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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]
Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] 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 ...
[91]: 149–69 For example, in the response to insulin, the phosphorylation of multiple enzymes, including glycogen synthase, helps control the synthesis or degradation of glycogen and allows the cell to respond to changes in blood sugar. [92] Another example of post-translational modification is the cleavage of the polypeptide chain.
These enzymes have a variety of uses including degradation of plant materials (e.g., cellulases for degrading cellulose to glucose, which can be used for ethanol production), in the food industry (invertase for manufacture of invert sugar, amylase for production of maltodextrins), and in the paper and pulp industry (xylanases for removing ...
A degradative enzyme is an enzyme (in a broader sense a protein) which degrades biological molecules. Some examples of degradative enzymes: Lipase, which digests lipids, [1] Carbohydrases, which digest carbohydrates (e.g., sugars), [2] Proteases, which digest proteins, [3] [4] Nucleases, which digest nucleic acids.
Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.
It is the covalent attachment between the carbonil group of a reducing sugar (mainly glucose and fructose) and the amino acid side chain of the protein. In this process the intervention of an enzyme is not needed. It takes place across and close to the water channels and the protruding tubules. [21]
β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. [1] [2] Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase.