The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin
<p>Abstract</p> <p>Background</p> <p>The enzymatic hydrolysis step converting lignocellulosic materials into fermentable sugars is recognized as one of the major limiting steps in biomass-to-ethanol process due to the low efficiency of enzymes and their cost. Xylanases...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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BMC
2013-01-01
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| Series: | Biotechnology for Biofuels |
| Subjects: | |
| Online Access: | http://www.biotechnologyforbiofuels.com/content/6/1/18 |
| _version_ | 1811340678329794560 |
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| author | Zhang Junhua Moilanen Ulla Tang Ming Viikari Liisa |
| author_facet | Zhang Junhua Moilanen Ulla Tang Ming Viikari Liisa |
| author_sort | Zhang Junhua |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>The enzymatic hydrolysis step converting lignocellulosic materials into fermentable sugars is recognized as one of the major limiting steps in biomass-to-ethanol process due to the low efficiency of enzymes and their cost. Xylanases have been found to be important in the improvement of the hydrolysis of cellulose due to the close interaction of cellulose and xylan. In this work, the effects of carbohydrate-binding module (CBM family II) of the xylanase 11 from <it>Nonomuraea flexuosa</it> (Nf Xyn11) on the adsorption and hydrolytic efficiency toward isolated xylan and lignocellulosic materials were investigated.</p> <p>Results</p> <p>The intact family 11 xylanase of <it>N. flexuosa</it> clearly adsorbed on wheat straw and lignin, following the Langmuir-type isotherm. The presence of the CBM in the xylanase increased the adsorption and hydrolytic efficiency on insoluble oat spelt xylan. But the presence of the CBM did not increase adsorption on pretreated wheat straw or isolated lignin. On the contrary, the CBM decreased the adsorption of the core protein to lignin containing substrates, indicating that the CBM of <it>N. flexuosa</it> xylanase did not contribute to the non-productive adsorption.</p> <p>Conclusion</p> <p>The CBM of the <it>N. flexuosa</it> xylanase was shown to be a xylan-binding module, which had low affinity on cellulose. The CBM of the <it>N. flexuosa</it> xylanase reduced the non-specific adsorption of the core protein to lignin and showed potential for improving the hydrolysis of lignocellulosic materials to platform sugars.</p> |
| first_indexed | 2024-04-13T18:45:27Z |
| format | Article |
| id | doaj.art-a22a914943ac4eb394cfa5cdb3ff9271 |
| institution | Directory Open Access Journal |
| issn | 1754-6834 |
| language | English |
| last_indexed | 2024-04-13T18:45:27Z |
| publishDate | 2013-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Biotechnology for Biofuels |
| spelling | doaj.art-a22a914943ac4eb394cfa5cdb3ff92712022-12-22T02:34:36ZengBMCBiotechnology for Biofuels1754-68342013-01-01611810.1186/1754-6834-6-18The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on ligninZhang JunhuaMoilanen UllaTang MingViikari Liisa<p>Abstract</p> <p>Background</p> <p>The enzymatic hydrolysis step converting lignocellulosic materials into fermentable sugars is recognized as one of the major limiting steps in biomass-to-ethanol process due to the low efficiency of enzymes and their cost. Xylanases have been found to be important in the improvement of the hydrolysis of cellulose due to the close interaction of cellulose and xylan. In this work, the effects of carbohydrate-binding module (CBM family II) of the xylanase 11 from <it>Nonomuraea flexuosa</it> (Nf Xyn11) on the adsorption and hydrolytic efficiency toward isolated xylan and lignocellulosic materials were investigated.</p> <p>Results</p> <p>The intact family 11 xylanase of <it>N. flexuosa</it> clearly adsorbed on wheat straw and lignin, following the Langmuir-type isotherm. The presence of the CBM in the xylanase increased the adsorption and hydrolytic efficiency on insoluble oat spelt xylan. But the presence of the CBM did not increase adsorption on pretreated wheat straw or isolated lignin. On the contrary, the CBM decreased the adsorption of the core protein to lignin containing substrates, indicating that the CBM of <it>N. flexuosa</it> xylanase did not contribute to the non-productive adsorption.</p> <p>Conclusion</p> <p>The CBM of the <it>N. flexuosa</it> xylanase was shown to be a xylan-binding module, which had low affinity on cellulose. The CBM of the <it>N. flexuosa</it> xylanase reduced the non-specific adsorption of the core protein to lignin and showed potential for improving the hydrolysis of lignocellulosic materials to platform sugars.</p>http://www.biotechnologyforbiofuels.com/content/6/1/18Carbohydrate binding moduleXylanaseAdsorptionXylan |
| spellingShingle | Zhang Junhua Moilanen Ulla Tang Ming Viikari Liisa The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin Biotechnology for Biofuels Carbohydrate binding module Xylanase Adsorption Xylan |
| title | The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin |
| title_full | The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin |
| title_fullStr | The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin |
| title_full_unstemmed | The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin |
| title_short | The carbohydrate-binding module of xylanase from <it>Nonomuraea flexuosa</it> decreases its non-productive adsorption on lignin |
| title_sort | carbohydrate binding module of xylanase from it nonomuraea flexuosa it decreases its non productive adsorption on lignin |
| topic | Carbohydrate binding module Xylanase Adsorption Xylan |
| url | http://www.biotechnologyforbiofuels.com/content/6/1/18 |
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