestinal threonine oxidation in piglets only accounted for 2-9% of the total threonine utilization, while threonine incorporation into mucosal proteins accounted for 71% of the total threonine utilization (46). Thus, threonine extracted by the intestine is primarily used for the mucosal protein synthesis (55). In addition, the peptide backbone of mucins contains large amounts of threonine that represents 28-35% of the total amino acid residues (57-61). Therefore, a large proportion of the threonine extracted by the intestine is used for mucin production. However, mucin proteins cannot be digested and their amino acids cannot be reutilized by the body (44, 59). Thus, the intestinal mucin secretion represents a net loss of threonine from the animal."

"It is reported that some specific amino acids, especially threonine, are of critical importance to intestinal mucosal integrity (52, 62). A large amount of dietary threonine taken up and utilized by the intestinal mucosa may aid in maintaining the integrity and function of the intestinal mucosa."

"Recently, a large number of studies have focused on the role of dietary threonine availability in the intestinal mucin synthesis in different animal models (Table 1). For example, compared with no threonine perfusion, infusion of threonine (56 mg/g of an amino acid mixture) into isolated porcine gut loops markedly increased the fractional synthesis rates of mucins and total mucosal proteins (66%/day versus 42%/day, and 414%/day versus 323%/day, respectively) (67). This demonstrates that de novo synthesis of intestinal mucins and mucosal proteins critically depends on the availability of threonine in the intestinal lumen. In addition, piglets fed a deficient or excess dietary threonine (0.37% and 1.11% true ileal digestible (TID) threonine, respectively) remarkably decreased the total amount of mucin in duodenum and mucin-2 mRNA expression in the duodenum and jejunum, and greatly changed the mucin subtypes, compared with piglets fed the optimal level (0.89%) of dietary TID threonine (66)."

"These data indicate that dietary threonine deficiency can decrease intestinal mucin production. Moreover, threonine supplied by oral route is preferred for the maintenance of the intestinal integrity and barrier function (10)."

"Under pathological conditions, such as ileitis and sepsis, threonine requirement is enhanced because of the increase in mucin synthesis to maintain intestinal mucosal integrity."

"[..]intestinal inflammation would increase mucin synthesis to protect the gut, which may necessitate a greater amount of dietary threonine. Besides, Faure et al. demonstrated that sepsis increased mucin fractional synthesis rate and absolute synthesis rate in rats. Collectively, dietary threonine availability is a major determinant of intestinal mucin production."

"As mentioned above, intestinal paracellular permeability can be used to assess the intestinal mucosal integrity. With the increase in paracellular permeability, the intestinal integrity and epithelial barrier may decrease. A moderate threonine deficiency (6.5 g threonine/kg diet) increased the intestinal mucosal paracellular permeability in the ileum of piglets, and changed the expression of genes related with the regulation of intestinal mucosal paracellular permeability, such as tight junction protein ZO-1, cingulin, and myosin light chain kinase (65). Furthermore, the digestive enzymes contain abundance of threonine which accounts for 5-11% of the total amino acid residues. Research findings have shown that dietary threonine restriction decreased the production of digestive enzymes (71). Thus, we can speculate that dietary threonine availability may the digestion and absorption of dietary nutrients. Collectively, both intestinal paracellular permeability and brush border enzyme activities are important indicators of the intestinal mucosal integrity."

"Recently, studies with animals and humans with intestinal inflammation (11, 49, 73), sepsis (74, 75), colonic carcinoma (48), HIV infection (76) or other types of immunological challenge (77, 78) revealed an increase in threonine requirement by the intestinal mucosa due to enhanced synthesis of intestinal proteins (Table 2). Under these pathological conditions, supply of threonine in regular diets designed for healthy animals may be inadequate for the maintenance of intestinal mucosal integrity, leading to the impairment of intestinal barrier function. Interestingly, some of these studies also showed increasing dietary threonine provision with or without other amino acids enhanced mucin synthesis and re-equilibrated the gut microbiota to benefit gut function (11, 49, 75)."

