01972nas a2200253   4500008004100000022001400041245008700055210006900142260009500211300001400306490000700320520108100327653001901408653001001427653002201437653001601459653001801475653001501493100002301508700002201531700002401553700002601577856011501603       2010                        eng d  a0147-651300aEfficient industrial dye decolorization by Bacillus sp. VUS with its enzyme system0 aEfficient industrial dye decolorization by Bacillus sp VUS with   a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcOCT  a1696-17030 v733 a<p>This work presents role of different enzymes in decolorization of industrial dye Orange T4LL by Bacillus sp. VUS. Bacillus sp. strain VUS decolorized dye Orange T4LL, under static anoxic condition in 24 h. During decolorization of Orange T4LL a significant induction in the activities of lignin peroxidase, tyrosinase, and reductases (NADH-DCIP, azo, and riboflavin) was observed. The biodegradation was monitored by Ultraviolet-visible spectroscopy, Fourier transform infrared spectroscopy, and high performance liquid chromatography. The final products 4-methyl-2-o-tolylazo-benzene-1,3-diamine and [3-(phenyl-hydrazono)-cyclohexa-1,4-dienyl]-methanol were characterized by gas chromatography-mass spectroscopy. Phytotoxicity, COD, and BUD revealed non-toxicity of degraded products. Phytotoxicity study demonstrated non-toxicity of the biodegraded products for crop plants with respect to Triticum aestivum and Sorghum bicolor. Bacillus sp. VUS with its enzyme system could be a useful tool for textile effluent treatment. (C) 2010 Elsevier Inc. All rights reserved.</p>10aDecolorization10aGC-MS10aLignin peroxidase10aOrange T4LL10aPhytotoxicity10aReductases1 aDawkar, Vishal, V.1 aJadhav, Umesh, U.1 aTamboli, Dhawal, P.1 aGovindwar, Sanjay, P.  uhttps://library.ncl.res.in/content/efficient-industrial-dye-decolorization-bacillus-sp-vus-its-enzyme-system-002192nas a2200253   4500008004100000022001400041245014400055210006900199260014500268300001200413490000700425520113300432653002501565653001801590653002301608653003201631653002801663100002401691700002001715700002301735700002401758700002601782856013001808       2011                        eng d  a1226-837200aPurification and characterization of bacterial aryl alcohol oxidase from sphingobacterium sp ATM and Its uses in textile dye decolorization0 aPurification and characterization of bacterial aryl alcohol oxid  aKOREAN SCIENCE TECHNOLOGY CENTER, \#704 YEOGSAM-DONG, KANGNAM-KU, SEOUL 135-703, SOUTH KOREAbKOREAN SOC BIOTECHNOLOGY & BIOENGINEERINGcAUG  a661-6680 v163 a<p>Aryl alcohol oxidase (AAO) produced by dye decolorizing bacteria Sphingobacterium sp. ATM, was purified 22.63 fold to a specific activity of 21.75 mu mol/min/mg protein using anion exchange and size exclusion chromatography. The molecular weight of the purified AAO was found to be 71 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and confirmed by zymography of AAO using L-dopa. The enzyme showed substrate specificity towards veratryl alcohol, followed by n-propanol. The optimum pH and temperature of purified AAO were found to be 3.0 and 40 degrees C, respectively. The K(m) and V(max) of AAO was 1.1615 mM and 3.13 mM/min when veratryl alcohol was used as substrate. Sodium azide showed maximum inhibition while ethylenediamine tetra acetic acid (EDTA), L-cysteine and dithiothreitol showed slight inhibition. Metal ions also showed slight inhibition. HPLC analysis confirmed the degradation of Direct Red 5B. The metabolite obtained after decolorization of Direct Red 5B was characterized as 3 diazenyl 7 [-(phenyl carbonyl) amino] naphthalene-2-sulfonic acid using GC-MS analysis.</p>10aaryl alcohol oxidase10aDirect Red 5B10adye decolorization10aion exchange chromatography10aSphingobacterium sp ATM1 aTamboli, Dhawal, P.1 aTelke, Amar, A.1 aDawkar, Vishal, V.1 aJadhav, Shekhar, B.1 aGovindwar, Sanjay, P.  uhttps://library.ncl.res.in/content/purification-and-characterization-bacterial-aryl-alcohol-oxidase-sphingobacterium-sp-atm-0