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2003/01/13, 02:17 PM
I just thought I'd post some of my favorite recipes, Enjoy........
High Protein Mac & Cheese
You'll need~
2tsp. flour
1 1/3 cups skim milk
8 oz. finely shredded fat-free sharp cheddar cheese
6 oz. finely shredded low-fat mozzarella cheese, divided
1/2 tsp salt
6 cups cooked macaroni (could try whole wheat if available)
Pam (butter-flavored)
*Preheat oven to 400 degrees.
Spray a casserole dish ('bout 8.5 x 11 or something close) w/ Pam (butter-flavored) then set aside
*In a small bowl mix flour w/ enough milk to form a paste, then continue to add milk until smooth (lump-free)
*Pour in a med saucepan along w/ the rest of the milk.
Add cheddar cheese, 3 oz. of the mozzarella and salt.
*Cook over med heat, stirring continuously, until the cheese is COMPLETELY melted and mixture starts ta thicken.
*When the mixture is smooth (no longer runny) remove from heat and pour over top of cooked macaroni which is in a casserole pan
*Sprinkle the rest (3 oz.) of the mozzarella on top.
*Bake on bottom rack for about 20-25 min once it's good 'n' bubbly.
Makes 6 servings:
Per serving~ 329 Cal 27g Protein 46g Carbs
3g Fat 3g Fiber
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2003/01/13, 02:26 PM
Hmmmm, I've never tried that, but I don't see why it wouldn't work.....although, some do believe that once protein powder is heated to a certain tempature, it loses it's protein?.?.?.
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2003/01/13, 02:42 PM
Thanks for the protein powder tip, I will try this now, if it has protein powder in it and wheat mac, he will eat it.
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I will lift my own weight someday!!!!!
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2003/01/13, 08:47 PM
I don't think the protien looses anything when it is heated.
One way to be sure is...think of all the food we cook, it still has a protien count. Just my thought.
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The trouble with jogging is that, by the time you realize you are not in shape for it, it is too far to walk back! Franklin P. Jones
Ivan Montreal Canada
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2003/01/13, 09:15 PM
I'm still on the fence w/ this one?.?.?.?
Oh, and I should have been more clear....I've heard the Whey protein breaks down when heated. Of-course I've read many different sides to this but here's a lil' something I found. ~
ß-lactoglobulins, (-lactalbumins, bovine serum albumin (BSA), and immunoglobulins (Ig) . These are known as whey proteins. These globular proteins are more water-soluble and acid-stable than caseins, but denature at temperatures above 170°F. Denaturation increases their water-holding capacity. The isoelectric point of the proteins covers a wide range, depending on the compound. The major whey protein, ß-lactoglobulin has an isoelectric point at about 5.4, making whey stable at lower pHs.
So in short, process of heating and Pasteurization, causes critical bonds holding the cystine together get broken down ("denatured", meaning they loose their original nature--similar to the denaturing and irreversible changing of liquid egg white by the heating process involved in frying an egg). The exact type of proteins that serve to increase tissue and serum glutathione most effectively are lost or diminished.
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2003/01/13, 09:20 PM
Good info. (Now I'm on the fence)! :)
I am really curious now, I will ask a well known Dr of chemistry and satisfy my mind. I'm really puzzled with that one.
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The trouble with jogging is that, by the time you realize you are not in shape for it, it is too far to walk back! Franklin P. Jones
Ivan Montreal Canada
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2003/01/14, 12:32 PM
Let us know what he says.
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2003/01/14, 06:10 PM
If you tune in on the net www.surfernet.com on cjad 800 am
between 10:30-noon. You will hear me. I will call DR. Joe Schwartz. .
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The trouble with jogging is that, by the time you realize you are not in shape for it, it is too far to walk back! Franklin P. Jones
Ivan Montreal Canada
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2003/01/15, 11:36 AM
Good discussion! I've been trying to find this out myself. I found this:
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Eggs are rich in protein, especially the egg whites. Protein is made up of strings of amino acids all joined together. When the protein is first made, these strings fold up on themselves. The way it folds up determines its chemical and biological properties. The protein is held in shape by cross-links between different parts of the amino acid string. When you cook an egg you break these cross-links, causing the proteins to unfold. This is called denaturing the protein.
You can denature protein in a variety of ways: with heat, mechanically, and by using chemicals. All these process work in slightly different ways but end up with the same result - 'cooked' egg. Here's how the different methods work:
Heat: All molecules are in constant motion. When the heat is turned up, the protein gains more vibrational energy and literally shakes the weak bonds (non-covalent) apart allowing the protein to unfold. At higher temperatures, the protein may be given enough energy to form new strong bonds (covalent) with other molecules in the food. Very high temperatures may also damage the amino acids that make up the protein, lowering the nutritional value of the food. Because heat effects all of the cross-links in the protein, it is the most effective way to cook an egg.
Mechanical Energy: Two things happen when you beat an egg. First the whipping has a tearing action on the protein, literally pulling it apart and denaturing it. Secondly, the surface tension at the surface of all the little bubbles also makes the protein unfold and denature.
