Quinone-mediated decolorization of sulfonated azo dyes by cells and cell extracts from Sphingomonas xenophaga

2009 ◽  
Vol 21 (4) ◽  
pp. 503-508 ◽  
Author(s):  
Ling JIAO ◽  
Hong LU ◽  
Jiti ZHOU ◽  
Jing WANG
2002 ◽  
Vol 68 (9) ◽  
pp. 4341-4349 ◽  
Author(s):  
Andreas Keck ◽  
Jörg Rau ◽  
Thorsten Reemtsma ◽  
Ralf Mattes ◽  
Andreas Stolz ◽  
...  

ABSTRACT During aerobic degradation of naphthalene-2-sulfonate (2NS), Sphingomonas xenophaga strain BN6 produces redox mediators which significantly increase the ability of the strain to reduce azo dyes under anaerobic conditions. It was previously suggested that 1,2-dihydroxynaphthalene (1,2-DHN), which is an intermediate in the degradative pathway of 2NS, is the precursor of these redox mediators. In order to analyze the importance of the formation of 1,2-DHN, the dihydroxynaphthalene dioxygenase gene (nsaC) was disrupted by gene replacement. The resulting strain, strain AKE1, did not degrade 2NS to salicylate. After aerobic preincubation with 2NS, strain AKE1 exhibited much higher reduction capacities for azo dyes under anaerobic conditions than the wild-type strain exhibited. Several compounds were present in the culture supernatants which enhanced the ability of S. xenophaga BN6 to reduce azo dyes under anaerobic conditions. Two major redox mediators were purified from the culture supernatants, and they were identified by high-performance liquid chromatography-mass spectrometry and comparison with chemically synthesized standards as 4-amino-1,2-naphthoquinone and 4-ethanolamino-1,2-naphthoquinone.


2019 ◽  
Vol 411 (22) ◽  
pp. 5833-5843 ◽  
Author(s):  
Missael Antonio Arroyo Negrete ◽  
Kazimierz Wrobel ◽  
Eunice Yanez Barrientos ◽  
Alma Rosa Corrales Escobosa ◽  
Francisco Javier Acevedo Aguilar ◽  
...  

2007 ◽  
Vol 6 (9) ◽  
pp. 1010 ◽  
Author(s):  
Katrina M. Tait ◽  
John A. Parkinson ◽  
David I. Gibson ◽  
Patricia R. Richardson ◽  
Warren J. Ebenezer ◽  
...  

1991 ◽  
Vol 26 (10) ◽  
pp. 826-830 ◽  
Author(s):  
Susan D. Richardson ◽  
Alfred D. Thruston ◽  
John M. McGuire ◽  
George L. Baughman

1987 ◽  
Vol 1 (3) ◽  
pp. 48-50 ◽  
Author(s):  
Donald A. Flory ◽  
Matthew M. McLean ◽  
Marvin L. Vestal ◽  
Leon D. Betowski ◽  
S. J. Gaskell

2000 ◽  
Vol 66 (4) ◽  
pp. 1429-1434 ◽  
Author(s):  
Rainer Russ ◽  
Jörg Rau ◽  
Andreas Stolz

ABSTRACT A flavin reductase, which is naturally part of the ribonucleotide reductase complex of Escherichia coli, acted in cell extracts of recombinant E. coli strains under aerobic and anaerobic conditions as an “azo reductase.” The transfer of the recombinant plasmid, which resulted in the constitutive expression of high levels of activity of the flavin reductase, increased the reduction rate for different industrially relevant sulfonated azo dyes in vitro almost 100-fold. The flavin reductase gene (fre) was transferred to Sphingomonas sp. strain BN6, a bacterial strain able to degrade naphthalenesulfonates under aerobic conditions. The flavin reductase was also synthesized in significant amounts in theSphingomonas strain. The reduction rates for the sulfonated azo compound amaranth were compared for whole cells and cell extracts from both recombinant strains, E. coli, and wild-typeSphingomonas sp. strain BN6. The whole cells showed less than 2% of the specific activities found with cell extracts. These results suggested that the cytoplasmic anaerobic “azo reductases,” which have been described repeatedly in in vitro systems, are presumably flavin reductases and that in vivo they have insignificant importance in the reduction of sulfonated azo compounds.


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