Final answer:
Low temperature processing doesn't automatically guarantee a protein will be 100% bioavailable. Bioavailability is influenced by digestibility and absorbability, and while denaturation can affect a protein's function, denatured proteins can often still be digested and their amino acids used by the body.
Step-by-step explanation:
If a protein is low temperature processed, it does not necessarily mean it will be 100% bioavailable. Bioavailability is determined by the protein's ability to be digested, absorbed, and utilized in the body. Proteins with a higher biological value, such as animal proteins, tend to be more similar to human proteins, thus having higher digestibility and absorbability. For example, the biological values of egg and milk proteins are near 100% (94% and 96% respectively).
Protein denaturation can occur due to changes in temperature, pH, or exposure to chemicals. While denaturation sometimes affects the function of the protein, it is a process that often does not change the primary structure, and can potentially be reversible if the denaturing conditions are removed. However, some denaturation, such as the cooking of an egg white, results in irreversible loss of protein function.
It is important to note that proteins that have undergone denaturation are not necessarily rendered non-bioavailable. The enzymes in the digestive system can often still break down these proteins into amino acids, which can then be absorbed and used by the body. Therefore, whether a low temperature processed protein is 100% bioavailable depends on how it is processed and the nature of the protein itself.