Biodegradation of acrylamide by acrylamidase from Stenotrophomonas acidaminiphila MSU12 and analysis of degradation products by MALDI-TOF and HPLC

The present study examines an improved detoxification and rapid biological degradation of toxic pollutant acrylamide using a bacterium. The acrylamide degrading bacterium was isolated from the soil followed by its screening to know the acrylamide degrading capability. The minimal medium containing a...

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Veröffentlicht in:International biodeterioration & biodegradation 2014-10, Vol.94, p.214-221
Hauptverfasser: Lakshmikandan, M., Sivaraman, K., Elaiya Raja, S., Vasanthakumar, P., Rajesh, R.P., Sowparthani, K., Jebasingh, S. Emmanuel Joshua
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Sprache:eng
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Zusammenfassung:The present study examines an improved detoxification and rapid biological degradation of toxic pollutant acrylamide using a bacterium. The acrylamide degrading bacterium was isolated from the soil followed by its screening to know the acrylamide degrading capability. The minimal medium containing acrylamide (30 mM) served as a sole source of carbon and nitrogen for their active growth. The optimization of three different factors was analyzed by using Response Surface Methodology (RSM). The bacteria actively degraded the acrylamide at a temperature of 32 °C, with a maximum growth at 30 mM substrate (acrylamide) concentration at a pH of 7.2. The acrylamidase activity and degradation of acrylamide was determined by High Performance Liquid Chromatography (HPLC) and Matrix Assisted Laser Desorption and Ionization Time of Flight mass spectrometer (MALDI-TOF). Based on 16S rRNA analysis the selected strain was identified as Gram negative bacilli Stenotrophomonas acidaminiphila MSU12. The acrylamidase was isolated from bacterial extract and was purified by HPLC, whose mass spectrum showed a molecular mass of 38 kDa. •The bacterium Stenotrophomonas acidaminiphila MSU12 can degrade 30 mM of acrylamide within 48–54 h.•The bacterial acrylamidase enzyme was purified by using different chromatographic method.•Using MALDI-TOF mass spectrometry the purified acrylamidase enzyme molecular mass (38 kDa) was determined.
ISSN:0964-8305
1879-0208
DOI:10.1016/j.ibiod.2014.07.014