The Consequences Of Cheese As A Main Source Of Protein

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Amazoniac

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:handpointup:

"The two formulae used were casein predominant and therefore reasonably low in cysteine. Thus, the supplementation with taurine may have a cysteine-sparing effect and make more cysteine available for protein synthesis, thereby decreasing the necessity for increased endogenous protein breakdown."

This is in line with what has been discussed before.
 

bistecca

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A few questions, sorry if I missed the answers..

Do different animals produce dairy with differing levels of casein?

Is there evidence that an animal's diet influences proportion of casein?

Is there an evolutionary benefit or role to casein with respect to it's function in the dairy-producing species?
Opioid-like qualities sedating young and keeping them off the radar of predators? Promoting immune function at a time when it's most important to simply stay alive rather than grow quickly?
 
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Amazoniac

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A few questions, sorry if I missed the answers..

[1] Do different animals produce dairy with differing levels of casein?

[2] Is there evidence that an animal's diet influences proportion of casein?

[3] Is there an evolutionary benefit or role to casein with respect to it's function in the dairy-producing species?
Opioid-like qualities sedating young and keeping them off the radar of predators? Promoting immune function at a time when it's most important to simply stay alive rather than grow quickly?
[1] Yes, that is one of the problems that appear from giving utter instead of breast milk to infants.

Determine%20the%20Quantity%20of%20Casein.jpg

Stolen from here, I'm not sure if it's reliable.​

[2] I remember Trawis posting something about the changes in milk composition depending on the time of the day that it was collected (also not sure if the protein content varies), it wouldn't surprise me if the protein content changes.


[3] They must have an useful purpose. Have you readed this?


--
@paymanz, you made a good point on a previous page, about good digestibility of caseid in general. But if this was always the case, people wouldn't have issues with it, some are clearly due to casein and not other components.

Regarding binding of minerals, I don't know if this has any effect when the casein has been coagulated outside of the body (away from the meal). Either way, it must not affect the rest of the meals, so it shouldn't be too concerning.

These might interest you:

- Cow’s Milk: a Food and a Potential Source of Allergens

"Caseins exist primarily as calcium phosphate stabilised micellar complexes. The casein fraction comprises predominately four proteins (as1, as2, b and k caseins) with little primary structure homology. Caseins contain no disulfide bounds and possess an unusually high content of proline residues which cause particular ‘bending’ of proteins chains and inhibit the formation of a close-packed, ordered secondary structure. Since they do not contain any tertiary structure there is considerable exposure of hydrophobic residues. Casein micelles function as a carrier for a large amount of highly insoluble Ca (more than 85%) and P and enhance their bioavailability in intestinal absorption by keeping them soluble and preventing precipitation (Hoffman and Falvo 2004)."​

- Potential Uses of Caseinophosphopeptides [:moneybag:]

"The term phosphopeptide (CPP) appears to have been first introduced by Mellander in 1950 to describe caseinderived phosphorylated peptides which enhanced vitamin D independent bone calcification in rachitic infants. Since then CPPs have been shown to possess the unique property of being able to bind macroelements such as Ca, Mg and Fe along with trace elements such as Zn, Ba, Cr, Ni, Co and Se. Milk and dairy products are an excellent source of Ca2+ and it is thought that CPPs produced during the digestion of caseins enhance the bioavailability of Ca2+ in the diet speciÞcally by increasing the solubility of Ca2+ in the alkaline environment of the small intestine where maximal passive absorption of dietary Ca2+ is thought to take place. CPPs have been produced in vitro following digestion of casein mainly with pancreatic enzymes. Analysis of the intestinal chyme of rats and minipigs has also shown that CPPs are formed during casein digestion in vivo (Naito et al., 1972; Meisel and Frister, 1988) and they have also been found in fermented dairy products such as cheese (Pause and Lembke, 1993; Roudot-Algaron et al., 1994). CPPs can arise from as1-, as2- and b-casein."

