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Canning the 6 meals, 'clean' eating, the Post Workout Anabolic Window and GI myths
MaxBrenner
New member
Cook your Eggs
Digestibility of Cooked and Raw Egg Protein in Humans as Assessed by Stable Isotope Techniques
24hr digestibility cooked egg protein: 90%
24hr digestibility raw egg protein: 50%
"The higher digestibility of cooked egg protein presumably results from structural changes in the protein molecule induced by heating, thereby enabling the digestive enzymes to gain broader access to the peptide bonds. It has been suggested that the reduced digestibility of raw egg white is at least partially related to the presence of trypsin inhibitors in raw egg white (Matthews 1990)."
Digestibility of Cooked and Raw Egg Protein in Humans as Assessed by Stable Isotope Techniques
24hr digestibility cooked egg protein: 90%
24hr digestibility raw egg protein: 50%
"The higher digestibility of cooked egg protein presumably results from structural changes in the protein molecule induced by heating, thereby enabling the digestive enzymes to gain broader access to the peptide bonds. It has been suggested that the reduced digestibility of raw egg white is at least partially related to the presence of trypsin inhibitors in raw egg white (Matthews 1990)."
jzpowahz
Well-known member
MaxBrenner
New member
That was a really good one. Reposted
Alan always comes up with great articulations for his articles. I'm really excited that I'll be able to use Alan's articles on my blog etc. Hoping to do a question & answer with him also
hey MB, i read the first couple pages the other day and has some questions but forgot most of them lol.
what happens when the stead stream of nutrients stops, eg after 12hours of not eating?
i read about ghrelin, was increased ghrelin bad for fat loss/muscle gain or is increased levels good?
what happens when the stead stream of nutrients stops, eg after 12hours of not eating?
i read about ghrelin, was increased ghrelin bad for fat loss/muscle gain or is increased levels good?
MaxBrenner
New member
No problems Ener
Firstly, you would not be without a 'stream' of nutrients after not eating for 12 hours (Note I fast for 16 HOURS A DAY, EVERYDAY).
Simply put, 200 grams of Whey Protein (the fastest) digesting source of protein digests at 8-10 grams per hour (if taken with no other nutrients and made on water). So that would take a total of 20 hours to digest. When you add in the other macronutrients and whole food types (which digest at a much slower rate than Whey) of those macronutrients, the digestion speed slows down and down and down.
Now with fasting your metabolic rate doesn't drop until the 72 hours mark without food! And even then the down turn in metabolic speed is only 8%. So in real world situations, that is never something anyone needs to worry about. I'm not going to get into server long term calorie restriction as it does not apply either in 90% of the population.
Here is the best explanation (in layman's terms) - Ghrelin
Released primarily from the stomach, ghrelin goes to the brain where, predictable, there is a specific receptor. Among other functions, ghrelin raises levels of growth hormone. But that’s far from all.
Ghrelin also stimulates hunger (the only hormone so far found to do so) and appears to be a key hormone in initiating the hunger that goes along with meals; ghrelin drops prior to hunger and injection of ghrelin stimulates hunger specifically.
Even more interestingly, there is research suggesting that ghrelin levels become entrained to normal meal times.
So if you normally eat at 3pm (or whatever), you’ll likely find yourself becoming hungry at 3pm; this appears to occur from changes in ghrelin. I suspect this explains why people often have problems changing meal frequency, at least until ghrelin re-entrains itself to the new frequency.
That is, moving from a higher to lower frequency of meals is often accompanied by hunger at the previously ‘normal’ meal times. Moving from lower to higher is often accompanied by a lack of hunger until the body adjusts to the new frequency. I haven’t seen any work examining how long this takes but empirically it seems like it’s a couple of weeks or so.
Increased ghrelin also negatively impacts on pretty much all aspects of metabolism, slowing metabolism and increasing fat storage, at least it does this in rats with daily infusion.
