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Compost metagenome

ABSTRACT: eukaryotic community analysis

PROVIDER: PRJDB2331 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR003887.fastq.gz	Fastqsanger.gz
	DRR003888.fastq.gz	Fastqsanger.gz
	DRR003889.fastq.gz	Fastqsanger.gz
	DRR003890.fastq.gz	Fastqsanger.gz
	DRR003891.fastq.gz	Fastqsanger.gz

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compost metagenome

Project description:structural analysis of microbial community for feild soil and compost made from coffee lees

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Characterisation of three novel α-L-arabinofuranosidases from a compost metagenome.

Project description:BackgroundThe importance of the accessory enzymes such as α-L-arabinofuranosidases (AFases) in synergistic interactions within cellulolytic mixtures has introduced a paradigm shift in the search for hydrolytic enzymes. The aim of this study was to characterize novel AFase genes encoding enzymes with differing temperature optima and thermostabilities for use in hydrolytic cocktails.ResultsThree fosmids, pFos-H4, E3 and D3 were selected from the cloned metagenome of high temperature compost, expressed in Escherichia coli and subsequently purified to homogeneity from cell lysate. All the AFases were clustered within the GH51 AFase family and shared a homo-hexameric structure. Both AFase-E3 and H4 showed optimal activity at 60 °C while AFase-D3 had unique properties as it showed optimal activity at 25 °C as well as the ability to maintain substantial activity at temperatures as high as 90 °C. However, AFase-E3 was the most thermostable amongst the three AFases showing full activity even at 70 °C. The maximum activity was observed at a pH profile between pH 4.0-6.0 for all three AFases with optimal activity for AFase H4, D3 and E3 at pH 5.0, 4.5 and 4.0, respectively. All the AFases showed KM range between 0.31 mM and 0.43 mM, Kcat range between 131 s- 1 and 219 s- 1 and the specific activity for AFase-H4, AFases-E3 and was 143, 228 and 175 U/mg, respectively. AFases-E3 and D3 displayed activities against pNP-β-L-arabinopyranoside and pNP-β-L-mannopyranoside respectively, and both hydrolysed pNP-β-D-glucopyranoside.ConclusionAll three AFases displayed different biochemical characteristics despite all showing conserved overall structural similarity with typical domains of AFases belonging to GH51 family. The hydrolysis of cellobiose by a GH51 family AFase is demonstrated for the first time in this study.

| S-EPMC6472066 | biostudies-literature

compost metagenome

Project description:metagenome of compost fungal community Metagenome

| PRJNA288412 | ENA

compost metagenome

Project description:Bacterial community during oyster mushroom (Pleurotus ostreatus) production

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soil metagenome

Project description:wetland eukaryotic community

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eukaryotic metagenome

Project description:airborne eukaryotic community

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aquatic metagenome

Project description:Eukaryotic community Metagenome

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Discovery and characterization of a thermostable two-domain GH6 endoglucanase from a compost metagenome.

Project description:Enzymatic depolymerization of recalcitrant polysaccharides plays a key role in accessing the renewable energy stored within lignocellulosic biomass, and natural biodiversities may be explored to discover microbial enzymes that have evolved to conquer this task in various environments. Here, a metagenome from a thermophilic microbial community was mined to yield a novel, thermostable cellulase, named mgCel6A, with activity on an industrial cellulosic substrate (sulfite-pulped Norway spruce) and a glucomannanase side activity. The enzyme consists of a glycoside hydrolase family 6 catalytic domain (GH6) and a family 2 carbohydrate binding module (CBM2) that are connected by a linker rich in prolines and threonines. MgCel6A exhibited maximum activity at 85°C and pH 5.0 on carboxymethyl cellulose (CMC), but in prolonged incubations with the industrial substrate, the highest yields were obtained at 60°C, pH 6.0. Differential scanning calorimetry (DSC) indicated a Tm(app) of 76°C. Both functional data and the crystal structure, solved at 1.88 Å resolution, indicate that mgCel6A is an endoglucanase. Comparative studies with a truncated variant of the enzyme showed that the CBM increases substrate binding, while not affecting thermal stability. Importantly, at higher substrate concentrations the full-length enzyme was outperformed by the catalytic domain alone, underpinning previous suggestions that CBMs may be less useful in high-consistency bioprocessing.

| S-EPMC5968413 | biostudies-literature

compost metagenome

Project description:Bacterial community changes during substrate preparation for oyster mushroom cultivation

| PRJNA397447 | ENA

lake water metagenome

Project description:Lake eukaryotic community

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