"The caseins can be subdivided into four types, i.e. as1-, as2-, b- and k-casein, a classification initially based on their different mobilities during electrophoresis in alkaline urea polyacrylamide gels. Phosphorous is bound to the caseins via monoester linkages to seryl residues. The extent of phosphorylation is dependent on casein type, i.e. bovine a42-casein can have up to 13 phosphate groups, whereas i-casein has only one phosphate (for reviews see West, 1986; Reynolds, 1994). The sequences of the different CPPs found in bovine milk are shown in Fig. 1. It is apparent that many of these contain a common motif, i.e. a sequence of three phosphoseryl followed by two glutamic acid residues. These highly polar acidic domains represent the binding sites for minerals."

"As previously stated, milk and dairy products are excellent sources of Ca2+ and in Western society, milk and dairy products supply over 75% of the recommended daily allowance for Ca2+ (Buttriss, 1990). The excellent bioavailability of Ca2+ from milk has been attributed to phosphopeptide mediated enhanced solubility of Ca2+ in the small intestine (Gammelgaard- Larsen, 1991; Kitts and Yuan, 1992; Schaafsma, 1997). CPPs are formed in vivo following digestion of casein by gastrointestinal proteinases (Naito et al., 1972; Sato et al., 1983; Meisel and Frister, 1988). CPPs are relatively resistant to further proteolytic degradation (Hirayama et al. 1992; Kasai et al., 1992, 1995) and can accumulate in the distal ileum (Naito et al., 1972; Naito and Suzuki, 1974; Lee et al., 1980; Meisel and Frister, 1988). They form soluble complexes with Ca2+ phosphate at alkaline pH in vitro (Reeves and Latour, 1958; Sato et al., 1991; Ono et al., 1994; Holt et al., 1996). It has been proposed that these CPP/Ca2+ complexes can lead to enhanced Ca2+ absorption across the intestinal mucosa by limiting the precipitation of Ca2+ in the distal ileum (Lee et al., 1980, 1983; Mykannen and Wasserman, 1980; Meisel and Frister, 1988; Li et al., 1989a, b; West, 1990; Kitts and Yuan, 1992; Kitts et al., 1992a)."

"There are three modes of Ca2+ absorption in man, i.e. a saturable, vitamin D-dependent transport system located in the duodenum and jejunum and a passive, vitamin D-independent system located in the ileum and the distal small intestine (Bronner, 1987). It is thought that the passive transport route is the major mode of Ca2+ absorption from the diet (Schaafsma, 1997). A pinocytotic system for mineral absorption also exists, this system, though present in adults, is thought important in mineral absorption in infants (Walker and Isselbacher, 1974). Several factors affect the absorption of Ca2+ from the diet including phytate, oxalate, phenol compounds, lactose, phosphorus and obviously vitamin D. Phytate, as present in many non-reÞned cereals and legumes, forms insoluble or poorly soluble complexes with Ca2+ at intestinal pH (Rossander et al., 1992; Schaafsma, 1997)."

"While numerous animal studies are available on the effect of CPPs on mineral bioavailability, very little information is available from human studies. However, it has been demonstrated that CPPs increase Ca2+ and Zn2+ absorption from a rice-based infant gruel in human adults by approximately 30%. No e¤ect was seen when CPPs were ingested in either high or low phytate whole-grain cereal meals (Hansen, 1995). These results serve to emphasise the complex interactions between meal constituents and mineral bioavailability (Rossander et al., 1992). The above Þndings are of signiÞcance to inhabitants in the Eastern Pacific who have rice-based diets containing little or very low quantities of dairy products."​

- The study of zinc ions binding to casein
- Binding of zinc to bovine and human milk proteins
- Intestinal absorption of calcium in rats given diets containing casein or amino acid mixture: the role of casein phosphopeptides
 
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LAB Fermentation appears to be the most effective method for rendering milk peptides hypoallergenic...

Milk processing as a tool to reduce cow’s milk allergenicity: a mini-review

Health-Promoting Properties of Lactobacillus helveticus

Lactobacillus helveticus : "Lactobacillus helveticus is a lactic-acid producing, rod-shaped bacterium of the genus Lactobacillus. It is most commonly used in the production of American Swiss cheese and Emmental cheese, but is also sometimes used in making other styles of cheese, such as Cheddar, Parmesan, Romano, provolone, and mozzarella."
This green lights cheese in my book.

FWIW Whey has given me no problems, and i get the cheapest WP concentrate, all i did was stop supping niacin cuz the tryptophan
 
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Amazoniac

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My experiences with casein aren't great in general, but I have reasons to believe that issues with it can be eased or eliminated with adequate nutrition.