In this vein, I’ve heard rumors that ghrelin is being promoted as a bulking aid for athletes and bodybuilders, both for the appetite increasing effects and the GH release. Given the negative aspects of ghrelin on metabolism, this is truly an awful idea unless the goal is to just get really fat.
In contrast, a ghrelin antagonist might be a very nice thing indeed for dieting. There appears to be work on orally available ghrelin antagonists going on.
As it turns out, ghrelin changes in the opposite direction of leptin; while leptin falls on a diet, ghrelin goes up. It almost goes without saying that leptin levels have a hand in controlling ghrelin; leptin appears to restrain both grhelin release from the gut and its stimulation of hunger.
So dieting, as usual is a double whammy in this regards: leptin goes down as ghrelin is going up with the reduction in leptin being partly responsible for the increase in ghrelin.
Ghrelin appears to play a role in both short- and long-term hunger and long-term bodyweight regulation. As mentioned above, ghrelin goes up prior to a meal; it also comes back down after eating.
However, ghrelin levels also increase overall with a loss of weight/bodyfat, decreasing when weight is gained. Individuals with a high BMI have lower ghrelin (and the idea of ghrelin resistance has been thrown around) and anorexics have higher ghrelin (which decreases with refeeding).
Nutritionally, carbohydrates appear to play a primary role in regulating ghrelin levels with dietary fat having less of an impact, the effect of protein is currently unclear. In one study, a high carbohydrate/low-fat diet generated weight loss without the normal increase in ghrelin levels.
And although only tested in anorexics, at least one study showed that the consumption of non-caloric fiber reduced ghrelin levels. Consuming small amounts of guar gum or psyllium fiber between meals might help to keep ghrelin down during a diet.
Perhaps ironically, it appears that low-sodium intakes increase ghrelin levels (although there is a racial effect). As I discussed in this article, I wonder if the low-sodium intakes taht contest bodybuilders and figure competitors often obsess about isn’t making things worse rather than better.
In one study increases in ghrelin with weight loss were related primarily to fat free mass loss but not body fat loss per se. As good reason as any to ensure that the diet is set up to prevent lean body mass loss.
Of some interest, one of the ways that bariatric surgery appears to be so successful is that, despite the massive weight loss generated, there is often no increase in ghrelin levels as would be seen with diet induced weight loss.
This may explain why weight is so rapidly lost, seemingly without hunger, with that surgery. I’d note that research also suggests that other hormone (such as Peptide YY, discussed next, and Glucagon like peptide 1, are more relevant to the hunger suppressing effect of the surgery).
For the rest of article that looks at all the hormones involved in fat loss have a read of this - Bodyweight Regulation Wrap-Up: A Few More Hormones | BodyRecomposition - The Home of Lyle McDonald
Thanks for replying MB.
So after 72hours of there about your metabolic speed(rate?) drops by ~8%. just for discussion, does the body tend to break down its own muscle/fats at this stage or later down the track?(or even at all)
I also read that article on ghrelin. What i have taken from it is that meal consistency is important for fat loss due to ghrelin being entrained by meal times and hence will increase at those intervals?
Also does that mean ignoring hunger will cause ghrelin to stay high?
im not sure if i am on the right path or not, quite a bit for me to take in
So after 72hours of there about your metabolic speed(rate?) drops by ~8%. just for discussion, does the body tend to break down its own muscle/fats at this stage or later down the track?(or even at all)
I also read that article on ghrelin. What i have taken from it is that meal consistency is important for fat loss due to ghrelin being entrained by meal times and hence will increase at those intervals?
Also does that mean ignoring hunger will cause ghrelin to stay high?
im not sure if i am on the right path or not, quite a bit for me to take in
MaxBrenner
New member
Thanks for replying MB.
So after 72hours of there about your metabolic speed(rate?) drops by ~8%. just for discussion, does the body tend to break down its own muscle/fats at this stage or later down the track?(or even at all)
I also read that article on ghrelin. What i have taken from it is that meal consistency is important for fat loss due to ghrelin being entrained by meal times and hence will increase at those intervals?
