Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we stu...
| Autores principales: | , , , , , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
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Springer
2022
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/12415 https://link.springer.com/article/10.1007/s00253-022-12061-3 https://doi.org/10.1007/s00253-022-12061-3 |
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| author | Garrido, Mercedes Maria Piccinni, Florencia Elizabeth Landoni, Malena Peña, María Jesús Topalian, Juliana Couto, Alicia Wirth, Sonia Alejandra Urbanowicz, Breeanna Rae Campos, Eleonora |
| author_browse | Campos, Eleonora Couto, Alicia Garrido, Mercedes Maria Landoni, Malena Peña, María Jesús Piccinni, Florencia Elizabeth Topalian, Juliana Urbanowicz, Breeanna Rae Wirth, Sonia Alejandra |
| author_facet | Garrido, Mercedes Maria Piccinni, Florencia Elizabeth Landoni, Malena Peña, María Jesús Topalian, Juliana Couto, Alicia Wirth, Sonia Alejandra Urbanowicz, Breeanna Rae Campos, Eleonora |
| author_sort | Garrido, Mercedes Maria |
| collection | INTA Digital |
| description | Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization. |
| format | info:ar-repo/semantics/artículo |
| id | INTA12415 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | INTA124152022-07-27T11:15:28Z Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A Garrido, Mercedes Maria Piccinni, Florencia Elizabeth Landoni, Malena Peña, María Jesús Topalian, Juliana Couto, Alicia Wirth, Sonia Alejandra Urbanowicz, Breeanna Rae Campos, Eleonora Hemicellulose Xylans Hemicelulosa Cellulomonas Xilanos Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization. Instituto de Biotecnología Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina Fil: Garrido, Mercedes Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Garrido, Mercedes Maria. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina Fil: Piccinni, Florencia Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Piccinni, Florencia Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Landoni, Malena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina Fil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Peña, María Jesús. University of Georgia. Complex Carbohydrate Research Center; Estados Unidos Fil: Topalian, Juliana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina Fil: Topalian, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Couto, Alicia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina Fil: Wirth, Sonia Alejandra. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Urbanowicz, Breeanna Rae. University of Georgia. Department of Biochemistry and Molecular Biology; Estados Unidos Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 2022-07-27T11:10:21Z 2022-07-27T11:10:21Z 2022 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/12415 https://link.springer.com/article/10.1007/s00253-022-12061-3 1432-0614 https://doi.org/10.1007/s00253-022-12061-3 eng info:eu-repograntAgreement/INTA/2019-PD-E6-I116-001/2019-PD-E6-I116-001/AR./Identificación y análisis funcional de genes o redes génicas de interés biotecnológico con fin agropecuario, forestal, agroalimentario y/o agroindustrial. info:eu-repograntAgreement/INTA/2019-PD-E7-I152-001/2019-PD-E7-I152-001/AR./Alimentos nutracéuticos, funcionales o para regímenes especiales. info:eu-repograntAgreement/INTA/2019-PE-E7-I149-001/2019-PE-E7-I149-001/AR./Bioenergía generada en origen como aporte al desarrollo territorial info:eu-repo/semantics/restrictedAccess application/pdf Springer Applied Microbiology and Biotechnology (Published: 08 July 2022) |
| spellingShingle | Hemicellulose Xylans Hemicelulosa Cellulomonas Xilanos Garrido, Mercedes Maria Piccinni, Florencia Elizabeth Landoni, Malena Peña, María Jesús Topalian, Juliana Couto, Alicia Wirth, Sonia Alejandra Urbanowicz, Breeanna Rae Campos, Eleonora Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title | Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title_full | Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title_fullStr | Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title_full_unstemmed | Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title_short | Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A |
| title_sort | insights into the xylan degradation system of cellulomonas sp b6 biochemical characterization of rcsxyn10a and rcsabf62a |
| topic | Hemicellulose Xylans Hemicelulosa Cellulomonas Xilanos |
| url | http://hdl.handle.net/20.500.12123/12415 https://link.springer.com/article/10.1007/s00253-022-12061-3 https://doi.org/10.1007/s00253-022-12061-3 |
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