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Title: | Biodecolorization of a food azo dye by the deep sea Dermacoccus abyssi MT1.1<sup>T</sup>strain from the Mariana Trench |
Authors: | Weeranuch Lang Sarote Sirisansaneeyakul Lígia O. Martins Lukana Ngiwsara Nobuo Sakairi Wasu Pathom-aree Masayuki Okuyama Haruhide Mori Atsuo Kimura |
Authors: | Weeranuch Lang Sarote Sirisansaneeyakul Lígia O. Martins Lukana Ngiwsara Nobuo Sakairi Wasu Pathom-aree Masayuki Okuyama Haruhide Mori Atsuo Kimura |
Keywords: | Environmental Science |
Issue Date: | 1-Jan-2014 |
Abstract: | This study reports the characterization of the ability of Dermacoccus spp. isolated from the deepest point of the world's oceans for azo dye decolorization. A detailed investigation of D ermacoccus abyssi MT1.1Twith respect to the azoreductase activity and enzymatic mechanism as well as the potential role of the bacterial strain for biocleaning of industrial dye baths is reported. Resting cells with oxygen-insensitive azoreductase resulted in the rapid decolorization of the polysulfonated dye Brilliant Black BN (BBN) which is a common food colorant. The highest specific decolorization rate (vs) was found at 50°C with a moderately thermal tolerance for over 1h. Kinetic analysis showed the high rates and strong affinity of the enzymatic system for the dye with a Vmax=137mg/gcell/h and a Km=19mg/L. The degradation of BBN produces an initial orange intermediate, 8-amino-5-((4-sulfonatophenyl)diazenyl)naphthalene-2-sulfonic acid, identified by mass spectrometry which is later converted to 4-aminobenzene sulfonic acid. Nearly 80% of the maximum vsis possible achieved in resting cell treatment with the salinity increased up to 5.0% NaCl in reaction media. Therefore, this bacterial system has potential for dye decolorization bioprocesses occurring at high temperature and salt concentrations e.g. for cleaning dye-containing saline wastewaters. © 2013 Elsevier Ltd. |
URI: | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84896940733&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/53594 |
ISSN: | 10958630 03014797 |
Appears in Collections: | CMUL: Journal Articles |
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