Also does that mean ignoring hunger will cause ghrelin to stay high?
im not sure if i am on the right path or not, quite a bit for me to take in
The metabolic rate slows to preserve energy to maintain function and if there is no incoming nutrients, once glycogen stores have been depleted the breakdown of protein and fats for energy will occur. It just comes back to how much 'food' has been consumed prior to the fasting period as to when and how much of the protein (muscle) and fats are used etc.
In a generalization, Ghrelin can be looked at like the insulin response. If you eat frequently it will have smaller but regular increases. With less frequent feeding, there will be larger but less regular response. At the end of the day it is same same. So ignoring 'hunger' will not keep it increased, as like all hormonal functions it adapts to the situation.
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MaxBrenner
New member
"Is it possible to eat too frequently?
It’s not uncommon to read about bodybuilders or other athletes taking the eat-more-frequently dictum to extreme levels, eating every one to two hours. The idea behind this is the idea that optimal results should occur by maintaining a near continuous influx of nutrients into the body. I imagine if they could find a way to do it, some enterprising athletes would set up a continuous intravenous drip with carbohydrates, amino acids and essential fatty acids.
This may not be a good idea in the first place. Some research, primarily using amino acid infusion, suggests that skeletal muscle can become insensitive to further stimulation of protein synthesis. In one study, amino acids were infused for several hours to 70% over normal levels (17). Protein synthesis increased after roughly 30 minutes and was maintained for the next two hours at which point protein synthesis decreased back to baseline.
Importantly, this decrease occurred despite the maintenance of high levels of blood amino acids. Additionally, there was an increase in urea production (a waste product of protein metabolism), indicating that the excess AAs were simply being catabolized in the liver to be excreted in the urine; that is, those AAs were wasted and never utilized by the muscle.
The researchers took this as a suggestion that there might be a maximum amount of protein synthesis that can occur at any one given time before a “muscle full” situation is reached (18). Perhaps more interestingly, based on the amounts of AAs infused, the researchers estimated that only 3.5 grams of AAs would be required to result in this “muscle full” situation (18). I want to make it very clear that this doesn’t mean that 3.5 grams of orally ingested AAs would cause the same effect. Rather, this represented the delivery of 3.5 grams of AAs to the muscle itself.
However, the total amount of dietary protein to achieve this amount wouldn’t be huge. Most dietary proteins are roughly 40-50% EAAs, and due to processing in the liver, slightly less than half of the ingested AAs actually make it into the bloodstream. To provide 3.5 g EAAs to skeletal muscle would require roughly 15-20 grams of whole protein over a two hour time span.
Interestingly, other more direct research supports this value. In a study I described in an earlier chapter, subjects received doses of EAAs ranging from zero to 20 g EAAs and protein synthesis was studied (19). In young subjects, muscle protein synthesis was maximized with an intake of 10 g EAAs and there was no further increase with 20 g EAAs. This represents roughly 20-25 grams of whole protein.
Consumed every three waking hours (roughly six meals per day), this would allow for a maximum protein intake of 120 grams per day before skeletal muscle protein synthesis is maxed out. For a 100kg (220 pound) athlete, this is only 1.2 g/kg, lower than even the most conservative estimates discussed in Chapter 4. As discussed previously, this research is a difficult to reconcile with other, much higher recommendations or empirical results.
However, recall from Chapter 4 that dietary protein has more functions for athletes than simply the stimulation of protein synthesis. Although the amount described above might very well maximize skeletal muscle protein synthesis, optimizing the function of other important pathways of AA metabolism would very likely raise requirements even further (20). As well, while excess amino acids may simple be oxidized off, there is evidence that increased AA oxidation is involved in the overall “anabolic drive” of the body.
