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Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation
OBJECTIVES: Efficient enzymatic saccharification of plant cell wall material is key to industrial processing of agricultural and forestry waste such as straw and wood chips into fuels and chemicals. RESULTS: Saccharification assays were performed on steam-pretreated wheat straw under ambient and O(2...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767857/ https://www.ncbi.nlm.nih.gov/pubmed/26543036 http://dx.doi.org/10.1007/s10529-015-1989-8 |
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author | Scott, Brian R. Huang, Hong Zhi Frickman, Jesper Halvorsen, Rune Johansen, Katja S. |
author_facet | Scott, Brian R. Huang, Hong Zhi Frickman, Jesper Halvorsen, Rune Johansen, Katja S. |
author_sort | Scott, Brian R. |
collection | PubMed |
description | OBJECTIVES: Efficient enzymatic saccharification of plant cell wall material is key to industrial processing of agricultural and forestry waste such as straw and wood chips into fuels and chemicals. RESULTS: Saccharification assays were performed on steam-pretreated wheat straw under ambient and O(2)-deprived environments and in the absence and presence of a lytic polysaccharide monooxygenase (LPMO) and catalase. A kinetic model was used to calculate catalytic rate and first-order inactivation rate constants of the cellulases from reaction progress curves. The addition of a LPMO significantly (P < 0.01, Student’s T test) enhanced the rate of glucose release from 2.8 to 6.9 h(−1) under ambient O(2) conditions. However, this also significantly (P < 0.01, Student’s T test) increased the rate of inactivation of the enzyme mixture, thereby reducing the performance half-life from 65 to 35 h. Decreasing O(2) levels or, strikingly, the addition of catalase significantly reduced (P < 0.01, Student’s T test) enzyme inactivation and, as a consequence, higher efficiency of the cellulolytic enzyme cocktail was achieved. CONCLUSION: Oxidative inactivation of commercial cellulase mixtures is a significant factor influencing the overall saccharification efficiency and the addition of catalase can be used to protect these mixtures from inactivation. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10529-015-1989-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4767857 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-47678572016-03-29 Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation Scott, Brian R. Huang, Hong Zhi Frickman, Jesper Halvorsen, Rune Johansen, Katja S. Biotechnol Lett Original Research Paper OBJECTIVES: Efficient enzymatic saccharification of plant cell wall material is key to industrial processing of agricultural and forestry waste such as straw and wood chips into fuels and chemicals. RESULTS: Saccharification assays were performed on steam-pretreated wheat straw under ambient and O(2)-deprived environments and in the absence and presence of a lytic polysaccharide monooxygenase (LPMO) and catalase. A kinetic model was used to calculate catalytic rate and first-order inactivation rate constants of the cellulases from reaction progress curves. The addition of a LPMO significantly (P < 0.01, Student’s T test) enhanced the rate of glucose release from 2.8 to 6.9 h(−1) under ambient O(2) conditions. However, this also significantly (P < 0.01, Student’s T test) increased the rate of inactivation of the enzyme mixture, thereby reducing the performance half-life from 65 to 35 h. Decreasing O(2) levels or, strikingly, the addition of catalase significantly reduced (P < 0.01, Student’s T test) enzyme inactivation and, as a consequence, higher efficiency of the cellulolytic enzyme cocktail was achieved. CONCLUSION: Oxidative inactivation of commercial cellulase mixtures is a significant factor influencing the overall saccharification efficiency and the addition of catalase can be used to protect these mixtures from inactivation. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10529-015-1989-8) contains supplementary material, which is available to authorized users. Springer Netherlands 2015-11-05 2016 /pmc/articles/PMC4767857/ /pubmed/26543036 http://dx.doi.org/10.1007/s10529-015-1989-8 Text en © The Author(s) 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Research Paper Scott, Brian R. Huang, Hong Zhi Frickman, Jesper Halvorsen, Rune Johansen, Katja S. Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title | Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title_full | Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title_fullStr | Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title_full_unstemmed | Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title_short | Catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
title_sort | catalase improves saccharification of lignocellulose by reducing lytic polysaccharide monooxygenase-associated enzyme inactivation |
topic | Original Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4767857/ https://www.ncbi.nlm.nih.gov/pubmed/26543036 http://dx.doi.org/10.1007/s10529-015-1989-8 |
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