It looks like you're using an Ad Blocker.
Please white-list or disable AboveTopSecret.com in your ad-blocking tool.
Some features of ATS will be disabled while you continue to use an ad-blocker.
Carbon monoxide keeps meat looking red longer
Shoppers who judge the freshness of meat by its color may be deceived by a relatively new industry practice of treating meat with carbon monoxide, critics say.
The meat industry defends the use of carbon monoxide to help meat retain its pink hue, saying large sums of money are wasted when sellers throw away meat that is still safe to eat but is not as attractive because it is slightly brown.
"Color is the number one indicator that's used" in selecting meat, said Don Berdahl, vice president of Kalsec Inc., a maker of natural food extracts in Kalamazoo, Michigan. In November, Kalsec filed a petition with the Food and Drug Administration seeking a ban on the use of carbon monoxide in meat packaging.
Nitrosamides are also used to keep meats red longer, especially hot dogs. Nitrosamides are chemicals specific granular lymphocytes (I want to cay it's neutrophils) use in your body. It's a carcinogen. Yum!
Originally posted by soficrow
I get properly aged meat from the family ranch - and there is a HUGE difference in taste from supermarket meat. Plus, supermarket meat gives me a stomache ache - but aged meat from the family farm does not.
Originally posted by Valhall
P.S. Follow-up pondering...and what does the CO do during cooking??? Does it interact with the chemicals of the meat and make something new? Does it get released? Do we get brain damage cooking CO injected meat? Could we all pass out and die if we had a huge in-door meat-fest cooking this stuff at the same time?
See, when I start wondering, I wonder big. I also wander big...but that's another personal problem we'll discuss else where.
Methods for rapid initiation of protein folding can be roughly classified into three categories: photochemical triggering, temperature or pressure jump, and ultrarapid mixing methods. The first fast-folding study employed a photochemical trigger: the photodissociation of carbon monoxide from denatured cytochrome c ( 17, 59). This experiment takes advantage of the fact that CO binds much more strongly to the heme of the denatured protein than to the heme of the native protein.
Basic Ideas of Fast-Folding Methods
Aside from its role in transporting oxygen to our tissues, a process critical to life, hemoglobin is a model system for understanding allostery. Allostery is a mechanism that regulates the function of many proteins by changing the shape of an active site on the protein when a ligand binds to another site. Hemoglobin is highly amenable to such studies, because it binds ligands such as carbon monoxide
Dynamics of Biomedical Molecules in Vision, Allostery, and Folding
...carbon monoxide, ...binds tightly to the heme and blocks formation of the native link between the Met80 sulfur and the heme iron
Protein Folding, Structure and Function
Absorption of a photon by myoglobin breaks a bond between the central iron atom and a carbon monoxide molecule, initiating a series of spectroscopic and structural changes, ultimately followed by rebinding of the carbon monoxide.
12 Experimental Techniques at Synchrotron Light Source Beamlines
The early work of Ansari et al.  showed the existence of “protein-quakes”, i.e. the cascading relaxation of myoglobin after the photodissociation of carbon monoxide. The protein-quake is an example of the wide-spread self-organized criticality phenomena [37, 38], where an increasing tension is met with a restricted relaxation.
Water and molecular chaperones act as weak links of protein folding networks: energy landscape and punctuated equilibrium changes point towards a game theory of proteins