Uma, L; Kalaiselvi, R; Subramanian, G., 1994: Isolation of a lignolytic bacterium for the degradation and possible utilization of coir waste. Biotechnology letters 16(3): 303-308 Coir, fibre of coconut used for making ropes results in the accumulation of huge quantities of lignin waste. Enrichment technique yielded a lignin a degrading bacterium characterized as Pseudomonas sp. [...]
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Oxidase 
In biochemistry, an oxidase is any kind of enzyme that brings about an oxidation-reduction reaction involving the oxygen molecule as the electron receptor. There are many kinds of oxidases, including the cytochrome c oxidase, an essential enzyme that allows a living body to use oxygen in the generation of energy. The cytochrome c oxidase is also the final component of the electron transfer chain.
The glucose oxidase is an oxido-reductase enzyme that brings about the oxidation of glucose to hydrogen peroxide and glucono delta-lactone. In living cells, glucose oxidase helps in breaking sugar molecules down into its metabolites. This enzyme is widely used for determining the free glucose in body fluids, as well as in the food industry. Glucose oxidase is also an important substance in various fields of biotechnologies, biochemistry, and even nanotechnologies.
Monoamine oxidases, on the other hand, are a family of enzymes that bring about the oxidation of monoamines. They are typically bound to the outer memberane of mitochondria in just about any cell type in the body. This enzyme was discovered by the British biochemist Mary Bernheim in the liver and she named it tyramine oxidase.
Xanthine oxidase is basically a form of xanthine oxidoreductase, an enzyme that produces reactive oxygen species. It brings about the oxidation of hypoxanthine into xanthine, and pushes the catalyzing process further into oxidizing xanthine to uric acid. Xanthine oxidase has an essential role in the catabolism of purines in many species, including humans.
In the study of microbiogy, oxidases are used in the oxidase test, which is instrumental in the phenotypic characteristic for the identification of a variety of bacterial strains. The oxidase test also determines whether a specific bacterium sample produces cytochrome oxidases, and can therefore use oxygen with an electron transfer chain.
This category contains scientific information on oxidase, any kind of enzyme that brings about an oxidation-reduction reaction with an oxygen molecule as the electron receptor.
Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants
Smith, Ag; Marsh, O; Elder, Gh, 1993: Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochemical journal, 292(2): 503-508 The subcellular location of two enzymes in the biosynthetic pathway for protoporphyrin Ix, coproporphyrinogen (coprogen) oxidase (Ec 1.3.3.3) and protoporphyrinogen (protogen) oxidase (Ec 1.3.3.4) has been investigated in etiolated pea [...]
Interactive potential of omega-3 fatty acids with clofibrate or DEHP on hepatic peroxisome proliferation in male Wistar rats
Wysynski, Anna Marie; Baldwin, Linda A.; Leonard, Denise A.; Calabrese, Edward J., 1993: Interactive potential of omega-3 fatty acids with clofibrate or DEHP on hepatic peroxisome proliferation in male Wistar rats. Human & Experimental Toxicology. 12(4): 337-340 The interactive potential of three known peroxisome proliferators, omega-3 fatty acids, clofibrate and di(2-ethylhexylphthalate (Dehp), was evaluated in [...]
Influence of exogenous hormones on the growth and secondary metabolite formation in transformed root cultures
“Rhodes, M. J. C.; Parr, A. J.; Giulietti, A.; Aird, E. L. H., 1994: Influence of exogenous hormones on the growth and secondary metabolite formation in transformed root cultures. Plant Cell Tissue & Organ Culture. 38(2-3): 143-151 Transformed organ cultures formed following transformation of plant tissues with Agrobacterium species owe their phenotypes to alterations in [...]
Influence of CO2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seedlings
Finlayson, S. A.; Reid, D. M., 1994: Influence of CO2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seedlings. Phytochemistry 35(4): 847-851 The activity of the ethylene forming enzyme Acc oxidase was assayed in vitro under aerobic conditions with and without high levels of exogenous Co2, varying the parameters of ascorbate, pH, temperature, [...]
In vitro activation of grape polyphenol oxidase by polyglucan type elicitors
Jimenez, Mercedes; Garcia Carmona, Francisco, 1993: In vitro activation of grape polyphenol oxidase by polyglucan type elicitors. Plant Physiology & Biochemistry (montrouge). 31(4): 541-546 Latent polyphenol oxidase, extracted and partially purified from grapevine (Vitis vinifera L. cv. Gamay) cell suspension cultures, was shown to be activated by the polyglucans zymosan and chitosan. Activation increased with [...]
Immunochemical and immunohistochemical study of apple chlorogenic acid oxidase
Murata, Masatsune; Kurokami, Chiyo; Homma, Seiichi; Matsuhashi, Choku, 1993: Immunochemical and immunohistochemical study of apple chlorogenic acid oxidase. Journal Of Agricultural & Food Chemistry. 41(9): 1385-1390 Mouse antibody was raised against chlorogenic acid oxidase from apple (Malus pumila cv. Fuji). This antiserum was used for immunochemical characterization of the enzyme of apple and other plants [...]
Identification and characterization of an auxin-degrading enzyme in downy mildew infected sunflower
Benz, A.; Spring, O., 1995: Identification and characterization of an auxin-degrading enzyme in downy mildew infected sunflower. Physiological & Molecular Plant Pathology. 46(3): 163-175 An auxin-metabolizing enzyme was purified from growth-retarded sunflower plants (Helianthus annuus L.) infected with downy mildew (Plasmopara halstedii (Far).) Berl. et de Toni) by means of differential centrifugation, salt precipitation and [...]
Hydrogen-peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase
Guillen, F; Martinez, At; Martinez, Mj; Evans, Cs, 1994: Hydrogen-peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase. Applied microbiology and biotechnology 41(4): 465-470 The effect of benzyl alcohol, benzaldehyde and benzoic acid on the production of extracellular hydrogen peroxide (H2o2) by the ligninolytic fungus Pleurotus eryngii was investigated. It was found that [...]
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