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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.
Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.
in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...
The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis–Menten constant (K m), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic K M for a given substrate.
The first assumption is the so-called quasi-steady-state assumption (or pseudo-steady-state hypothesis), namely that the concentration of the substrate-bound enzyme (and hence also the unbound enzyme) changes much more slowly than those of the product and substrate and thus the change over time of the complex can be set to zero [] / =!.
Enzymes catalyze chemical reactions involving the substrate(s). In the case of a single substrate, the substrate bonds with the enzyme active site, and an enzyme-substrate complex is formed. The substrate is transformed into one or more products, which are then released from the active site. The active site is then free to accept another ...
Glucose oxidase enzyme powder from Aspergillus niger. GOx is a dimeric protein, the 3D structure of which has been elucidated. The active site where glucose binds is in a deep pocket. The enzyme, like many proteins that act outside of cells, is covered with carbohydrate chains. GOx is a glucose oxidising enzyme with a molecular weight of 160 kDa.
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.