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Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose

BACKGROUND: Plant expansins and fungal swollenin that can disrupt crystalline cellulose have great potential for applications in conversion of biomass. Recent studies have been mainly focused on Trichoderma reesei swollenin that show relatively low activity in the promotion of cellulosic hydrolysis....

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Autores principales: Kang, Kang, Wang, Shaowen, Lai, Guohong, Liu, Gang, Xing, Miao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681723/
https://www.ncbi.nlm.nih.gov/pubmed/23688024
http://dx.doi.org/10.1186/1472-6750-13-42
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author Kang, Kang
Wang, Shaowen
Lai, Guohong
Liu, Gang
Xing, Miao
author_facet Kang, Kang
Wang, Shaowen
Lai, Guohong
Liu, Gang
Xing, Miao
author_sort Kang, Kang
collection PubMed
description BACKGROUND: Plant expansins and fungal swollenin that can disrupt crystalline cellulose have great potential for applications in conversion of biomass. Recent studies have been mainly focused on Trichoderma reesei swollenin that show relatively low activity in the promotion of cellulosic hydrolysis. Our aim was to isolate a novel swollenin with greater disruptive activity, to establish an efficient way of producing recombinant swollenin, and to optimize the procedure using swollenin in facilitation of cellulosic hydrolysis. RESULTS: A novel gene encoding a swollenin-like protein, POSWOI, was isolated from the filamentous fungus Penicillium oxalicum by Thermal Asymmetric Interlaced PCR (TAIL-PCR). It consisted of a family 1 carbohydrate-binding module (CBM1) followed by a linker connected to a family 45 endoglucanase-like domain. Using the cellobiohydrolase I promoter, recombinant POSWOI was efficiently produced in T. reesei with a yield of 105 mg/L, and showed significant disruptive activity on crystalline cellulose. Simultaneous reaction with both POSWOI and cellulases enhanced the hydrolysis of crystalline cellulose Avicel by approximately 50%. Using a POSWOI-pretreatment procedure, cellulases can produce nearly twice as many reducing sugars as without pretreatment. The mechanism by which POSWOI facilitates the saccharification of cellulose was also studied using a cellulase binding assay. CONCLUSION: We present a novel fungal swollenin with considerable disruptive activity on crystalline cellulose, and develop a better procedure for using swollenin in facilitating cellulosic hydrolysis. We thus provide a new approach for the effective bioconversion of cellulosic biomass.
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spelling pubmed-36817232013-06-14 Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose Kang, Kang Wang, Shaowen Lai, Guohong Liu, Gang Xing, Miao BMC Biotechnol Research Article BACKGROUND: Plant expansins and fungal swollenin that can disrupt crystalline cellulose have great potential for applications in conversion of biomass. Recent studies have been mainly focused on Trichoderma reesei swollenin that show relatively low activity in the promotion of cellulosic hydrolysis. Our aim was to isolate a novel swollenin with greater disruptive activity, to establish an efficient way of producing recombinant swollenin, and to optimize the procedure using swollenin in facilitation of cellulosic hydrolysis. RESULTS: A novel gene encoding a swollenin-like protein, POSWOI, was isolated from the filamentous fungus Penicillium oxalicum by Thermal Asymmetric Interlaced PCR (TAIL-PCR). It consisted of a family 1 carbohydrate-binding module (CBM1) followed by a linker connected to a family 45 endoglucanase-like domain. Using the cellobiohydrolase I promoter, recombinant POSWOI was efficiently produced in T. reesei with a yield of 105 mg/L, and showed significant disruptive activity on crystalline cellulose. Simultaneous reaction with both POSWOI and cellulases enhanced the hydrolysis of crystalline cellulose Avicel by approximately 50%. Using a POSWOI-pretreatment procedure, cellulases can produce nearly twice as many reducing sugars as without pretreatment. The mechanism by which POSWOI facilitates the saccharification of cellulose was also studied using a cellulase binding assay. CONCLUSION: We present a novel fungal swollenin with considerable disruptive activity on crystalline cellulose, and develop a better procedure for using swollenin in facilitating cellulosic hydrolysis. We thus provide a new approach for the effective bioconversion of cellulosic biomass. BioMed Central 2013-05-20 /pmc/articles/PMC3681723/ /pubmed/23688024 http://dx.doi.org/10.1186/1472-6750-13-42 Text en Copyright © 2013 Kang et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Kang, Kang
Wang, Shaowen
Lai, Guohong
Liu, Gang
Xing, Miao
Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title_full Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title_fullStr Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title_full_unstemmed Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title_short Characterization of a novel swollenin from Penicillium oxalicum in facilitating enzymatic saccharification of cellulose
title_sort characterization of a novel swollenin from penicillium oxalicum in facilitating enzymatic saccharification of cellulose
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681723/
https://www.ncbi.nlm.nih.gov/pubmed/23688024
http://dx.doi.org/10.1186/1472-6750-13-42
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