Abstract：
:Aerobic granules are cultivated by a single bacterial strain, Acinetobacter calcoaceticus, in a sequencing batch reactor (SBR). This strain presents as a good phenol reducer and an efficient auto coagulator in the presence of phenol, mediated by heat-sensitive adhesins proteins. Stable 2.3-mm granules were formed in the SBR following a 7-week cultivation. These granules exhibit excellent settling attributes and degrade phenol efficiently at concentrations of 250-2,000 mg l(-1). The corresponding phenol degradation rate reached 993.6 mg phenol g(-1) volatile suspended solids (VSS) day(-1) at 250 mg l(-1) phenol and 519.3 mg phenol g(-1) VSS day(-1) at 2,000 mg l(-1) phenol concentration. Meanwhile, free A. calcoaceticus cells were fully inhibited at phenol>1,500 mg l(-1). Denaturing gradient gel electrophoresis fingerprint profile demonstrated no genetic modification in the strain during aerobic granulation. The present single-strain granules showed long-term structural stability and performed high phenol degrading capacity and high phenol tolerance. The confocal laser scanning microscopic test revealed that live A. calcoaceticus cells principally distributed at 200-250 microm beneath the outer surface, with an extracellular polymeric substance layer covering them to defend phenol toxicity. Autoaggregation assay tests demonstrated the possibly significant role of secreted proteins on the formation of single-culture A. calcoaceticus granules.
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Adav SS,Lee DJdoi
10.1007/s00253-007-1325-xsubject
Has Abstractpub_date
2008-03-01 00:00:00pages
551-7issue
3eissn
0175-7598issn
1432-0614journal_volume
78pub_type
杂志文章abstract：:Microbial genome sequencing has left a legacy of annotated yet uncharacterized genes or open reading frames, activities that may have useful applications in health and/or the environment. We are interested in the discovery and characterization of potentially new pectinolytic activities for the enzymatic retting of nat...
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