Kalyani et al (2009) studied an isolated strain of Pseudomonas sp. SUK1 from the waste disposal sites of local textile industries in India, with the objective of evaluate an ecofriendly textile dyes biodegradation.
To isolate the microorganism, they first collected a soil sample from the waste disposal site and inoculated the sample in a nutrient medium with a dye. Then they incubated and plated in agar with dye. The colonies that had a halo of decolorization were selected to be submitted to biochemical tests and 16S rDNA analyses that identified Pseudomonas sp. SUK1. The phylogenetic analyses showed a close relation with other strains that already have reports of a role in biodegradation of dye.
The study of acclimatation with increasing …show more content…
It also showed that the mechanism and structure are different from the other peroxidases classifications; this can is demonstrated by the ability of this peroxidase to degrade anthraquinone-dyes (Reactive Blue19).
Other result showed was the comparison of the specific activity of the Bacillus subtillis peroxidase with the peroxidase of other microorganisms and the results this study was between the results of the other studies. The specific activity of B. subtillis peroxidase was higher than from Thermobifida fusca and lower than cyanobacterium Anabaena species. Other observation made based on its specific activity was that B. subtillis peroxidase slightly preferred azo- than anthraquinone-dye, on the other hand the other enzymes studied were more effective for anthraquinone-dye (Reactive Blue19) than azo-dye …show more content…
The maximum of activity of laccase was 8.4 U/ml on day 6, the peak of MnP was 26.8 U/ ml and only occurred a few days later, on day 9. This data was obtained with the enzymes in the presence of PBB-HGR, but in the absence of the dyes the activity detected was considerably lower. The activity of MnP was four times higher in the presence of PBB-HGR and two-fold higher in the presence of RFB. The enzyme laccase had two-fold higher activity in the presence of PBB-HGR but not in the presence of RFB, this can be explained by the fact that RFB is an azo dye and is not a substrate of laccase. In the other hand the higher results obtained with shows that it is a substrate of laccase. The decolorization that occurred was not by the mechanism of adsorption, because the adsorption of dyes to bacterial biomass was not observed in this
To isolate the microorganism, they first collected a soil sample from the waste disposal site and inoculated the sample in a nutrient medium with a dye. Then they incubated and plated in agar with dye. The colonies that had a halo of decolorization were selected to be submitted to biochemical tests and 16S rDNA analyses that identified Pseudomonas sp. SUK1. The phylogenetic analyses showed a close relation with other strains that already have reports of a role in biodegradation of dye.
The study of acclimatation with increasing …show more content…
It also showed that the mechanism and structure are different from the other peroxidases classifications; this can is demonstrated by the ability of this peroxidase to degrade anthraquinone-dyes (Reactive Blue19).
Other result showed was the comparison of the specific activity of the Bacillus subtillis peroxidase with the peroxidase of other microorganisms and the results this study was between the results of the other studies. The specific activity of B. subtillis peroxidase was higher than from Thermobifida fusca and lower than cyanobacterium Anabaena species. Other observation made based on its specific activity was that B. subtillis peroxidase slightly preferred azo- than anthraquinone-dye, on the other hand the other enzymes studied were more effective for anthraquinone-dye (Reactive Blue19) than azo-dye …show more content…
The maximum of activity of laccase was 8.4 U/ml on day 6, the peak of MnP was 26.8 U/ ml and only occurred a few days later, on day 9. This data was obtained with the enzymes in the presence of PBB-HGR, but in the absence of the dyes the activity detected was considerably lower. The activity of MnP was four times higher in the presence of PBB-HGR and two-fold higher in the presence of RFB. The enzyme laccase had two-fold higher activity in the presence of PBB-HGR but not in the presence of RFB, this can be explained by the fact that RFB is an azo dye and is not a substrate of laccase. In the other hand the higher results obtained with shows that it is a substrate of laccase. The decolorization that occurred was not by the mechanism of adsorption, because the adsorption of dyes to bacterial biomass was not observed in this