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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Microbial degradation of protein in the environment can be regulated by nutrient availability. For example, limitation for major elements in proteins (carbon, nitrogen, and sulfur) induces proteolytic activity in the fungus Neurospora crassa [5] as well as in of soil organism communities. [6] Proteins in cells are broken into amino acids.

  4. Maillard reaction - Wikipedia

    en.wikipedia.org/wiki/Maillard_reaction

    This can be discouraged by heating at a lower temperature, adding asparaginase, or injecting carbon dioxide. [5] In the cooking process, Maillard reactions can produce hundreds of different flavor compounds depending on the chemical constituents in the food, the temperature, the cooking time, and the presence of air.

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]

  6. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Many allergies are caused by the incorrect folding of some proteins because the immune system does not produce the antibodies for certain protein structures. [5] Denaturation of proteins is a process of transition from a folded to an unfolded state. It happens in cooking, burns, proteinopathies, and other contexts. Residual structure present ...

  7. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    For example, extremes of pH or temperature usually cause denaturation of all protein structure, but this is a non-specific effect. Similarly, some non-specific chemical treatments destroy protein structure: for example, heating in concentrated hydrochloric acid will hydrolyse the peptide bonds holding proteins together, releasing free amino acids.

  8. Proteinase K - Wikipedia

    en.wikipedia.org/wiki/Proteinase_K

    It is highly suited to this application since the enzyme is active in the presence of chemicals that denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is used for the destruction of proteins in cell lysates (tissue, cell culture cells) and for ...

  9. Dry heat sterilization - Wikipedia

    en.wikipedia.org/wiki/Dry_heat_sterilization

    The presence of moisture, such as in steam sterilization, significantly speeds up heat penetration. There are two types of hot air convection (Convection refers to the circulation of heated air within the chamber of the oven) sterilizers: Gravity convection; Mechanical convection