Publications des scientifiques de l'IRD

Ben Ayed A., Saint-Genis G., Vallon L., Linde D., Turbe-Doan A., Haon M., Daou M., Bertrand E., Faulds C. B., Sciara G., Adamo M., Marmeisse R., Comtet-Marre S., Peyret P., Abrouk D., Ruiz-Duenas F. J., Marchand Cyril, Hugoni M., Luis P., Mechichi T., Record E. (2021). Exploring the diversity of fungal DyPs in mangrove soils to produce and characterize novel biocatalysts. Journal of Fungi, 7 (5), 321 [23 p.].

Titre du document
Exploring the diversity of fungal DyPs in mangrove soils to produce and characterize novel biocatalysts
Année de publication
2021
Type de document
Article référencé dans le Web of Science WOS:000654160900001
Auteurs
Ben Ayed A., Saint-Genis G., Vallon L., Linde D., Turbe-Doan A., Haon M., Daou M., Bertrand E., Faulds C. B., Sciara G., Adamo M., Marmeisse R., Comtet-Marre S., Peyret P., Abrouk D., Ruiz-Duenas F. J., Marchand Cyril, Hugoni M., Luis P., Mechichi T., Record E.
Source
Journal of Fungi, 2021, 7 (5), 321 [23 p.]
The functional diversity of the New Caledonian mangrove sediments was examined, observing the distribution of fungal dye-decolorizing peroxidases (DyPs), together with the complete biochemical characterization of the main DyP. Using a functional metabarcoding approach, the diversity of expressed genes encoding fungal DyPs was investigated in surface and deeper sediments, collected beneath either Avicennia marina or Rhizophora stylosa trees, during either the wet or the dry seasons. The highest DyP diversity was observed in surface sediments beneath the R. stylosa area during the wet season, and one particular operational functional unit (OFU1) was detected as the most abundant DyP isoform. This OFU was found in all sediment samples, representing 51-100% of the total DyP-encoding sequences in 70% of the samples. The complete cDNA sequence corresponding to this abundant DyP (OFU 1) was retrieved by gene capture, cloned, and heterologously expressed in Pichia pastoris. The recombinant enzyme, called DyP1, was purified and characterized, leading to the description of its physical-chemical properties, its ability to oxidize diverse phenolic substrates, and its potential to decolorize textile dyes; DyP1 was more active at low pH, though moderately stable over a wide pH range. The enzyme was very stable at temperatures up to 50 degrees C, retaining 60% activity after 180 min incubation. Its ability to decolorize industrial dyes was also tested on Reactive Blue 19, Acid Black, Disperse Blue 79, and Reactive Black 5. The effect of hydrogen peroxide and sea salt on DyP1 activity was studied and compared to what is reported for previously characterized enzymes from terrestrial and marine-derived fungi.
Plan de classement
Sciences fondamentales / Techniques d'analyse et de recherche [020] ; Limnologie biologique / Océanographie biologique [034] ; Biologie du sol [074] ; Etudes, transformation, conservation du milieu naturel [082]
Description Géographique
NOUVELLE CALEDONIE
Localisation
Fonds IRD [F B010081517]
Identifiant IRD
fdi:010081517
Contact