"Threonine is a major component of plasma immunoglobulins in animals and humans (79-81). Some studies (8, 12, 82-84) with different animal species demonstrated that dietary threonine levels influenced plasma antibody concentrations and whole-body immune function. Furthermore, results of our research indicated that dietary threonine supplementation improved the intestinal morphology and specific immunological responses in the piglets challenged with E. coli K88+ (data no published). These findings suggest that dietary threonine availability is of great importance for supporting both intestinal-mucosal and whole-body immunity."
 

Jing

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I take it sometimes before and sometimes after. Not necessarily with every meal or even near a meal. Can't tell that it matters.

375 servings per bottle. Lasts up to 3 months. First bottle last 2.5 months. Using more now but can't tell that more is more beneficial.

This stuff is incredible. I will never go without it. I have 10 extra bottles , but I am not sharing.
Thanks.
 
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@Jing

Hi, I just purchased this over the phone if you're in the UK where I am,
I had to be put through to their practitioner who quizzed me on the reasoning behind me wanting to purchase this
I assured her I had some knowledge about amino acids and just wanted it for health.
She mentioned some contraindications regarding glucose can't remember if it was hyperglycemia or hypoglycemia. Hope this helps.
Here's the phone number. 0333 577 0404 (3)
 

Jing

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@Jing

Hi, I just purchased this over the phone if you're in the UK where I am,
I had to be put through to their practitioner who quizzed me on the reasoning behind me wanting to purchase this
I assured her I had some knowledge about amino acids and just wanted it for health.
She mentioned some contraindications regarding glucose can't remember if it was hyperglycemia or hypoglycemia. Hope this helps.
Here's the phone number. 0333 577 0404 (3)
Ok thank you.
 

GAF

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Can you say a bit more about how did it help your digestion? i don't understand how such a small amount of amino acids would be better than a powdered version in a higher amount? Also, any idea where can you get these from? looks like you can get them only thru the practitioner.

on Amazon
 

Ideonaut

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You''ll have to check what is the solubility of each amino in water. I know some of them like glycine or lysine are quite soluble in water but I am not sure about the others such as taurine. In theory, a gelatin drink would only need some threonine and BCAA added to make it a complete protein. So, try it out and let us know.
So what would be a good ratio of BCAA and threonine to gelatin? Say if I mix up 3 Tbsps (45g?) of gelatin, how much BCCA and threonine should I use?
 

Amazoniac

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So what would be a good ratio of BCAA and threonine to gelatin? Say if I mix up 3 Tbsps (45g?) of gelatin, how much BCCA and threonine should I use?
Depends on your reference and diet. BCAA ratios:

[Leucin]:[Valin]:[Isoleucin]​
[2.1]:[1.8]:[1] - Collagen​
[2.0]:[1.3]:[1] - FAO​
[1.3]:[1.1]:[1] - Jorge's MAP
[2.0]:[1.0]:[1] - BCAA supp​

Combining collagen with a typical BCAA supplement will skew the ratio towards the FAO recommendations {[2.0−2.1]:[1.0−1.8]:[1]}. However, if the reference is Jorge's MAP, you'll either have too much valine (along with leucine) or not enough isoleucine, it's better to have them separate.

The composition of collagens can vary, but if we consider that BCAAs are responsible for 6% of the weight of gelatin, 50 g would contain 3 g of BCAAs. In post #248, it's possible to tell that doubling the content of BCAAs would modify the profile in a way that gets closer to the proportions recommended by FAO.

A capsule of (2:1:1) BCAAs may contain 600 mg of amino acids, therefore, 5 of them would be needed to provide 3 g. A tablespoon is capable of holding about 10 g of gelatin (almost half if hydrolyzed collagen due to being disorganized): one such capsule per tablespoon.

Note there that when compared to other proteins, it remains devoid of tryptophan and practically cysteine as well, very low in methionine, tyrosine and histidine, and low in lysine and phenylalanine. Also, the worthless amino acids in surplus. Compound the lack of micronutrients (some that are important for protein metabolism) and you have an approach that's not sustainable, unless the products are included on top of a great deal of protein requirements already being covered and a nutritious diet is making up for what's missing.

One ingredient in a meal is capable of throwing these calculations off. The most practical approach would be to evaluate (with apps) the composition of each meal containing collagen and have the amino acids isolated to adjust as needed.


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