Thermomyces lanuginosus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA88653 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR2059702_1.fastq.gz | Fastqsanger.gz | |||
| SRR2059702_2.fastq.gz | Fastqsanger.gz | |||
| SRR2059703_1.fastq.gz | Fastqsanger.gz | |||
| SRR2059703_2.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:Thermomyces lanuginosus is a thermophilic fungus whose genome encodes many carbohydrate-active enzymes involved in Avicel degradation. This study examined and compared the transcriptomes of T. lanuginosus during cultivation on Avicesl or glucose. We identified approximately 4485 genes that showed expression differences when T. lanuginosus was cultured on Avicel compared to glucose. Functional annotation of up-regulated genes showed enrichment for proteins predicted to be involved in Avicel degradation, but also many genes encoding proteins of unknown function. Our study represents the first analysis of transcriptomes, with biologic replicates, generated by RNA-seq technology. We conclude that RNA-seq based transcriptome characterization would expedite genetic network analyses and permit the dissection of complex biologic functions.
2015-06-17 | GSE69763 | GEO
Project description:Thermomyces lanuginosus is a thermophilic fungus whose genome encodes many carbohydrate-active enzymes involved in Avicel degradation. This study examined and compared the transcriptomes of T. lanuginosus during cultivation on Avicesl or glucose. We identified approximately 4485 genes that showed expression differences when T. lanuginosus was cultured on Avicel compared to glucose. Functional annotation of up-regulated genes showed enrichment for proteins predicted to be involved in Avicel degradation, but also many genes encoding proteins of unknown function. Our study represents the first analysis of transcriptomes, with biologic replicates, generated by RNA-seq technology. We conclude that RNA-seq based transcriptome characterization would expedite genetic network analyses and permit the dissection of complex biologic functions. mRNA profiles of 2-day old Thermomyces lanuginosus were generated by deep sequencing,in duplicate, using Illumina GAIIx.
2015-06-17 | E-GEOD-69763 | biostudies-arrayexpress
Project description:Transcriptome Analysis of Avicel Utilization by Thermomyces lanuginosus
| PRJNA286684 | ENA
Project description:Thermomyces lanuginosus SSBP Genome sequencing and assembly
| PRJNA88097 | ENA
Project description:The low cost lipase derived from Thermomyces lanugionous was chosen to conjugate with Fe3O4 nanoparitcles as a magnetic responsive lipase (MRL) biocatalyst. The structure of MRL was observed by atomic force microscopy (AFM). The Fourier transform infrared (FTIR) spectroscopy analysis confirmed the lipase conjugated to Fe3O4 nanoparticles. Optimized conditions for the process of biodiesel production by MRL were investigated by the response surface methodology (RSM) and the Box-Behnken design (BBD). The optimized conditions for biodiesel production by MRL were as follows. The molar ratio of methanol to oil was 4.0, water content was 1.5 % as oil weight, the dosage of MRL to oil was 9.0 % (W/W) under 41 °C for 28 h. Under the optimized conditions, the yield of FAMEs by MRL reached 82.20 %. Further experiments showed that the MRL could be used 10 cycles and the yield of FAMEs decreased slightly by 10.97 %. These results indicated that Fe3O4 nanoparticle carrier could efficiently improve the FAMEs synthesis and enhance the MRL stabilization and reusability in the biodiesel production.
| S-EPMC7245248 | biostudies-literature
Project description:Highly efficient production of a Thermomyces lanuginosus IOC-4145 beta-1,4-xylanase was achieved in Pichia pastoris under the control of the AOX1 promoter. P. pastoris colonies expressing recombinant xylanase were selected by enzymatic activity plate assay, and their ability to secrete high levels of the enzyme was evaluated in small-scale cultures. Furthermore, an optimization of enzyme production was carried out with a 2(3) factorial design. The influence of initial cell density, methanol, and yeast nitrogen base concentration was evaluated, and initial cell density was found to be the most important parameter. A time course profile of recombinant xylanase production in 1-liter flasks with the optimized conditions was performed and 148 mg of xylanase per liter was achieved. Native and recombinant xylanases were purified by gel filtration and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, circular dichroism spectroscopy, matrix-assisted laser desorption ionization-time of flight-mass spectrometry and physicochemical behavior. Three recombinant protein species of 21.9, 22.1, and 22.3 kDa were detected in the mass spectrum due to variability in the amino terminus. The optimum temperature, thermostability, and circular dichroic spectra of the recombinant and native xylanases were identical. For both enzymes, the optimum temperature was 75 degrees C, and they retained 60% of their original activity after 80 min at 70 degrees C or 40 min at 80 degrees C. The high level of fully active recombinant xylanase obtained in P. pastoris makes this expression system attractive for fermentor growth and industrial applications.
| S-EPMC201252 | biostudies-literature
Project description:A new strain of Thermomyces lanuginosus was isolated from the Atlantic Forest biome, and its β-xylosidases optimization in response to agro-industrial residues was performed. Using statistical approach as a strategy for optimization, the induction of β-xylosidases activity was evaluated in residual corn straw, and improved so that the optimum condition achieved high β-xylosidases activities 1003U/mL. According our known, this study is the first to show so high levels of β-xylosidases activities induction. In addition, the application of an experimental design with this microorganism to induce β-xylosidases has not been reported until the present work. The optimal conditions for the crude enzyme extract were pH 5.5 and 60°C showing better thermostability at 55°C. The saccharification ability of β-xylosidase in the presence of hemicellulose obtained from corn straw raw and xylan from beechwood substrates showed a xylo-oligosaccharide to xylose conversion yield of 80 and 50%, respectively, at 50°C. Our data strongly indicated that the β-xylosidases activities was not subjected to the effects of potential enzyme inhibitors often produced during fermentation process. These data suggest the application of this enzyme studied for saccharification of hemicellulose, an abundant residue in the American continents, thus providing an interesting alternative for future tests for energy production.
| S-EPMC4927647 | biostudies-literature
Project description:Thermomyces lanuginosus strain:0065 Raw sequence reads
| PRJNA842093 | ENA
Project description:Thermomyces lanuginosus strain:ATCC200065 Transcriptome or Gene expression
| PRJNA213840 | ENA
Project description:Purified endoxylanase from Thermomyces lanuginosus PC7S1T was immobilized in calcium alginate, resulting in a yield of 78.5% and a reusability for 11 cycles. The stability of the immobilized enzyme was given for a pH range of 4 to 9 for 96 h. Endoxylanase immobilized in calcium alginate at 65 °C exhibited thermal stability equal to the soluble enzyme for 5 h, and at high temperatures of 75 °C and 85 °C showed half-lives of 4 and 3 h, respectively. Both soluble endoxylanase and immobilized forms were able to hydrolyze hemicellulose, obtained from low-lignin sorghum biomass pretreated with 5% H2O2 and 2% NaOH, after 1 h of incubation at 65 °C, releasing a mixture of short-chain xylooligosaccharides (X2-X6). The highest amounts of XOS generated were those for X5 (24 to 40%), X4 (33 to 39%), and X3 (11 to 22%). These XOS acted as prebiotics, promoting the growth of the probiotic L. acidophilus, similar to glucose in the MRS broth. These results show the potential of low-lignin sorghum to generate XOS with prebiotic activity, suggesting the application of these compounds in the food industry.
| S-EPMC9433589 | biostudies-literature