Finishing up this discussion, in their most recent study, the same group examined the effect on protein synthesis of a variety of doses of infused AAs (21). Infusing AAs at four different ranges, the group saw a similar pattern to their earlier work, an initial increase in protein synthesis followed by a return to baseline despite maintenance of high AA levels. Additionally, while the lower infusion rates caused a significant increase in protein synthesis, further increases at the higher concentration levels showed smaller additional benefits. Essentially, providing low to moderate amounts of AAs gave the greatest result.
Finally, and perhaps most interestingly, the paper demonstrated conclusively that it was extracellular AA concentrations (rather than the concentration of AAs inside the muscle cell) that were involved in stimulating protein synthesis. The researchers suggested the existence of some type of amino acid “sensor” in the muscle cell membrane that sensed AA levels. The study also suggested that it was the changes in extracellular AA concentration, rather than the absolute amounts that were driving the changes in protein synthesis. That is, it was the change from lower to higher that had the effect more than the absolute amount of AAs present.
Along with the indication of a “resistance” to further stimulation of protein synthesis, it appears that raising AA concentrations (after a meal) followed by a decrease in concentrations yield the best results. Basically, spacing meals apart and allowing blood AA levels to drop, rather than maintaining AA concentrations at continuously stable levels, appears to have the greatest impact on protein synthesis. Unfortunately, this still gives no indication of how far apart those meals need to be spaced to allow a “resensitization” of the muscle to a subsequent increase in AA concentrations.
Additionally, since it was based on an amino acid infusion, it’s unclear how this would relate exactly to the consumption of meals. Between digestion and the hormonal response that occurs with eating, it may very well be that eating protein would yield a different result than what the above research found using AA infusion.
In this vein, it’s interesting to look back at the original casein versus whey research that I discussed in Chapter 2. In that study, whey protein showed an initial spike in protein synthesis followed by an increase in amino acid oxidation in the liver, a pattern not dissimilar to the work examined above (22). It seems plausible that once whey had maximally stimulated protein synthesis, the remaining AAs were simply metabolized in the liver.
In contrast, when very small amounts of whey (a few grams at a time) were sipped over a six hour span to mimic the effects of casein, there was no increase in amino acid oxidation (23); however the impact on protein synthesis was also smaller. It may very well be that flooding the body with large amounts of AAs simply overloads the muscle’s ability to utilize amino acids, causing the excess to be burned off. This would also be consistent with the fact that the slower protein, casein, actually generated a higher overall gain in leucine in the body compared to whey; by never overloading the body’s protein synthetic machinery, overall better results were obtained.
Related to the above research, another group compared the body’s use of leucine with subjects either given small hourly meals or three separate meals (24). They found that protein oxidation was decreased (by 16%) in the group given three meals. Essentially, providing amino acids too frequently appears to decrease the body’s utilization of those aminos. Rather, having discrete meals where blood amino acid levels first increase (stimulating protein synthesis without overloading the body’s ability to utilize AA’s) and then decrease for some time (so that muscle can become “sensitive” to the effect of aminos again) would seem to be ideal.
At this point it would appear that eating too frequently (less than every three hours) has no real benefit, and could possibly be detrimental due to the muscle becoming insensitive to the impact of amino acids. It’s interesting to note the preliminary report above which found increased LBM gains with three versus six meals per day. Perhaps by spacing the meals further apart, greater stimulation of protein synthesis occurred when protein was eaten.
For the remainder of this chapter, I’ll take three hours to represent the minimum amount of time that should pass between meals. Eating more frequently is unlikely to be beneficial and may very well have a negative effect."
It’s not uncommon to read about bodybuilders or other athletes taking the eat-more-frequently dictum to extreme levels, eating every one to two hours. The idea behind this is the idea that optimal results should occur by maintaining a near continuous influx of nutrients into the body. I imagine if they could find a way to do it, some enterprising athletes would set up a continuous intravenous drip with carbohydrates, amino acids and essential fatty acids.
This may not be a good idea in the first place. Some research, primarily using amino acid infusion, suggests that skeletal muscle can become insensitive to further stimulation of protein synthesis. In one study, amino acids were infused for several hours to 70% over normal levels (17). Protein synthesis increased after roughly 30 minutes and was maintained for the next two hours at which point protein synthesis decreased back to baseline.
