RESUMEN
Removal of combined nitrogen and addition of Poly R-478 to the growth medium enhanced oxidative stress, and altered the activities of ligninolytic enzymes of Oscillatoria willei BDU 130511. The activities of ligninolytic and antioxidative enzymes (LiP-like, LAC, PPO, SOD, POD, CAT, and APX) were increased upon nitrogen limitation and dye supplementation. The metabolic enzymes tested (GR, GPX, EST, and MDH) showed differential expressions under varied growth conditions. Up on nitrogen limitation, O. willei BDU 130511 showed enhanced ligninolytic activity as shown by alpha-keto-gamma-methylthiolbutyric acid (KTBA) oxidation and increased H(2)O(2) production. The organism decolourized 52% of Poly R-478 due to partial degradation and adsorption of dye particles from dye-added medium after 7 days of growth. This manuscript discusses the responses of ligninolytic and antioxidative enzymes of O. willei BDU 130511 during Poly R-478 decolourization/degradation, and the organism's potential in bioremediation.
Asunto(s)
Antraquinonas/aislamiento & purificación , Antioxidantes/metabolismo , Lignina/metabolismo , Oscillatoria/enzimología , Polímeros/aislamiento & purificación , Agua de Mar/microbiología , Biodegradación Ambiental , Color , Etilenos/biosíntesis , Isoenzimas/metabolismo , Modelos Biológicos , Oscillatoria/crecimiento & desarrollo , Oscillatoria/metabolismo , Estrés Oxidativo , EspectrofotometríaRESUMEN
The mixed-ligand copper(II) complex [Cu(tdp)(tmp)](ClO4), where H(tdp) is 2-[(2-(2-hydroxyethylamino)ethylimino)methyl]phenol and tmp is 3,4,7,8-tetramethyl-1,10-phenanthroline, exhibits cleavage of the proteins bovine serum albumin and lysozyme, producing approximately 5 and 4 kDa protein fragments respectively within a few minutes at micromolar concentrations. The hydrophobic tmp ligand recognizes the hydrophobic site and enhances protein binding and cleavage even at physiological pH and temperature.
