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Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover
Enzymatic conversion of oligomeric xylose and insoluble xylan remaining after effective pretreatment offers significant potential to improve xylan-to-xylose yields while minimizing yields of degredation products and fermentation inhibitors. In this work, a commercial enzyme cocktail is demonstrated...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458197/ https://www.ncbi.nlm.nih.gov/pubmed/22847186 http://dx.doi.org/10.1007/s12010-012-9786-5 |
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author | Shekiro, Joseph Kuhn, Erik M. Selig, Michael J. Nagle, Nicholas J. Decker, Stephen R. Elander, Richard T. |
author_facet | Shekiro, Joseph Kuhn, Erik M. Selig, Michael J. Nagle, Nicholas J. Decker, Stephen R. Elander, Richard T. |
author_sort | Shekiro, Joseph |
collection | PubMed |
description | Enzymatic conversion of oligomeric xylose and insoluble xylan remaining after effective pretreatment offers significant potential to improve xylan-to-xylose yields while minimizing yields of degredation products and fermentation inhibitors. In this work, a commercial enzyme cocktail is demonstrated to convert up to 70 % of xylo-oligomers found in dilute acid-pretreated hydrolyzate liquor at varying levels of dilution when supplemented with accessory enzymes targeting common side chains. Commercial enzyme cocktails are also shown to convert roughly 80 % of insoluble xylan remaining after effective high-solids, dilute acid pretreatment. |
format | Online Article Text |
id | pubmed-3458197 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-34581972013-07-15 Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover Shekiro, Joseph Kuhn, Erik M. Selig, Michael J. Nagle, Nicholas J. Decker, Stephen R. Elander, Richard T. Appl Biochem Biotechnol Article Enzymatic conversion of oligomeric xylose and insoluble xylan remaining after effective pretreatment offers significant potential to improve xylan-to-xylose yields while minimizing yields of degredation products and fermentation inhibitors. In this work, a commercial enzyme cocktail is demonstrated to convert up to 70 % of xylo-oligomers found in dilute acid-pretreated hydrolyzate liquor at varying levels of dilution when supplemented with accessory enzymes targeting common side chains. Commercial enzyme cocktails are also shown to convert roughly 80 % of insoluble xylan remaining after effective high-solids, dilute acid pretreatment. Springer-Verlag 2012-07-31 2012 /pmc/articles/PMC3458197/ /pubmed/22847186 http://dx.doi.org/10.1007/s12010-012-9786-5 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Article Shekiro, Joseph Kuhn, Erik M. Selig, Michael J. Nagle, Nicholas J. Decker, Stephen R. Elander, Richard T. Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title | Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title_full | Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title_fullStr | Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title_full_unstemmed | Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title_short | Enzymatic Conversion of Xylan Residues from Dilute Acid-Pretreated Corn Stover |
title_sort | enzymatic conversion of xylan residues from dilute acid-pretreated corn stover |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458197/ https://www.ncbi.nlm.nih.gov/pubmed/22847186 http://dx.doi.org/10.1007/s12010-012-9786-5 |
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