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Coriolopsis trogii

ABSTRACT: Coriolopsis trogii overview

PROVIDER: PRJNA747578 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
		Other
	SZVL01.dat.gz	Other
	SZVL01.fasta.gz	Fasta.gz
	SZVL01.master.dat	Other
	SRR15182900_1.fastq.gz	Fastqsanger.gz

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Project description:Six new furan derivatives, named 5-(3-methoxy-3-oxopropyl)-furan-2-carboxylic acid (1), 1-(5-(2-hydroxypropanoyl)-furan-2-yl)-pentan-3-one (2), 2-hydroxy-1-(5-(1-hydroxypentyl)-furan-2-yl)-propan-1-one (3), 1-(5-(1,2-dihydroxypropyl)-furan-2-yl)-pentan-1-one (4), 5-(1-hydroxypent-4-en-1-yl)-furan-2-carboxylic acid (5) and 5-(3-hydroxypentyl)-furan-2-carboxylic acid (6), together with two new natural products, named 5-(1-hydroxypentyl)-furan-2-carboxylic acid (7) and (E)-5-(2-carboxyvinyl)-furan-2-carboxylic acid (8), were isolated from the solid rice fermentation of endophytic fungus Coriolopsis sp. J5, which was derived from mangrove plant Ceriops tagal. Their structures were unambiguously elucidated based on 1D and 2D NMR spectroscopy, and by HRESIMS measurements, as well as by comparison with the literature.

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Green production of a yellow laccase by Coriolopsis gallica for phenolic pollutants removal.

Project description:As a group of green biocatalysts, fungal laccases have aroused great interest in diverse biotechnological fields. Therein, yellow laccase has advantages over blue laccase in catalytic performance, but it is not common in the reported fungal laccases. Here, we report a yellow laccase from white-rot fungus Coriolopsis gallica NCULAC F1 about its production, purification, characterization, and application. Laccase production in the co-fermentation of pomelo peel and wheat bran reached the enzyme activity by 10,690 U/L after 5 days with a 13.58-time increase. After three steps of purification, laccase increased the specific activity from 30.78 to 188.79 U/mg protein with an activity recovery of 45.64%. The purified C. gallica laccase (CGLac) showed a molecular mass of about 57 kDa. CGLac had a yellow color and no absorption peaks at 610 nm and 330 nm, suggesting that it's a yellow laccase. CGLac exhibited stability towards temperature (40-60 °C) and neutral pH (6.0-8.0). Fe3+ and Mn2+ strongly stimulated CGLac activity by 162.56% and 226.05%, respectively. CGLac remained high activities when exposed to organic reagents and putative inhibitors. Additionally, CGLac contributed to 90.78%, 93.26%, and 99.66% removal of phenol, p-chlorophenol and bisphenol A after 120 min, respectively. In conclusion, a green efficient production strategy was introduced for fungal laccase, and the obtained CGLac presented great enzymatic properties and catalytic potential in the removal of phenolic pollutants.

| S-EPMC9288578 | biostudies-literature

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