Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity
Mangrove sediments from New Caledonia were screened for xylanase sequences. One enzyme was selected and characterized both biochemically and for its industrial potential. Using a specific cDNA amplification method coupled with a MiSeq sequencing approach, the diversity of expressed genes encoding GH...
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MDPI AG
2021-07-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/9/7/1484 |
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| author | Corinne Ivaldi Mariane Daou Laurent Vallon Alexandra Bisotto Mireille Haon Sona Garajova Emmanuel Bertrand Craig B. Faulds Giuliano Sciara Adrien Jacotot Cyril Marchand Mylène Hugoni Harivony Rakotoarivonina Marie-Noëlle Rosso Caroline Rémond Patricia Luis Eric Record |
| author_facet | Corinne Ivaldi Mariane Daou Laurent Vallon Alexandra Bisotto Mireille Haon Sona Garajova Emmanuel Bertrand Craig B. Faulds Giuliano Sciara Adrien Jacotot Cyril Marchand Mylène Hugoni Harivony Rakotoarivonina Marie-Noëlle Rosso Caroline Rémond Patricia Luis Eric Record |
| author_sort | Corinne Ivaldi |
| collection | DOAJ |
| description | Mangrove sediments from New Caledonia were screened for xylanase sequences. One enzyme was selected and characterized both biochemically and for its industrial potential. Using a specific cDNA amplification method coupled with a MiSeq sequencing approach, the diversity of expressed genes encoding GH11 xylanases was investigated beneath <i>Avicenia marina</i> and <i>Rhizophora stylosa</i> trees during the wet and dry seasons and at two different sediment depths. GH11 xylanase diversity varied more according to tree species and season, than with respect to depth. One complete cDNA was selected (OFU29) and expressed in <i>Pichia pastoris</i>. The corresponding enzyme (called Xyn11-29) was biochemically characterized, revealing an optimal activity at 40–50 °C and at a pH of 5.5. Xyn11-29 was stable for 48 h at 35 °C, with a half-life of 1 h at 40 °C and in the pH range of 5.5–6. Xyn11-29 exhibited a high hydrolysis capacity on destarched wheat bran, with 40% and 16% of xylose and arabinose released after 24 h hydrolysis. Its activity on wheat straw was lower, with a release of 2.8% and 6.9% of xylose and arabinose, respectively. As the protein was isolated from mangrove sediments, the effect of sea salt on its activity was studied and discussed. |
| first_indexed | 2024-03-10T09:31:38Z |
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| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T09:31:38Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-94f25a67212c4184b0d48a70b818d7a62023-11-22T04:26:26ZengMDPI AGMicroorganisms2076-26072021-07-0197148410.3390/microorganisms9071484Screening New Xylanase Biocatalysts from the Mangrove Soil DiversityCorinne Ivaldi0Mariane Daou1Laurent Vallon2Alexandra Bisotto3Mireille Haon4Sona Garajova5Emmanuel Bertrand6Craig B. Faulds7Giuliano Sciara8Adrien Jacotot9Cyril Marchand10Mylène Hugoni11Harivony Rakotoarivonina12Marie-Noëlle Rosso13Caroline Rémond14Patricia Luis15Eric Record16INRAE, FARE, UMR A 614, Chaire AFERE, Université de Reims Champagne Ardenne, 51097 Reims, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceCNRS, INRAE, VetAgro Sup, UMR Ecologie Microbienne, Université Lyon, Université Claude Bernard Lyon 1, F-69622 Villeurbanne, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceInstitut de Recherche pour le Développement (IRD), IMPMC, UPMC, CNRS, MNHN, 98851 Noumea, New Caledonia, FranceInstitut de Recherche pour le Développement (IRD), IMPMC, UPMC, CNRS, MNHN, 98851 Noumea, New Caledonia, FranceCNRS, INRAE, VetAgro Sup, UMR Ecologie Microbienne, Université Lyon, Université Claude Bernard Lyon 1, F-69622 Villeurbanne, FranceINRAE, FARE, UMR A 614, Chaire AFERE, Université de Reims Champagne Ardenne, 51097 Reims, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceINRAE, FARE, UMR A 614, Chaire AFERE, Université de Reims Champagne Ardenne, 51097 Reims, FranceCNRS, INRAE, VetAgro Sup, UMR Ecologie Microbienne, Université Lyon, Université Claude Bernard Lyon 1, F-69622 Villeurbanne, FranceINRAE, UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, 13288 Marseille, FranceMangrove sediments from New Caledonia were screened for xylanase sequences. One enzyme was selected and characterized both biochemically and for its industrial potential. Using a specific cDNA amplification method coupled with a MiSeq sequencing approach, the diversity of expressed genes encoding GH11 xylanases was investigated beneath <i>Avicenia marina</i> and <i>Rhizophora stylosa</i> trees during the wet and dry seasons and at two different sediment depths. GH11 xylanase diversity varied more according to tree species and season, than with respect to depth. One complete cDNA was selected (OFU29) and expressed in <i>Pichia pastoris</i>. The corresponding enzyme (called Xyn11-29) was biochemically characterized, revealing an optimal activity at 40–50 °C and at a pH of 5.5. Xyn11-29 was stable for 48 h at 35 °C, with a half-life of 1 h at 40 °C and in the pH range of 5.5–6. Xyn11-29 exhibited a high hydrolysis capacity on destarched wheat bran, with 40% and 16% of xylose and arabinose released after 24 h hydrolysis. Its activity on wheat straw was lower, with a release of 2.8% and 6.9% of xylose and arabinose, respectively. As the protein was isolated from mangrove sediments, the effect of sea salt on its activity was studied and discussed.https://www.mdpi.com/2076-2607/9/7/1484lignocellulose degrading enzymesxylanasesheterologous expressionbiomass degradationmarine fungusmangrove |
| spellingShingle | Corinne Ivaldi Mariane Daou Laurent Vallon Alexandra Bisotto Mireille Haon Sona Garajova Emmanuel Bertrand Craig B. Faulds Giuliano Sciara Adrien Jacotot Cyril Marchand Mylène Hugoni Harivony Rakotoarivonina Marie-Noëlle Rosso Caroline Rémond Patricia Luis Eric Record Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity Microorganisms lignocellulose degrading enzymes xylanases heterologous expression biomass degradation marine fungus mangrove |
| title | Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity |
| title_full | Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity |
| title_fullStr | Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity |
| title_full_unstemmed | Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity |
| title_short | Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity |
| title_sort | screening new xylanase biocatalysts from the mangrove soil diversity |
| topic | lignocellulose degrading enzymes xylanases heterologous expression biomass degradation marine fungus mangrove |
| url | https://www.mdpi.com/2076-2607/9/7/1484 |
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