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Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan

Xylanases with high specific activity has been focused with great interest as a useful enzyme in biomass utilization. The production of recombinant GH11 xylanase (MYCTH_56237) from Myceliophthora thermophila has been improved through N-terminal signal peptide engineering in P. pastoris. The producti...

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Autores principales: Miao, Ting, Basit, Abdul, Liu, Junquan, Zheng, Fengzhen, Rahim, Kashif, Lou, Huiqiang, Jiang, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8429496/
https://www.ncbi.nlm.nih.gov/pubmed/34513809
http://dx.doi.org/10.3389/fbioe.2021.690702
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author Miao, Ting
Basit, Abdul
Liu, Junquan
Zheng, Fengzhen
Rahim, Kashif
Lou, Huiqiang
Jiang, Wei
author_facet Miao, Ting
Basit, Abdul
Liu, Junquan
Zheng, Fengzhen
Rahim, Kashif
Lou, Huiqiang
Jiang, Wei
author_sort Miao, Ting
collection PubMed
description Xylanases with high specific activity has been focused with great interest as a useful enzyme in biomass utilization. The production of recombinant GH11 xylanase (MYCTH_56237) from Myceliophthora thermophila has been improved through N-terminal signal peptide engineering in P. pastoris. The production of newly recombinant xylanase (termed Mtxyn11C) was improved from 442.53 to 490.7 U/mL, through a replacement of α-factor signal peptide with the native xylanase signal peptide segment (MVSVKAVLLLGAAGTTLA) in P. pastoris. Scaling up of Mtxyn11C production in a 7.5 L fermentor was improved to the maximal production rate of 2503 U/mL. In this study, the degradation efficiency of Mtxyn11C was further examined. Analysis of the hydrolytic mode of action towards the birchwood xylan (BWX) revealed that Mtxyn11C was clearly more effective than commercial xylanase and degrades xylan into xylooligosaccharides (xylobiose, xylotriose, xylotetraose). More importantly, Mtxyn11C in combination with a single multifunctional xylanolytic enzyme, improved the hydrolysis of BWX into single xylose by 40%. Altogether, this study provided strategies for improved production of xylanase together with rapid conversion of xylose from BWX, which provides sustainable, cost-effective and environmental friendly approaches to produce xylose/XOSs for biomass energy or biofuels production.
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spelling pubmed-84294962021-09-11 Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan Miao, Ting Basit, Abdul Liu, Junquan Zheng, Fengzhen Rahim, Kashif Lou, Huiqiang Jiang, Wei Front Bioeng Biotechnol Bioengineering and Biotechnology Xylanases with high specific activity has been focused with great interest as a useful enzyme in biomass utilization. The production of recombinant GH11 xylanase (MYCTH_56237) from Myceliophthora thermophila has been improved through N-terminal signal peptide engineering in P. pastoris. The production of newly recombinant xylanase (termed Mtxyn11C) was improved from 442.53 to 490.7 U/mL, through a replacement of α-factor signal peptide with the native xylanase signal peptide segment (MVSVKAVLLLGAAGTTLA) in P. pastoris. Scaling up of Mtxyn11C production in a 7.5 L fermentor was improved to the maximal production rate of 2503 U/mL. In this study, the degradation efficiency of Mtxyn11C was further examined. Analysis of the hydrolytic mode of action towards the birchwood xylan (BWX) revealed that Mtxyn11C was clearly more effective than commercial xylanase and degrades xylan into xylooligosaccharides (xylobiose, xylotriose, xylotetraose). More importantly, Mtxyn11C in combination with a single multifunctional xylanolytic enzyme, improved the hydrolysis of BWX into single xylose by 40%. Altogether, this study provided strategies for improved production of xylanase together with rapid conversion of xylose from BWX, which provides sustainable, cost-effective and environmental friendly approaches to produce xylose/XOSs for biomass energy or biofuels production. Frontiers Media S.A. 2021-08-27 /pmc/articles/PMC8429496/ /pubmed/34513809 http://dx.doi.org/10.3389/fbioe.2021.690702 Text en Copyright © 2021 Miao, Basit, Liu, Zheng, Rahim, Lou and Jiang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Miao, Ting
Basit, Abdul
Liu, Junquan
Zheng, Fengzhen
Rahim, Kashif
Lou, Huiqiang
Jiang, Wei
Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title_full Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title_fullStr Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title_full_unstemmed Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title_short Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan
title_sort improved production of xylanase in pichia pastoris and its application in xylose production from xylan
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8429496/
https://www.ncbi.nlm.nih.gov/pubmed/34513809
http://dx.doi.org/10.3389/fbioe.2021.690702
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