Importantly, this decrease occurred despite the maintenance of high levels of blood amino acids. Additionally, there was an increase in urea production (a waste product of protein metabolism), indicating that the excess AAs were simply being catabolized in the liver to be excreted in the urine; that is, those AAs were wasted and never utilized by the muscle.
The researchers took this as a suggestion that there might be a maximum amount of protein synthesis that can occur at any one given time before a “muscle full” situation is reached (18). Perhaps more interestingly, based on the amounts of AAs infused, the researchers estimated that only 3.5 grams of AAs would be required to result in this “muscle full” situation (18). I want to make it very clear that this doesn’t mean that 3.5 grams of orally ingested AAs would cause the same effect. Rather, this represented the delivery of 3.5 grams of AAs to the muscle itself.
However, the total amount of dietary protein to achieve this amount wouldn’t be huge. Most dietary proteins are roughly 40-50% EAAs, and due to processing in the liver, slightly less than half of the ingested AAs actually make it into the bloodstream. To provide 3.5 g EAAs to skeletal muscle would require roughly 15-20 grams of whole protein over a two hour time span.
Interestingly, other more direct research supports this value. In a study I described in an earlier chapter, subjects received doses of EAAs ranging from zero to 20 g EAAs and protein synthesis was studied (19). In young subjects, muscle protein synthesis was maximized with an intake of 10 g EAAs and there was no further increase with 20 g EAAs. This represents roughly 20-25 grams of whole protein.
Consumed every three waking hours (roughly six meals per day), this would allow for a maximum protein intake of 120 grams per day before skeletal muscle protein synthesis is maxed out. For a 100kg (220 pound) athlete, this is only 1.2 g/kg, lower than even the most conservative estimates discussed in Chapter 4. As discussed previously, this research is a difficult to reconcile with other, much higher recommendations or empirical results.
However, recall from Chapter 4 that dietary protein has more functions for athletes than simply the stimulation of protein synthesis. Although the amount described above might very well maximize skeletal muscle protein synthesis, optimizing the function of other important pathways of AA metabolism would very likely raise requirements even further (20). As well, while excess amino acids may simple be oxidized off, there is evidence that increased AA oxidation is involved in the overall “anabolic drive” of the body.
Finishing up this discussion, in their most recent study, the same group examined the effect on protein synthesis of a variety of doses of infused AAs (21). Infusing AAs at four different ranges, the group saw a similar pattern to their earlier work, an initial increase in protein synthesis followed by a return to baseline despite maintenance of high AA levels. Additionally, while the lower infusion rates caused a significant increase in protein synthesis, further increases at the higher concentration levels showed smaller additional benefits. Essentially, providing low to moderate amounts of AAs gave the greatest result.
Finally, and perhaps most interestingly, the paper demonstrated conclusively that it was extracellular AA concentrations (rather than the concentration of AAs inside the muscle cell) that were involved in stimulating protein synthesis. The researchers suggested the existence of some type of amino acid “sensor” in the muscle cell membrane that sensed AA levels. The study also suggested that it was the changes in extracellular AA concentration, rather than the absolute amounts that were driving the changes in protein synthesis. That is, it was the change from lower to higher that had the effect more than the absolute amount of AAs present.
Along with the indication of a “resistance” to further stimulation of protein synthesis, it appears that raising AA concentrations (after a meal) followed by a decrease in concentrations yield the best results. Basically, spacing meals apart and allowing blood AA levels to drop, rather than maintaining AA concentrations at continuously stable levels, appears to have the greatest impact on protein synthesis. Unfortunately, this still gives no indication of how far apart those meals need to be spaced to allow a “resensitization” of the muscle to a subsequent increase in AA concentrations.
Additionally, since it was based on an amino acid infusion, it’s unclear how this would relate exactly to the consumption of meals. Between digestion and the hormonal response that occurs with eating, it may very well be that eating protein would yield a different result than what the above research found using AA infusion.