It's a more anabolic than other proteins. I can feel my teeth realigning every time I eat it, they start to press against each other before adjusting. The first time that I eat the effect is usually marked, and then it starts to fade away on consecutive consumptions. There are two ways that I can recover the effect: by not consuming for a while and letting the body fill up the reserves of whatever got depleted [citation needed] or by getting extra nutrition.

What's more interesting is that, as such effect fades away,* the detrimental start to appear.
Sometimes it's difficult to return to the original strength without a break (but it gets Janelle close), which probably means that there are still unidentified factors.
*Apologies for the elitist (Saturazione, 2017) commas, it was confusing without them.
 
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My experiences with casein aren't great in general, but I have reasons to believe that issues with it can be eased or eliminated with adequate nutrition.

It's a more anabolic than other proteins. I can feel my teeth realigning every time I eat it, they start to press against each other before adjusting. The first time that I eat the effect is usually marked, and then it starts to fade away on consecutive consumptions. There are two ways that I can recover the effect: by not consuming for a while and letting the body fill up the reserves of whatever got depleted [citation needed] or by getting extra nutrition.

What's more interesting is that, as such effect fades away,* the detrimental start to appear.
Sometimes it's difficult to return to the original strength without a break (but it gets Janelle close), which probably means that there are still unidentified factors.
*Apologies for the elitist (Saturazione, 2017) commas, it was confusing without them.
Just curious, what kind of casein are you talking about? Milk, cheese, casein powder?
 
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Amazoniac

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Just curious, what kind of casein are you talking about? Milk, cheese, casein powder?
:wave:

Not many forms, only these. But really: cheese, yogurt, milch, and so on, except for powders. The effect is milder with milch but probably because the protein is less concentrated and there are other confounding factors. I haven't been able to identify if the remaining part that's between how far I'm able to correct and the original effect, is from the common inconveniences with the nature of casein.
 
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Using these..
..I got the following averages per liter of whole milk:
  • Vitamin A - 1100 IU
  • Vitamin D - 45 IU*
  • Vitamin E - 1.6 IU
  • Calcium - 1200 mg
  • Magnesium - 120 mg
*Animal products contain both: the 25(OH)D form, which is the form produced by the liver from the vitamin D3 form. The first one is more potent which makes it more effective in raising blood vit D levels with the same amount; they suggest it's up to 5x stronger, I have used 4x for calculation and joined the forms.​
  • Vitamin A/D - 25:1
  • Vitamin A/E - Error
The content can vary a lot for the same reason that our status of these nutrients does.

It's obligatory to fortify defatted milk with (also per liter):
  • Vitamin A - 2100-3150 IU
  • Vitamin D - 420-630 IU
:nailbiting:
 

Wagner83

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Damn, vitamin a and d are pre-mixed with polysorbate, pufas oil (insignificant amount?), and the light sensitivity of riboflavin appears to be a big issue. The vitamin d is made from irradiation of lanolin, I wonder how good that is. I also wonder how vitamin a dispersion in water affects its use by the body.
 
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It's a burden that healthy kidneys can manage, but having them compromised can make you more susceptible to the effect:

- Dietary protein causes a decline in the glomerular filtration rate of theremnant kidney mediated by metabolic acidosis and endothelin receptors

"Increased dietary intake of protein as casein induces kidney injury in rats with intact nephron mass mediated by increased intrinsic acid production through endothelin A receptors.[one] Nevertheless, glomerular filtration rate (GFR) was preserved after nearly 2 years of follow-up.[one] By contrast, increased intake of dietary casein in rats with reduced nephron mass induces kidney injury as well as reduces GFR,[two] each of which is ameliorated by reduced dietary casein intake.[three] Dietary casein increases intrinsic acid production[four] and high-protein diet as casein induces endothelin-mediated kidney acidification that facilitates acid excretion.[five until seven] Endothelin has been implicated as a mediator of glomerulosclerosis[eight] and tubulo-interstitial injury,[one and nine] and so might contribute to kidney injury associated with dietary casein. On the other hand, dietary protein as soy induces less intrinsic acid production than casein[four] and is associated with less injury in remnant kidneys.[ten] Animals with reduced nephron mass might be more susceptible to casein-induced kidney injury, because this acid load is more likely associated with chronic metabolic acidosis in these animals[eleven] than in those with intact nephron mass.[twelve] Male Munich–Wistar rats are at higher risk for kidney injury than other strains,[thirteen] and it was in this strain that dietary protein-induced, endothelin-mediated augmented kidney acidification was shown.[five until seven]"

