"Incineration is possible, but it isn't as easy as burning the carcass in a fire. Temperatures of more than 1,100 degrees Fahrenheit — sometimes up to 1,800 degrees — are required to effectively neutralize prions. Unlike most bacteria, regular cooking won't help at all.
"Disposal issues are tough," says Barbara Powers, director of Colorado State University's Veterinary Diagnostic Laboratory."
No. You have to denature the protein to reduce the infectivity.
You need about 20 minutes, a pressurized autoclave, and some nasty chemicals to do this effectively. There is research into other methods but I really don't know anything about them.
Proteins aren't destroyed by cooking. Otherwise you would not be able to get any proteins from cooked meat or beans.
The only reliable method that I'm aware of to denature proteins without making the whole thing inedible is hydrolysis. Gelatin is made from collagen in the skin, bones, and connective tissues of various animals, but Jell-O is generally considered safe.
> Proteins aren't destroyed by cooking. Otherwise you would not be able to get any proteins from cooked meat or beans.
"Protein" in food really means "amino acids" as far as nutrition is concerned; even if the protein isn't denatured by cooking (and at least some proteins are), it will be broken down to amino acids by your digestive system before being absorbed into your body. Your body uses the amino acids to build its own proteins.
IIRC quite a few animal-source protein strings that are "fully compatible" with our own ('animal') bodies are taken up as-is without breakdown into AA and resynthesis into "human protein". Much more efficient.
"Proteins ingested in the diet are digested into amino acids or small peptides that can be absorbed by the intestine and transported in the blood."
If by "animal-source protein strings" you mean "small peptides", then yes. But in general they still have to be resynthesized into the proteins used by the body. There might be a few useful proteins that are small enough to fall into the "small peptide" range and would therefore be absorbed and used as-is.
Prions have a little over 200 amino acids, so they are on the large side to be considered "small peptides" (which AFAIK are typically a few to a couple of dozen amino acids). They appear to be resistant to the enzymes that normally digest proteins, and it doesn't appear to be clearly understood how they get from the digestive tract into the bloodstream. See, for example, here:
"Denaturing" means to make the protein take on a different shape, which is all that is necessary (since a prion is the correct amino acids arranged in a pathological arrangement). You can denature proteins with heat or very high or low pH, depending on which protein that it is.
But the dangerous part of a prion is the way it's folded, right? All you have to do is denature it to render it harmless. It's just harder to do for some proteins than others.
"Incineration is possible, but it isn't as easy as burning the carcass in a fire. Temperatures of more than 1,100 degrees Fahrenheit — sometimes up to 1,800 degrees — are required to effectively neutralize prions. Unlike most bacteria, regular cooking won't help at all. "Disposal issues are tough," says Barbara Powers, director of Colorado State University's Veterinary Diagnostic Laboratory."