Browse
Submit Data
Databases
API
Help

Dataset Information

10 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Biodegradation of Navy N5RL1 carpet dye by Staphylococcus saprophyticus strain BHUSS X3.

ABSTRACT: Biodegradation of Navy N5RL1, a widely used acidic azo dye in carpet industry, was studied by bacterial strain isolated from the dye-contaminated soil collected from a carpet industry premises located in Bhadohi, Sant Ravidas Nagar and Uttar Pradesh, India. The isolated strain was identified as Staphylococcus saprophyticus BHUSS X3 on the basis of morphological, biochemical and 16S rRNA gene sequencing analysis. The strain BHUSS X3 decolorized 95.7 % of dye (100 mg/l) within 6 h at optimum pH 8, temperature 35 °C, inoculum 4.0 % under static condition during 24 h incubation. The isolated bacterial strain BHUSS X3 can toralate dye concentration upto 1,000 mg/l. The dye degradation metabolites were confirmed by analysis of degraded products using UV-Vis spectrophotometric, HPLC and FTIR technique. The phytotoxicity analysis was also conducted on Phaseolus aureus and enhanced seed germination was recorded.

SUBMITTER: Kumari L

PROVIDER: S-EPMC4569626 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Decolourization and biodegradation of Navy blue HER (Reactive Blue 171) dye from Marasmius sp. BBKAV79.

Project description:White rot fungus Marasmius sp. BBKAV79 (GenBank accession number-KP455496, KP455497) exhibited decolourization and degradation of Navy blue HER dye (concentration 50 mg l-l) within 24 h under shaking condition. In the present study, various investigated parameters like initial dye concentration, pH, temperature, carbon and nitrogen sources were optimized to develop a faster decolourization process by Marasmius sp. BBKAV79. High-performance liquid chromatography, Fourier transform infrared spectroscopy and gas chromatography and mass spectroscopy analysis of the extracted product confirmed the biodegradation of Navy blue HER. The microbial toxicity and phytotoxicity assay revealed that the degradation of Navy blue HER produced nontoxic metabolites.

| S-EPMC5428106 | biostudies-literature

SdrI, a serine-aspartate repeat protein identified in Staphylococcus saprophyticus strain 7108, is a collagen-binding protein.

Project description:A gene encoding a serine-aspartate repeat protein of Staphylococcus saprophyticus, an important cause of urinary tract infections in young women, has been cloned and sequenced. In contrast to other SD repeat proteins, SdrI carries 21 additional N-terminal repeats with a consensus sequence of (P/A)ATKE(K/E)A(A/V)(T/I)(A/T/S)EE and has the longest SD(AD)(1-5) repetitive region (854 amino acids) described so far. This highly repetitive sequence contains only the amino acids serine, asparagine, and a distinctly greater amount of alanine (37%) than all other known SD repeat proteins (2.3 to 4.4%). In addition, it is a collagen-binding protein of S. saprophyticus and the second example in this organism of a surface protein carrying the LPXTG motif. We constructed an isogenic sdrI knockout mutant that showed decreased binding to immobilized collagen compared with wild-type S. saprophyticus strain 7108. Binding could be reconstituted by complementation. Collagen binding is specifically caused by SdrI, and the recently described UafA protein, the only LPXTG-containing protein in the genome sequence of the type strain, is not involved in this trait. Our experiments suggest that, as in other staphylococci, the presence of different LPXTG-anchored cell wall proteins is common in S. saprophyticus and support the notion that the presence of matrix-binding surface proteins is common in staphylococci.

| S-EPMC1539602 | biostudies-literature

The surface-associated protein of Staphylococcus saprophyticus is a lipase.