"Dietary casein increases intrinsic acid production but soy does not,[four] related in part to its higher methionine content. Consequently, dietary casein provides a greater acid challenge than soy. Casein Nx [group that underwent surgery to compromise kidneys] appears to have less capacity than Casein sham to excrete the acid load induced by dietary casein without maintaining a sustained metabolic acidosis. By contrast, the reduced nephron mass of Nx appears sufficient to maintain comparable acid–base status in Soy Nx and Soy sham with the lower acid challenge provided by the soy diet."

"Previous studies also showed that dietary acid increased kidney endothelin production in animals with intact nephron mass but did so without the animals developing sustained metabolic acidosis.[twelve] In this study, dietary acid increased urine endothelin production in Soy Nx that did develop sustained metabolic acidosis. These data support that dietary casein increases kidney endothelin production through increased intrinsic acid production with or without sustained metabolic acidosis. Increased kidney endothelins, in turn, appear to induce kidney injury through endothelin A receptors as described in animals with intact nephron mass.[one] In contrast to animals with intact nephron mass in which GFR was preserved up to 96 weeks, this study supports that this mechanism contributes to progressive GFR decline in Nx over 12 weeks. The reasons for this difference were not apparent, but the ability of animals with intact nephron mass to excrete the dietary acid challenge without developing metabolic acidosis, in contrast to the Nx animals, might be contributory."

"Supplemental dietary NaHCO3, but not NaCl, reduces intrinsic acid production in animals eating dietary casein.[fifteen]"​

- Late metabolic acidosis and poor weight gain in moderately pre-term babies fed with a casein-predominant formula: a continuing need for caution

"This study of 70 healthy, moderately preterm (32–35 weeks) Chinese babies has convincingly shown that a casein-predominant low protein formula is associated with significant metabolic acidosis, persisting sometimes for as long as 8 weeks, and poor weight gain when compared with infants fed on either a humanized or a special low-birthweight formula."​

- Metabolic Acidosis after Hyperalimentation with Casein Hydrolysate: Occurrence in a Starved Patient
- Goat milk acidosis

The remaining lactic acid in strained yogurts must not be concerning or it would be unpalatable. But speaking of straining, the strains of bacteria used can affect its composition; either way it doesn't help any in the issue.

The use of potassium citrate along with casein consumption was tried in a publication somewhere in this thread.
 

Kartoffel

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Dietary casein increases intrinsic acid production but soy does not,[four] related in part to its higher methionine content. Consequently, dietary casein provides a greater acid challenge than soy.

Babies all around the world will be devastated to read this. Since whey and casein contain about the same amount of methionine, they will all soon suffer from acidosis, if they don't substitute their mother's milk for healthy soy products with less methionine.
 
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Babies all around the world will be devastated to read this. Since whey and casein contain about the same amount of methionine, they will all soon suffer from acidosis, if they don't substitute their mother's milk for healthy soy products with less methionine.
Not as much as when they find out that their milk is being stolen, processed in a way that concentrates protein and sometimes fat, B-vitamins are wasted, minerals also being eliminated and replaced with sodium chloride. Everything against what was intended to prevent such issues.
 
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Kartoffel

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Not as much as when they find out that their milk is being stolen, processed in a way that concentrates protein and sometimes fat, B-vitamins are wasted, minerals also being eliminated and replaced with sodium chloride.

No formula is good for babies, but I guess any cow's or goat's milk formula will be better than soy-based garbage. I just wanted to point out that calling casein formula bad on the basis of its' methionine content is stupid because natural human milk will contain just as much methionine.
 

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Not as much as when they find out that their milk is being stolen, processed in a way that concentrates protein and sometimes fat, B-vitamins are wasted, minerals also being eliminated and replaced with sodium chloride. Everything against what was intended to prevent such issues.
Formula is an abomination. That is very correct! I still love cheese :p:
 
EMF Mitigation - Flush Niacin - Big 5 Minerals

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