GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
A novel bacterial isolate with polysaccharides degrading activity was identified as Paenibacillus sp., andnamed Paenibacillus sp. A59. Even though it is a strict mesophile, optimal xylanase activity of the crudeenzymatic extract was achieved between 50◦C and 70◦C and more than 60% of the activity wa...
| Autores principales: | , , , , , |
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| Formato: | info:eu-repo/semantics/article |
| Lenguaje: | Inglés |
| Publicado: |
2017
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| Acceso en línea: | http://hdl.handle.net/20.500.12123/986 http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73 https://doi.org/10.1016/j.micres.2016.02.006 |
| _version_ | 1855034739247808512 |
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| author | Ghio, Silvina Insani, Ester Marina Piccinni, Florencia Elizabeth Talia, Paola Mónica Grasso, Daniel Horacio Campos, Eleonora |
| author_browse | Campos, Eleonora Ghio, Silvina Grasso, Daniel Horacio Insani, Ester Marina Piccinni, Florencia Elizabeth Talia, Paola Mónica |
| author_facet | Ghio, Silvina Insani, Ester Marina Piccinni, Florencia Elizabeth Talia, Paola Mónica Grasso, Daniel Horacio Campos, Eleonora |
| author_sort | Ghio, Silvina |
| collection | INTA Digital |
| description | A novel bacterial isolate with polysaccharides degrading activity was identified as Paenibacillus sp., andnamed Paenibacillus sp. A59. Even though it is a strict mesophile, optimal xylanase activity of the crudeenzymatic extract was achieved between 50◦C and 70◦C and more than 60% of the activity was retainedafter incubation for 48 h at 50◦C, indicating thermotolerance of the enzymes involved. The extract wasalso active on pre-treated sugarcane residue (SCR) and wheat straw, releasing xylobiose and xylose asthe main products, therefore confirming its predominantly xylanolytic activity. By zymograms and massspectrometry of crude enzymatic extracts of xylan or SCR cultures, a 32 kDa GH10 beta- 1,4- endoxylanasewith xylanase and no CMCase activity was identified. We named this enzyme XynA and it was the onlyxylanase identified under both conditions assayed, suggesting that it is a good candidate for recombinantexpression and evaluation in hemicelluloses deconstruction applications. Also, a protein with two S-layerhomology domains (SLH) and a large uncharacterized C-terminal domain as well as an ABC substratebinding protein were identified in crude extracts of SCR cultures. We propose that Paenibacillus sp. A59uses a system similar to anaerobic and other Gram positive bacteria, with SLH-domain proteins anchoringpolysaccharide-degrading enzymes close to the membrane and the substrate binding protein assistingtranslocation of simple sugars to the cell interior. |
| format | info:eu-repo/semantics/article |
| id | INTA986 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2017 |
| publishDateRange | 2017 |
| publishDateSort | 2017 |
| record_format | dspace |
| spelling | INTA9862018-02-26T13:58:10Z GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass Ghio, Silvina Insani, Ester Marina Piccinni, Florencia Elizabeth Talia, Paola Mónica Grasso, Daniel Horacio Campos, Eleonora Biomasa Paenibacillus Lignocelulosa Xilanos Biomass Lignocellulose Xylans A novel bacterial isolate with polysaccharides degrading activity was identified as Paenibacillus sp., andnamed Paenibacillus sp. A59. Even though it is a strict mesophile, optimal xylanase activity of the crudeenzymatic extract was achieved between 50◦C and 70◦C and more than 60% of the activity was retainedafter incubation for 48 h at 50◦C, indicating thermotolerance of the enzymes involved. The extract wasalso active on pre-treated sugarcane residue (SCR) and wheat straw, releasing xylobiose and xylose asthe main products, therefore confirming its predominantly xylanolytic activity. By zymograms and massspectrometry of crude enzymatic extracts of xylan or SCR cultures, a 32 kDa GH10 beta- 1,4- endoxylanasewith xylanase and no CMCase activity was identified. We named this enzyme XynA and it was the onlyxylanase identified under both conditions assayed, suggesting that it is a good candidate for recombinantexpression and evaluation in hemicelluloses deconstruction applications. Also, a protein with two S-layerhomology domains (SLH) and a large uncharacterized C-terminal domain as well as an ABC substratebinding protein were identified in crude extracts of SCR cultures. We propose that Paenibacillus sp. A59uses a system similar to anaerobic and other Gram positive bacteria, with SLH-domain proteins anchoringpolysaccharide-degrading enzymes close to the membrane and the substrate binding protein assistingtranslocation of simple sugars to the cell interior. Inst. de Biotecnología Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina Fil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina 2017-08-16T17:23:17Z 2017-08-16T17:23:17Z 2016 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion info:ar-repo/semantics/artículo http://hdl.handle.net/20.500.12123/986 http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73 0944-5013 https://doi.org/10.1016/j.micres.2016.02.006 eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf Microbiological research 186–187 : 16-26. (May–June 2016) |
| spellingShingle | Biomasa Paenibacillus Lignocelulosa Xilanos Biomass Lignocellulose Xylans Ghio, Silvina Insani, Ester Marina Piccinni, Florencia Elizabeth Talia, Paola Mónica Grasso, Daniel Horacio Campos, Eleonora GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title | GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title_full | GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title_fullStr | GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title_full_unstemmed | GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title_short | GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass |
| title_sort | gh10 xyna is the main xylanase identified in the crude enzymatic extract of paenibacillus sp a59 when grown on xylan or lignocellulosic biomass |
| topic | Biomasa Paenibacillus Lignocelulosa Xilanos Biomass Lignocellulose Xylans |
| url | http://hdl.handle.net/20.500.12123/986 http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73 https://doi.org/10.1016/j.micres.2016.02.006 |
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