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The manipulation of organisms in order to yield a specific product has many applications to the real world like the production of some antibiotics, vitamins, enzymes, amino acids, solvents, alcohol and daily products. Microorganisms play a big role in the industry, with multiple ways to be used.
An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and functions outside that cell. Exoenzymes are produced by both prokaryotic and eukaryotic cells and have been shown to be a crucial component of many biological processes. Most often these enzymes are involved in the breakdown of larger macromolecules.
Extracellular enzyme production supplements the direct uptake of nutrients by microorganisms and is linked to nutrient availability and environmental conditions. The varied chemical structure of organic matter requires a suite of extracellular enzymes to access the carbon and nutrients embedded in detritus .
Phage lytic enzymes produced during bacteriophage infection are responsible for the ability of these viruses to lyse bacterial cells. [2] Penicillin and related β-lactam antibiotics cause the death of bacteria through enzyme-mediated lysis that occurs after the drug causes the bacterium to form a defective cell wall. [3]
Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) [1] is a purification technique that utilizes the reduced solubility of certain molecules in a solution of very high ionic strength.
The first plant phytase was found in 1907 from rice bran [3] [4] and in 1908 from an animal (calf's liver and blood). [4] [5] In 1962 began the first attempt at commercializing phytases for animal feed nutrition enhancing purposes when International Minerals & Chemicals (IMC) studied over 2000 microorganisms to find the most suitable ones for phytase production.
According to the book, Enzymatic Mechanism, by Perry A. Frey and Dexter B. Northrop, Muconate lactonizing enzymes and Mandelate Racemase are both the member of enolase superfamily. Even though both the enzyme are different in their chemical reactions, they both have the same end product that leads to extracting a proton from an alpha carbon to ...
Within all 69 PETase-like enzymes, there exists the same three residues within the active site, suggesting that the catalytic mechanism is the same in all forms of PETase-like enzymes. [ 9 ] Surface of the PETase double mutant ( R 103 G and S 131 A ) with HEMT (1-(2-hydroxyethyl) 4-methyl terephthalate) bound to its active site .