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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...

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Autores principales: Scott, Brian R., Huang, Hong Zhi, Frickman, Jesper, Halvorsen, Rune, Johansen, Katja S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2015
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.
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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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