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Thermoascus aurantiacus

ABSTRACT: Thermoascus aurantiacus overview

PROVIDER: PRJNA568344 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10849939_1.fastq.gz	Fastqsanger.gz
	SRR10849939_2.fastq.gz	Fastqsanger.gz
	SRR10849940_1.fastq.gz	Fastqsanger.gz
	SRR10849940_2.fastq.gz	Fastqsanger.gz
	SRR14574000.fastq.gz	Fastqsanger.gz

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Thermoascus aurantiacus ATCC 26904

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Thermoascus aurantiacus ATCC 26904

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Thermoascus aurantiacus ATCC 26904 isolate:ATCC 26904

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Diplacus aurantiacus

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Development of genetic tools for the thermophilic filamentous fungus Thermoascus aurantiacus

Project description:Background Fungal enzymes are vital for industrial biotechnology, including the conversion of plant biomass to biofuels and bio-based chemicals. In recent years, there is increasing interest in using enzymes from thermophilic fungi, which often have higher reaction rates and thermal tolerance compared to currently used fungal enzymes. The thermophilic filamentous fungus Thermoascus aurantiacus produces large amounts of highly thermostable plant cell wall-degrading enzymes. However, no genetic tools have yet been developed for this fungus, which prevents strain engineering efforts. The goal of this study was to develop strain engineering tools such as a transformation system, a CRISPR/Cas9 gene editing system and a sexual crossing protocol to improve the enzyme production. Results Here, we report Agrobacterium tumefaciens-mediated transformation (ATMT) of T. aurantiacus using the hph marker gene, conferring resistance to hygromycin B. The newly developed transformation protocol was optimized and used to integrate an expression cassette of the transcriptional xylanase regulator xlnR, which led to up to 500% increased xylanase activity. Furthermore, a CRISPR/Cas9 gene editing system was established in this fungus, and two different gRNAs were tested to delete the pyrG orthologue with 10% and 35% deletion efficiency, respectively. Lastly, a sexual crossing protocol was established using a hygromycin B- and a 5-fluoroorotic acid-resistant parent strain. Crossing and isolation of progeny on selective media were completed in a week. Conclusion The genetic tools developed for T. aurantiacus can now be used individually or in combination to further improve thermostable enzyme production by this fungus.

| S-EPMC7547499 | biostudies-literature

Purification and properties of an endoglucanase from <i>Thermoascus aurantiacus</i>.

Project description:An Endo-cellulase was purified to homogeneity using ammonium sulfate precipitation, ion exchange and size exclusion chromatography from newly isolated strain of Thermoascus aurantiacus RBB-1. The recovery and purification fold were 13.3% and 6.6, respectively, after size exclusion chromatography. The purified cellulase has a molecular mass (M) of 35 kDa. Optimum temperature for the enzyme was found to be 70 °C and stability was upto 80 °C for 1 h. Along with higher stability at 80 °C, enzyme showed half lives of 192 h and 144 h at 50 and 70 °C respectively. The purified cellulase was optimally active at pH 4.0 and was stable over a broad pH range of 3.0-7.0. The enzyme purified showed apparent Km and Vmax values of 37 mg/ml and 82.6 U/min/mg protein respectively with higher salt tolerance of 10% for 1 h.

| S-EPMC5466251 | biostudies-literature

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