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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. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    Polyphenol oxidase is an enzyme found throughout the plant and animal kingdoms, [31] including most fruits and vegetables. [32] PPO has importance to the food industry because it catalyzes enzymatic browning when tissue is damaged from bruising, compression or indentations, making the produce less marketable and causing economic loss.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Non-homologous isofunctional enzymes. Unrelated enzymes that have the same enzymatic activity have been called non-homologous isofunctional enzymes. [24] Horizontal gene transfer may spread these genes to unrelated species, especially bacteria where they can replace endogenous genes of the same function, leading to hon-homologous gene displacement.

  5. Chaperonin - Wikipedia

    en.wikipedia.org/wiki/Chaperonin

    The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found. Each ~60kDa peptide chain can be divided into three domains, apical, intermediate, and equatorial. [4]

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Different enzymes have different specificity for their substrate; trypsin, for example, cleaves the peptide bond after a positively charged residue (arginine and lysine); chymotrypsin cleaves the bond after an aromatic residue (phenylalanine, tyrosine, and tryptophan); elastase cleaves the bond after a small non-polar residue such as alanine or ...

  8. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    It is most likely that the new allele will be non-functional—in which case it will probably result in low fitness and be removed from the population by natural selection. [ 5 ] Alternatively, if the amino acid residue that is changed is in a relatively unimportant part of the enzyme (e.g., a long way from the active site ), then the mutation ...

  9. Chemical process of decomposition - Wikipedia

    en.wikipedia.org/wiki/Chemical_process_of...

    Lipids in the body are mainly contained in adipose tissue, which is made up of about 5-30% water, 2-3% protein, and 60-85% lipids, by weight, of which 90-99% are triglycerides. [3] Adipose tissue is largely composed of neutral lipids, which collectively refers to triglycerides , diglyercides , phospholipids , and cholesterol esters , of which ...