Can you count the protein used to cook with?

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Why would you think it DOESN'T count?

Proteins are strings of amino acids. To digest them, the bonds between the amino acids have to be broken (hydrolyzed) to release the amino acids, which are then absorbed out of the intestine. The amino acids in the protein in your food are then reassembled into YOUR proteins.

When you cook proteins, they denature - which means that they are irreversibly transformed from the carefully folded versions which are biologically active (as enzymes or structural proteins) into "dead" versions. The amino acids still are bonded together, and need to be digested (hydrolyzed to amino acids) to be used - so while they are cooked/denatured, and thus "dead" in terms of their biological function, as FOOD, they are just the same as before being cooked in their value to you. Think of the "live" protein as a Rubik's cube when it is in the goal position (all the same color on each side), and a denatured protein as a cube after a bunch of random rotations - all the same pieces are there, but the protein won't "work" - it's dead. But the pieces are all still there - and since it is as separate pieces (the amino acids) that they are of any use to you, it does not matter whether the protein is raw (alive) or cooked (dead) - the value to YOU as food is in the digested/hydrolyzed amino acids the protein is made from, and is broken down to when you eat it.

So long as the protein powder you are adding is a complete protein (and not some collagen-based crap, which doesn't have a balanced assortment of the essential amino acids that the human body can't synthesize for itself), it doesn't matter if you're adding raw meat, cooked meat, protein powder, or amino acids (except that amino acids will be absorbed 100%, while proteins - which need pancreatic enzymes to digest/hydrolyze them completely - will be partially malabsorbed) - the value is all in the amino acids they are made up from.
 
Why not? I don't think the protein is destroyed by heat, we cook our meats and eggs.
 
Oops, I posted at the same time as Diana. Her scientific explanation is what I would have said if I were smart enough to verbalize it, lolol. :biggrin:
 
Thanks for the thorough explanation @DianaCox I read that cooking denatures protein and I didn't really understand what that meant. Thank you for taking the time to explain it so well.

BTW do you know if cooking with live/cultured products lessens the effectiveness? I cooked some buttermilk I had and wonder if it nullifies its effectiveness. TIA.

Why would you think it DOESN'T count?

Proteins are strings of amino acids. To digest them, the bonds between the amino acids have to be broken (hydrolyzed) to release the amino acids, which are then absorbed out of the intestine. The amino acids in the protein in your food are then reassembled into YOUR proteins.

When you cook proteins, they denature - which means that they are irreversibly transformed from the carefully folded versions which are biologically active (as enzymes or structural proteins) into "dead" versions. The amino acids still are bonded together, and need to be digested (hydrolyzed to amino acids) to be used - so while they are cooked/denatured, and thus "dead" in terms of their biological function, as FOOD, they are just the same as before being cooked in their value to you. Think of the "live" protein as a Rubik's cube when it is in the goal position (all the same color on each side), and a denatured protein as a cube after a bunch of random rotations - all the same pieces are there, but the protein won't "work" - it's dead. But the pieces are all still there - and since it is as separate pieces (the amino acids) that they are of any use to you, it does not matter whether the protein is raw (alive) or cooked (dead) - the value to YOU as food is in the digested/hydrolyzed amino acids the protein is made from, and is broken down to when you eat it.

So long as the protein powder you are adding is a complete protein (and not some collagen-based crap, which doesn't have a balanced assortment of the essential amino acids that the human body can't synthesize for itself), it doesn't matter if you're adding raw meat, cooked meat, protein powder, or amino acids (except that amino acids will be absorbed 100%, while proteins - which need pancreatic enzymes to digest/hydrolyze them completely - will be partially malabsorbed) - the value is all in the amino acids they are made up from.
 
Oops, I posted at the same time as Diana. Her scientific explanation is what I would have said if I were smart enough to verbalize it, lolol. :biggrin:
LOL, I wasn't sure when I read people saying that cooking protein powder denatures it... thanks to Diana I now understand that :)
 
BTW do you know if cooking with live/cultured products lessens the effectiveness? I cooked some buttermilk I had and wonder if it nullifies its effectiveness. TIA.

Different answer for this:

Using yogurt as an example, it is milk that has been fermented by microorganisms. It contains two sources of value to you as a food:
  • The proteins in the milk it's made from, MINUS the lactose sugar that the microorganisms have pre-digested for you to the acids that curdle (denature) the milk proteins and add the tangy flavor.
  • The microorganisms themselves, which are ALIVE and can help repopulate your gut bacteria and yeasts (your microbiome) with good bugs.
When you cook with yogurt (or any other fermented/cultured product that contains LIVE microorganisms that are part of the value of the product as a probiotic), you KILL the microorganisms, which therefore cannot reproduce in your gut anymore - they''re dead, Jim. The yogurt protein is still good for you (that's just a source of amino acids, once you eat it) and the elimination of lactose by the bacteria in the process of culturing the milk into yogurt is still helpful for making the milk proteins less problematic to ingest (because they are now lactose-reduced or -free), but if the good bugs are cooked, they do not have any additional value as a probiotic - which requires that the bugs be alive.
 
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Cooking with protein powder "denatures" the protein FURTHER - it is already denatured by drying it out.

The problem with cooking with protein powder as opposed to just mixing it in a cold or just warm drink, is that it can cause it to clump and get even more disgusting than when it is a powder that disperses more smoothly into the drink.

