Search results
Results from the WOW.Com Content Network
A single Taq synthesizes about 60 nucleotides per second at 70 °C, 24 nucleotides/sec at 55 °C, 1.5 nucleotides/sec at 37 °C, and 0.25 nucleotides/sec at 22 °C. At temperatures above 90 °C, Taq demonstrates very little or no activity at all, but the enzyme itself does not denature and remains intact. [ 5 ]
Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%), [4] but cannot be synthesized by animal or human cells. [5] In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made.
The principle behind this test is to use enzymes native to the organism to create a colored product in the presence of foreign molecules. The chemical 5-bromo-4-chloro-3-indolyl-beta-D-galactoside is used in the test because N. lactamica can hydrolyze it with the production of β-galactosidase, turning the
Zymolyase (also known as lyticase, sometimes misspelled as Zymolase) is an enzyme mixture used to degrade the cell wall of yeast and form spheroplasts. [1] [2] Essential activities of zymolyase include β-1,3-glucan laminaripentao-hydrolase activity and β-1,3-glucanase activity. A common source of zymolyase is the Actinobacteria Arthrobacter ...
Plasmids are almost always purified from liquid bacteria cultures, usually E. coli, which have been transformed and isolated. [5] [6] Virtually all plasmid vectors in common use encode one or more antibiotic resistance genes as a selectable marker, for example a gene encoding ampicillin or kanamycin resistance, which allows bacteria that have been successfully transformed to multiply uninhibited.
The specific combination and concentrations of detergents, salts, and enzymes in lysing buffers can vary depending on the target enzyme, cell type, and experimental requirements, optimization of these components is crucial to achieve efficient cell lysis while preserving the stability and activity of the desired enzyme during the purification ...
Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. [2] Ureases are found in numerous bacteria, fungi, algae, plants, and some invertebrates, as well as in soils, as a soil enzyme. They are nickel-containing metalloenzymes of high molecular weight. [3]
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 ]