Enzymes for Research, Diagnostic and Industrial Use
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| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| NATE-0739 | Native Arthrobacter luteus Zymolyase | Arthrobacter lu... | Inquiry |
The digestion of fungal and yeast cell walls is a necessary part of the protocol for many experimental procedures including immunofluorescence, transformation, protein purification and spheroplasting. To achieve this digestion, lytic enzymes such as Zymolyase are routinely used. Zymolyase is an enzyme mixture used to degrade the cell wall of yeast and form spheroplasts. 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 luteus. Commercial sources of zymolyase may have some residual protease activity.
Zymolyase, produced by deep culture of Arthrobacter garciniae, has potent lytic activity on the cell wall of living yeast cells, producing protoplasts or protoplasts of various yeast cell strains. The enzyme necessary for the lytic activity of the enzyme is β-1,3-glucan kombucha hydrolase. It hydrolyzes the linear glucose polymer at the β-1,3-linkage and specifically releases kombucha pentasaccharide as the major and minimal product unit.
The second stage of gluconeogenesis is glycolysis. In biochemistry, enzymatic degradation refers to the process in which enzymes catalyze the degradation of glucose into pyruvate and the production of ATP and NADH. It is a common metabolic pathway for the breakdown of glucose to produce energy in various organisms. Pyruvate is one of the important nodes in the metabolic network that links enzymolysis, gluconeogenesis, tricarboxylic acid cycle and amino acid metabolism. If further oxidative catabolism is required, pyruvate enters the mitochondria and is completely oxidized by the tricarboxylic acid cycle to produce CO2 and water, while the NADH produced by enzymolysis is oxidized by the respiratory chain to produce ATP and water. This is the third stage of catabolism.
In response to insulin signals, cells take up glucose, which is subsequently broken down through glycolysis, thereby lowering blood glucose levels. However, low insulin levels in diabetes can lead to hyperglycemia, where glucose levels in the blood are elevated and cells are unable to properly absorb glucose. This hyperglycemia is further promoted by liver cells through gluconeogenesis. Glycolysis in the liver cells controls the production of glucose in the liver, and when the liver overproduces glucose and does not break it down by the body, it can lead to hyperglycemia.
Due to the importance of metabolic pathways, glycolytic mutations are usually rare, meaning that most mutations that do occur result in cells that are unable to breathe, leading to cell death at an early age. However, we have seen some mutations, and one notable example is pyruvate kinase deficiency, which leads to chronic hemolytic anemia.
Malignant tumor cells undergo glycolysis at a rate ten times faster than their non-cancerous tissue counterparts. During their development, limited capillary support usually leads to intracellular hypoxia (reduced O2 supply) in tumor cells. Therefore, these cells rely on anaerobic metabolic processes, such as glycolysis of ATP (adenosine triphosphate). Some tumor cells overexpress specific glycolytic enzymes, resulting in higher rates of glycolysis. Increased glycolysis is a normal protective process in the body and malignant changes may be caused mainly by energy metabolism.