In this vein, it’s interesting to look back at the original casein versus whey research that I discussed in Chapter 2. In that study, whey protein showed an initial spike in protein synthesis followed by an increase in amino acid oxidation in the liver, a pattern not dissimilar to the work examined above (22). It seems plausible that once whey had maximally stimulated protein synthesis, the remaining AAs were simply metabolized in the liver.
In contrast, when very small amounts of whey (a few grams at a time) were sipped over a six hour span to mimic the effects of casein, there was no increase in amino acid oxidation (23); however the impact on protein synthesis was also smaller. It may very well be that flooding the body with large amounts of AAs simply overloads the muscle’s ability to utilize amino acids, causing the excess to be burned off. This would also be consistent with the fact that the slower protein, casein, actually generated a higher overall gain in leucine in the body compared to whey; by never overloading the body’s protein synthetic machinery, overall better results were obtained.
Related to the above research, another group compared the body’s use of leucine with subjects either given small hourly meals or three separate meals (24). They found that protein oxidation was decreased (by 16%) in the group given three meals. Essentially, providing amino acids too frequently appears to decrease the body’s utilization of those aminos. Rather, having discrete meals where blood amino acid levels first increase (stimulating protein synthesis without overloading the body’s ability to utilize AA’s) and then decrease for some time (so that muscle can become “sensitive” to the effect of aminos again) would seem to be ideal.
At this point it would appear that eating too frequently (less than every three hours) has no real benefit, and could possibly be detrimental due to the muscle becoming insensitive to the impact of amino acids. It’s interesting to note the preliminary report above which found increased LBM gains with three versus six meals per day. Perhaps by spacing the meals further apart, greater stimulation of protein synthesis occurred when protein was eaten.
For the remainder of this chapter, I’ll take three hours to represent the minimum amount of time that should pass between meals. Eating more frequently is unlikely to be beneficial and may very well have a negative effect."
MaxBrenner
New member
Meal frequency and energy balance. [Br J Nutr. 1997] - PubMed result
Compared with nibbling, neither gorging nor a morn... [Int J Obes Relat Metab Disord. 2001] - PubMed result
Meal frequency and energy balance. [Br J Nutr. 1997] - PubMed result
Intermittent fasting does not affect whole-body glucose, lipid, or protein metabolism
Studies re: meal frequency.
Compared with nibbling, neither gorging nor a morn... [Int J Obes Relat Metab Disord. 2001] - PubMed result
Meal frequency and energy balance. [Br J Nutr. 1997] - PubMed result
Intermittent fasting does not affect whole-body glucose, lipid, or protein metabolism
Studies re: meal frequency.
IRON TANKS
Site Advertiser
Extremely important point from Aragon. I've seen this WAY too many times. It's dangerous.
MaxBrenner
New member
Had not seen that. But that hits the nail on the head! Much appreciate the find and post
Hmm, let's say you have a person who eats 250g of protein a day. If all of it is the fastest digesting protein, and digests at 10g/hour, it would take 25 hours to digest. But that means, only 240g would be digested per day.
So if he keeps eating 250g of protein every day... where will the extra 10g of protein each day go?
MaxBrenner
New member
Oh! It keeps building up over time and eventually his body can't store so much undigested food and his stomach bursts! Thanks.
MaxBrenner
New member
Hahahahaha yeah Bro.
No there is just a continual digestions process which leads to a continuation of storage and oxidation of nutrients.
Nothing stops after 24 hours.
I never said anything stops after 24h. Maybe you misunderstood me. Doesn't food need to be digested before it can be oxidized or stored?
MaxBrenner
New member
Yes that is correct (though some nutrients are oxidized during the digestion process so in all it starts there).
Yeah I'm guessing I've misunderstood you buddy
If you have eaten 250 grams of protein (all from whey) you will just have 25 hours of digesting etc going on. You don't lose it per se. Is that what you mean?