Bacillus altitudinis strain:KB1
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA670955 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR14203888_1.fastq.gz | Fastqsanger.gz | |||
| SRR14203888_2.fastq.gz | Fastqsanger.gz | |||
| SRR14301852_1.fastq.gz | Fastqsanger.gz | |||
| SRR14301852_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 5 |
Similar Datasets
Project description:L-asparaginase is a target for many researchers as its properties against cancer, especially leukaemia, and protective agents reduce acrylamide in fried food. In this study, the water samples from Thumba Arattuvazhi Beach in Kerala were screened for l-asparaginase producing microorganisms. This was followed by colourimetric screening using modified M9 media with 0.009% Phenol red dye and using l-asparagine as a sole nitrogen source. Then, the Nessler assay was performed to quantify the enzyme. Molecular identification was made by 16SrRNA sequencing and aligned the sequence with GeneBank for phylogenetic tree construction using BLAST. Seawater was serially diluted for 10-1 to 10-6 using nutrient agar plates. A total of 19 bacterial colonies were isolated. The colonies were evaluated to produce l-asparaginase according to the pink zone around the colonies on the modified M9 medium using a red phenol indicator. The KB1 sample was selected for further studies according to plate colour assay. Nessler assay of L-asparaginase quantified as 2.537 IU/ml. Molecular characterisation showed the sequence association with Bacillus altitudinis the sequence submitted in Genebank as B. altitudinis KB1 strain. The l-asparaginase II gene (AnsB) was amplified based on the entire length of the hypothetical protein of annotated genome with accession number CP022319.2. The l-asparaginase activity in this study was 57% higher than the reference organism B. altitudinis BITHSP010. The l-asparaginase producing bacterium B. altitudinis KB1 from a marine source in Kerala can produce asparaginase, which can be utilised for biotechnology applications.
| S-EPMC9326817 | biostudies-literature
Project description:Isolation of marine bacteria for the production of asparaginase
| PRJEB44382 | ENA
Project description:Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RNase from Bacillus altitudinis termed BALNASE (B. altitudinis RNase). Balnase is a close homolog of the well-known cytotoxic binase, differing by only one amino acid residue: nonpolar hydrophobic alanine at position 106 in the balnase molecule is replaced by a polar uncharged threonine in binase. The most exciting question is how the physico-chemical properties and biological effects of RNase might be changed by A106T substitution. Here, we have developed a chromatography-based rapid and modern technique for the purification of this new RNase which allowed us to get a protein sample of high quality with specific activity of 1.2 × 10(6) units in preparative amounts, suitable for further investigation of its biological properties.
| S-EPMC4794795 | biostudies-literature
Project description:We report here the draft genome of Bacillus altitudinis strain PAE4, a thermophilic plant growth-promoting rhizobacterium isolated from the coastal ridge of the Mediterranean Sea in Egypt. Besides heat shock protein genes, several genes encoding phytobeneficial properties were identified.
| S-EPMC6256563 | biostudies-literature
Project description:This study is aimed to isolate marine actinomycetes from sediments from Andaman and the Gulf of Thailand. All 101 marine actinomycetes were screened for anti-biofilm activity. Streptomyces sp. GKU223 showed significantly inhibited biofilm formation of S. aureus. The evaluation of supernatants of anti-biofilm activity produced by Streptomyces sp. GKU223 has been performed. Since the interaction between marine actinomycetes and biofilm forming bacteria has never been investigated, proteomic analysis has been used to identify whole cell proteins involved in anti–biofilm activity. Understanding the interaction at molecular level will lead to sustainably use for anti-biofilm producing marine actinomycetes in pharmaceutical and medicinal applications in the future.
2018-08-20 | PXD010815 | JPOST Repository
Project description:A thermostable keratinase designated as KBALT was purified from Bacillus altitudinis RBDV1 from a poultry farm in Gujarat, India. The molecular weight of the native KBALT (nKBALT) purified using ammonium sulfate and ion exchange and gel permeation chromatography with a 40% yield and 80-fold purification was estimated to be ~ 43 kDa. The gene for KBALT was successfully cloned, sequenced and expressed in Escherichia coli. Recombinant KBALT (rKBALT) when purified using a single step Ni-NTA His affinity chromatography achieved a yield of 38.20% and a 76.4-fold purification. Comparison of the deduced amino acid sequence of rKBALT with known proteases of Bacillus species and inhibitory effect of PMSF suggest that rKBALT was a subtilisin-like serine protease. Both native and rKBALT exhibited higher activity at 85 °C and pH 8.0 in the presence of Mg2+, Mn2+, Zn2+, Ba2+ and Fe3+ metal ions. Interestingly, 70% of their activity was retained at temperatures ranging from 35 to > 95 °C. The keratinolytic activity of both nKBALT and rKBALT was enhanced in the presence of reducing agents. They exhibited broad substrate specificity towards various protein substrates. KBALT was determined for its kinetic properties by calculating its Km (0.61 mg/ml) and Vmax (1673 U/mg/min) values. These results suggest KBALT as a robust and promising contender for enzymatic processing of keratinous wastes in waste processing plants.
| S-EPMC5794678 | biostudies-literature
Project description:Microbial-assisted biofortification attracted much attention recently due to its sustainable and eco-friendly nature for improving nutrient content in wheat. An endophytic strain Bacillus altitudinis WR10, which showed sophistical regulation of iron (Fe) homeostasis in wheat seedlings, inspired us to test its potential for enhancing Fe biofortification in wheat grain. In this study, assays in vitro indicated that WR10 has versatile plant growth-promoting (PGP) traits and bioinformatic analysis predicted its non-pathogenicity. Two inoculation methods, namely, seed soaking and soil spraying, with 107 cfu/ml WR10 cells were applied once before sowing of wheat (Triticum aestivum L. cv. Zhoumai 36) in the field. After wheat maturation, evaluation of yield and nutrients showed a significant increase in the mean number of kernels per spike (KPS) and the content of total nitrogen (N), potassium (K), and Fe in grains. At the grain filling stage, the abundance of Bacillus spp. and the content of N, K, and Fe in the root, the stem, and the leaf were also increased in nearly all tissues, except Fe in the stem and the leaf. Further correlation analysis revealed a positive relationship between the total abundance of Bacillus spp. and the content of N, K, and Fe in grains. Seed staining confirmed the enhanced accumulation of Fe, especially in the embryo and the endosperm. Finally, using a hydroponic coculture model, qPCR quantification indicated effective colonization, internalization, translocation, and replication of strain WR10 in wheat within 48 h. Collectively, strain WR10 assisted successful Fe biofortification in wheat in the field, laying a foundation for further large-scale investigation of its applicability and effectiveness.
| S-EPMC8368724 | biostudies-literature
Project description:This study is aimed to isolate marine actinomycetes from sediments from Andaman and the Gulf of Thailand. All 101 marine actinomycetes were screened for anti-biofilm activity. Streptomyces sp. GKU 257-1 showed significantly inhibited biofilm formation of E. coli. The evaluation of supernatants of anti-biofilm activity produced by Streptomyces sp. GKU 257-1 has been performed. Since the interaction between marine actinomycetes and biofilm forming bacteria has never been investigated, proteomic analysis has been used to identify whole cell proteins involved in anti–biofilm activity. Understanding the interaction at molecular level will lead to sustainably use for anti-biofilm producing marine actinomycetes in pharmaceutical and medicinal applications in the future.
2019-09-07 | PXD011027 | JPOST Repository