Microbial decolorization of reactive azo dyes in a sequential anaerobic-aerobic system

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Basic knowledge and perspectives of bioelimination of xenobiotic compounds

1,2-Dihydroxynaphthalene dioxygenase was purified to homogeneity from a bacterium that degrades naphthalenesulfonic acids (strain BN6). The enzyme requires Fe2+ for maximal activity and consists of eight identical subunits with a molecular weight of about 33,000. Analysis of the NH2-terminal amino acid sequence revealed a high degree of homology (22 of 29 amino acids) with the NH2-terminal amino acid sequence of 2,3-dihydroxybiphenyl dioxygenase from strain Pseudomonas paucimobilis Q1. 1,2-Dihydroxynaphthalene dioxygenase from strain BN6 shows a wide substrate specificity and also cleaves 5-, 6-, and 7-hydroxy-1,2-dihydroxynaphthalene, 2,3- and 3,4-dihydroxybiphenyl, catechol, and 3-methyl- and 4-methylcatechol. Similar activities against the hydroxy-1,2-dihydroxynaphthalenes were also found in cell extracts from naphthalene-degrading bacteria.

Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids.

BN6 was isolated from the river Elbe as a member of a multispecies bacterial culture which mineralized 6-aminonaphthalene-2-sulfonate. Pure cultures of strain BN6 converted a wide range of amino- and hydroxynaphthalene-2-sulfonates via a catabolic pathway similar to that described for the metabolism of naphthalene to salicylate by Pseudomonas putida NAH7 or Pseudomonas sp NCIB 9816. In contrast to the naphthalene-degrading pseudomonads, S. xenophaga BN6 only partially degraded the naphthalenesulfonates and excreted the resulting amino- and hydroxysalicylates in almost stoichiometric amounts. Enzymes that take part in the degradative pathway of the naphthalenesulfonates by strain BN6 were purified, characterized and compared with the isofunctional enzymes from the naphthalene-degrading pseudomonads. According to the enzyme structures and the catalytic constants, no fundamental differences were found between the 1,2-dihydroxynaphthalene dioxygenase or the 2′-hydroxybenzalpyruvate aldolase from strain BN6 and the isofunctional enzymes from the naphthalene-degrading pseudomonads. The limited available sequence information about the enzymes from strain BN6 suggests that they show about 40–60% sequence identity to the isofunctional enzymes from the pseudomonads. In addition to the gene for the 1,2-dihydroxynaphthalene dioxygenase, the genes for two other extradiol dioxygenases were cloned and sequenced from strain BN6 and the corresponding gene products were studied. S. xenophaga BN6 has also been used as a model organism to study the mechanism of the non-specific reduction of azo dyes under anaerobic conditions and to establish combined anaerobic/aerobic treatment systems for the degradation of sulfonated azo dyes. Furthermore, the degradation of substituted naphthalenesulfonates by mixed cultures containing strain BN6 was studied in continuous cultures and was described by mathematical models.

Degradation of substituted naphthalenesulfonic acids by Sphingomonas xenophaga BN6.

Fate of aromatic sulfonates in fluvial environment

The degradation of 6-aminonaphthalene-2-sulphonic acid (6A2NS) by mixed cultures via an interspecies transfer of 5-aminosalicylic acid (5AS) was investigated using a continuous chemostat culture. Two different bacterial communities were employed. Steady-state data were obtained from a multi-species culture only, but not from a defined two-species culture. Experimental data showed the conversion of 6A2NS into 5AS to be rate-determining for degradation. Both the Monod equation, and an extended model regarding the interspecies transfer of 5AS, were found to be suitable to describe the relationship between biomass and substrate concentration, depending on the flow rate of continuous culture. Substrate consumed for endogenous metabolism was considred according to Pirt (1975).

Degradation of 6-aminonaphthalene-2-sulphonic acid by mixed cultures: kinetic analysis

Production rates of CO2 were calculated on the basis of kinetic data obtained from 6-amino-2-naphthalenesulphonic acid (6A2NS) degradation with a mixed bacterial culture. A linear correlation between product (CO2) formation and growth rate was found for submersed growing cultures as well as for bacteria immobilized on sand particles. For immobilized biomass a distinction was made between active cells and bacterial exopolymers using model calculations.

R. Diekmann

Papers

Degradation of 6-aminonaphthalene-2-sulphonic acid by mixed cultures: kinetic analysis

Production rates of CO2 by suspended and immobilized bacteria degrading 6-amino-2-naphthalenesulphonic acid