Project description:Staphylococcus saprophyticus surface-associated protein (Ssp) was the first surface protein described for this organism. Ssp-positive strains display a fuzzy layer of surface-associated material in electron micrographs, whereas Ssp-negative strains appear to be smooth. The physiologic function of Ssp, however, has remained elusive. To clone the associated gene, we determined the N-terminal sequence, as well as an internal amino acid sequence, of the purified protein. We derived two degenerate primers from these peptide sequences, which we used to identify the ssp gene from genomic DNA of S. saprophyticus 7108. The gene was cloned by PCR techniques and was found to be homologous to genes encoding staphylococcal lipases. In keeping with this finding, strains 7108 and 9325, which are Ssp positive, showed lipase activity on tributyrylglycerol agar plates, whereas the Ssp-negative strain CCM883 did not. Association of enzyme activity with the cloned DNA was proven by introducing the gene into Staphylococcus carnosus TM300. When wild-type strain 7108 and an isogenic mutant were analyzed by transmission electron microscopy, strain 7108 exhibited the fuzzy surface layer, whereas the mutant appeared to be smooth. Lipase activity and the surface appendages could be restored by reintroduction of the cloned gene into the mutant. Experiments using immobilized collagen type I did not provide evidence for the involvement of Ssp in adherence to this matrix protein. Our experiments thus provided evidence that Ssp is a surface-associated lipase of S. saprophyticus.

| S-EPMC1230896 | biostudies-literature

Staphylococcus saprophyticus

Project description:Staphylococcus saprophyticus Genome sequencing and assembly

| PRJNA636387 | ENA

Staphylococcus saprophyticus

Project description:Staphylococcus saprophyticus whole genome sequencing

| PRJNA352403 | ENA

Staphylococcus saprophyticus

Project description:Commensal Staphylococcal species that can cause acute urinary tract infections

| PRJNA35739 | ENA

Staphylococcus saprophyticus

Project description:Draft Genome Sequence of Staphylococcus saprophyticus strains

| PRJNA700496 | ENA

A proteomic dataset of secreted proteins by three Staphylococcus saprophyticus strains.

Project description:This article presents a proteomic dataset generated from a comparative analysis of the exoproteome of Staphylococcus saprophyticus, ATCC 15305, 7108 and 9325 strains. The extract of secreted proteins were obtained after incubation of stationary phase cells in BHI medium. All samples were submitted to nano-ESI-UPLC-MSE, and the spectrum obtained was processed and analyzed by ProteinLynx Global Server (PLGS), Uniprot and Pedant databases, for identification, annotation and functional classification of proteins. Fold changes and protein relative abundances were properly reported. This report is related to the research article entitled "The exoproteome profiles of three Staphylococcus saprophyticus strains reveal diversity in protein secretion contents" (Oliveira et al., 2018). The proteomic data generated have been deposited to the ProteomeXchange Consortium, via the PRIDE partner repository, with a project number PXD008643, https://www.ebi.ac.uk/pride/archive/projects/PXD008643.

| S-EPMC6234272 | biostudies-literature

Transcriptome Analysis of Halotolerant Staphylococcus saprophyticus Isolated from Korean Fermented Shrimp.

Project description:Saeu-jeotgal, a Korean fermented shrimp food, is commonly used as an ingredient for making kimchi and other side dishes. The high salinity of the jeotgal contributes to its flavor and inhibits the growth of food spoilage microorganisms. Interestingly, Staphylococcus saprophyticus was discovered to be capable of growth even after treatment with 20% NaCl. To elucidate the tolerance mechanism, a genome-wide gene expression of S. saprophyticus against 0%, 10%, and 20% NaCl was investigated by RNA sequencing. A total of 831, 1314, and 1028 differentially expressed genes (DEGs) were identified in the 0% vs. 10%, 0% vs. 20%, and 10% vs. 20% NaCl comparisons, respectively. The Clusters of Orthologous Groups analysis revealed that the DEGs were involved in amino acid transport and metabolism, transcription, and inorganic ion transport and metabolism. The functional enrichment analysis showed that the expression of the genes encoding mechanosensitive ion channels, sodium/proton antiporters, and betaine/carnitine/choline transporter family proteins was downregulated, whereas the expression of the genes encoding universal stress proteins and enzymes for glutamate, glycine, and alanine synthesis was upregulated. Therefore, these findings suggest that the S. saprophyticus isolated from the saeu-jeotgal utilizes different molecular strategies for halotolerance, with glutamate as the key molecule.

| S-EPMC8870806 | biostudies-literature

Serratia sp. X3 strain:X3

Project description:Serratia sp. X3 strain:X3 Genome sequencing and assembly

| PRJNA668443 | ENA