Think of the albumin from an egg: when it is raw, it is "smooth" and mixes easily with other fluids, but when you cook it or denature it with acid (think egg drop soup), it curdles - condenses into dense aggregated clots. It is still the intact protein. but in a different form. And it still needs to be digested to be used.
 
Diana how the hell do you retain all this shit in your head! It boggles my mind! I am lucky if I can remember what the date and day of the week it is! You and a few others on here are walking talking encyclopedias! Hell I had to spell check boogles and encyclopedia. It probably took me longer to form these few sentences that it did for you to type all that. Crap!!!!
 
Thanks for the thorough explanation @DianaCox I read that cooking denatures protein and I didn't really understand what that meant. Thank you for taking the time to explain it so well.

BTW do you know if cooking with live/cultured products lessens the effectiveness? I cooked some buttermilk I had and wonder if it nullifies its effectiveness. TIA.
Don't feel bad, I though the same thing in the beginning and never added powders to anything over 110 degrees. That was super annoying when I was on liquids and adding it to everything!
 
Barb - I'm a scientist. This comes to me as naturally as playing an instrument does to someone who has the gift for music. It's what I do.

But most of this is not that hard - it can be explained to a 10 year old, in simple terms.

Proteins (polypeptides) are made up of amino acids, like beads on a string.
447px-Protein_primary_structure.svg.png

The chemical bond between the amino acids (a peptide bond) can be broken by acid or far more efficiently by peptidases, enzymes made in the pancreas and to some extent in the lining of the intestine. The individual amino acids can be absorbed through the intestinal wall, to get carried to the cells to make your own proteins.

A similar situation applies to carbs, which are chains of sugars.
carbohydrate-diagram.jpg


Ditto fats - although the situation is a little more complicated, because there are two main kinds of fats - linear chains of fatty acids carried on a glycerol backbone called triglycerides (three fatty acid chains per glycerol),
300px-Fat_triglyceride_shorthand_formula.PNG

and more complicated multi-ring versions which make up the sterols, which include cholesterol and all the steroid hormones that have a sterol structure, including bile acids and vitamin D
535px-Sterol_synthesis.svg.png
.


And the basic unit of all of this is the carbon, hydrogen and oxygen structure acetyl-CoA, which ALL of the above structures taken in as food can be broken down to, and then used to build almost everything else from scratch:
Catabolism (breaking things down to the smallest units, plus "charging the biological energy battery" molecule, i.e., synthesizing ATP):
425px-Catabolism_schematic.svg.png

(see next post)
 
(No more than 5 images allowed per post - and dammit, I had to redo what I tried to move.)

Anabolism is the process of synthesizing the bigger molecules (proteins, carbohydrates and fats, as well as nucleic acids (not shown) from the basic units, with the energy of the synthetic process being driven by the energy stored in the catabolic processes in ATP molecules:
590metabolism.gif


Although this simplified drawing doesn't show it, the amino acids from protein are about half essential amino acids (humans can't synthesize them ourselves, and they have to be provided as amino acids from our food; the other half, we can break down all the way and resynthesize from acetyl-CoA plus nitrogen. But importantly, notice that EXCESS protein gets converted to FAT: see the yellow arrow from the nitrogen pool to acetyl-CoA to the pink arrow to lipogenesis to fat.

This simplified drawing also doesn't show the relatively minor biosynthetic pathway by which acetyl-CoA can be used to make sugar and carbohydrates (e.g., glycogen), if we don't eat carbs (contrary to what many NUTs try to argue). This process is what maintains our blood sugar and replenishes our glycogen stores in our muscles (see the description of stalls I wrote) when we are at a calorie deficit.
 
Note how the process is somewhat like how an economy works, in that ATP is like energy currency.

It generally requires energy to force two molecules to react (to make two amino acids link together) because Nature prefers randomness rather than structure. ATP (adenosine triphosphate) stores a lot of energy in the bond between the second and third phosphate group when it is synthesized - when you break that bond to form ADP (adenosine diphosphate) and a phosphoric acid, energy is given off that can be used to drive a reaction that has to be "forced" to happen, usually making a bigger or more highly ordered molecule from a simpler one.

So, what happens when you break down bigger molecules to smaller ones, is that these kinds of reactions happen with the help of an enzyme that ties the breaking of a chemical bond from the bigger molecule (like the starch to a sugar, or a protein to an amino acid), to driving the synthesis of a molecule of ATP from ADP - pretty much conserving the energy that was used to make the bigger molecule in the ATP molecule. Then that ATP molecule can be used anywhere in the cell to drive a synthetic reaction that needs energy to make it happen.

The acetyl-CoA is kind of like a very small brick (it is a 2 carbon unit with an oxygen and 3 hydrogens) that can be used in many many biosynthetic reactions to build larger molecules, including sugars, fats, and proteins.

In the bigger picture, acetyl-CoA can also be fully catabolized down to carbon dioxide and water, to capture extra energy in the form of ATPs. And - to complete the cycle, all of this energy ultimately comes from the sun: photosynthesis is the process by which energy from the sun is used to - yes, you guessed it! - capture carbon dioxide from the air, to produce small carbon building block molecules inside plants, which use them to make sugars, starches, fats and protein (as well as giving off a portion of the dioxide as oxygen):
484px-Simple_photosynthesis_overview.svg.png

799px-Photosynthesis_equation.svg.png

And that's pretty much summarizes the biology of metabolism.
 
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