Chemicals: The alcohol in the vodka disrupts weak bonds (hydrogen bonds) in the protein, whereas the acid in the vinegar breaks ionic bonds (a bit stronger). By mixing the two together you break both types of bond, which is a more effective way to denature protein. Many other chemicals denature protein either by interfering with internal cross-links or by breaking down the amino acids.
In all the above methods, we permanently denature proteins, which means that the protein does not return to its original folding. It doesn't matter how long you leave your well whipped egg white to settle it is not going to turn back into the raw egg.
But why does egg white turn solid when the protein is denatured? By unfolding the protein, the areas that were forming internal cross-links are now able to cross-link to their neighbouring protein. The proteins form an extensive network turning the egg white into a solid. The water that surrounded each protein molecule in the liquid egg white is squeezed out from between adjacent proteins as they cross-link. At first, the protein forms a sponge, which holds the displaced water. However, the protein network may become so cross-linked that it forces the water out altogether - this is what happens when you over-whisk egg white.
http://www.bbc.co.uk/science/scienceshack/backcat/experiments/maboiledeggs.shtml
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So does this mean that we glean no protein from a cooked egg? I wouldn't think so. Sounds to me like you still benefit from a denatured protein, so long as you don't heat it TOO much and damage the amino acids. You can bet I'm going to keep looking at this one.
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"Don't follow leaders and watch your parking meters!"
-- Bob Dylan
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2003/01/15, 12:08 PM
I also found this:
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Q. What happens to the protein if I Heat it? Freeze it? Blend it?
A. Any extreme heat (above ~140ºF), can denature protein (produce cross-linking) and reduce its solubility, digestibility and bio-availability.
Blending a protein solution (heat and foaming) can result in the denaturation of proteins, leading to a loss of solubility and biological functionality. However, the small amount of heat or foaming produced during preparation of a shake from a powder by blending in a household blender will not cause any damage to the proteins.
Freezing the protein shake immediately after preparing it, is perfectly acceptable. However, the protein shake must be ingested FROZEN, as the thawing process would break down it’s biological functionality.
As in everything…When in doubt, Call the manufacturer!
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The source isn't exactly scientific, but that sounds reasonable. *SIGH* I'm going to keep researching this, though.
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"Don't follow leaders and watch your parking meters!"
-- Bob Dylan
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2003/01/15, 07:11 PM
Good Info Mack.
Ok....I was at a food ingredient company today and met with my client in the confrence room. While discussing what I had to discuss, I noticed an easle over in the corner with protien written on it and its different sources!
Well My lights came on and I spoke to the chemist at this company.
She said there is no REAL answer for this, as it all depends on the manufacturer. She then asked me why i need to know, and I told her about this discussion. She said it all depends what the protien is used for, and they would make sure it does or doesn't break down under heat.In her case, the protiens that they have do not break down as they are specifacly for food ingredients. She said the only one who can answer that is the person in the lab who makes our protien powders. I will still ask the DR. Seems like we are getting somewhere.
Chicken and Turkey is heated above 140f and still has the protien. Makes me think, would it have more when it is raw?
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The trouble with jogging is that, by the time you realize you are not in shape for it, it is too far to walk back! Franklin P. Jones
Ivan Montreal Canada
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2003/01/17, 03:02 PM
I was wondering the same thing, carivan. There's protein in a ton of other foods that we eat, particularly meat, and I imagine that we're not destroying that protein when we cook it. I haven't yet found anything that expresses that any certain type of protein only denatures at 140 degrees, they all just say 'protein.' Perhaps it is only certain protein structures and animal proteins aren't included. The more I find out, the more questions I have.
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"Don't follow leaders and watch your parking meters!"
-- Bob Dylan
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2003/01/17, 06:32 PM
Perhaps the protiens that are found in yeast would breakdown, because of the nature of yeast.
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The trouble with jogging is that, by the time you realize you are not in shape for it, it is too far to walk back! Franklin P. Jones
Ivan Montreal Canada
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2003/01/18, 02:20 PM
Protein consists of chains of amino acids fixed together in a specific shape by side bonds and chains. When a protein is denatured its 3D shape is disrupted, it now cannot function in the manner it originally did, this is done in cooking food, the protein still exists only in a now biologically useless form.
However when we digest protein it is broken into polypeptides in our stomach and small intestine, and eventually into individual amino acids. So that it dose not matter if the protein has been denatured before eating as long as its constituent amino acids remain intact. I so although the protein might be denatures what we need is unaffected as I very much doubt we reach high enough temperatures to destroy amino acids in cooking.
For general interest there are just over 20 amino acids, three quarters of these are non-essential amino acids the remainder are essential. The difference been that the non-essential amino acids can be synthesized by humans, the essential amino acids cannot. So that we can get by with a slight deficiency in a nonessential amino acid as our body can replicate them. This dose mean that all protein sources are not the same, eggs are the best natural sources of all of the essential amino acids and why vegetarians often find problems having deficiencies (vegetables contain all essential amino acids but you need to match several incomplete sources to get then and so eat the right combination of vegetables). Whey powder is so popular as it comes form a dairy protein (another complete source), but in processing becomes an even better source than eggs.
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2003/01/21, 11:27 AM
Thanks for the info, erirvine! That puts my mind at ease.
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"Don't follow leaders and watch your parking meters!"
-- Bob Dylan
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