High activity CAZyme cassette for improving biomass degradation in thermophiles
Abstract Background Thermophilic microorganisms and their enzymes offer several advantages for industrial application over their mesophilic counterparts. For example, a hyperthermophilic anaerobe, Caldicellulosiruptor bescii, was recently isolated from hot springs in Kamchatka, Siberia, and shown to...
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ftdoajarticles:oai:doaj.org/article:97f1d72c32114de4891a86d522dddfa2 2023-05-15T16:59:27+02:00 High activity CAZyme cassette for improving biomass degradation in thermophiles Roman Brunecky Daehwan Chung Nicholas S. Sarai Neal Hengge Jordan F. Russell Jenna Young Ashutosh Mittal Patthra Pason Todd Vander Wall William Michener Todd Shollenberger Janet Westpheling Michael E. Himmel Yannick J. Bomble 2018-02-01T00:00:00Z https://doi.org/10.1186/s13068-018-1014-2 https://doaj.org/article/97f1d72c32114de4891a86d522dddfa2 EN eng BMC http://link.springer.com/article/10.1186/s13068-018-1014-2 https://doaj.org/toc/1754-6834 doi:10.1186/s13068-018-1014-2 1754-6834 https://doaj.org/article/97f1d72c32114de4891a86d522dddfa2 Biotechnology for Biofuels, Vol 11, Iss 1, Pp 1-12 (2018) Biofuels Biomass degrading enzymes Cellulose Biomass Thermophile Caldicellulosiruptor bescii Fuel TP315-360 Biotechnology TP248.13-248.65 article 2018 ftdoajarticles https://doi.org/10.1186/s13068-018-1014-2 2022-12-30T23:17:28Z Abstract Background Thermophilic microorganisms and their enzymes offer several advantages for industrial application over their mesophilic counterparts. For example, a hyperthermophilic anaerobe, Caldicellulosiruptor bescii, was recently isolated from hot springs in Kamchatka, Siberia, and shown to have very high cellulolytic activity. Additionally, it is one of a few microorganisms being considered as viable candidates for consolidated bioprocessing applications. Moreover, C. bescii is capable of deconstructing plant biomass without enzymatic or chemical pretreatment. This ability is accomplished by the production and secretion of free, multi-modular and multi-functional enzymes, one of which, CbCel9A/Cel48A also known as CelA, is able to outperform enzymes found in commercial enzyme preparations. Furthermore, the complete C. bescii exoproteome is extremely thermostable and highly active at elevated temperatures, unlike commercial fungal cellulases. Therefore, understanding the functional diversity of enzymes in the C. bescii exoproteome and how inter-molecular synergy between them confers C. bescii with its high cellulolytic activity is an important endeavor to enable the production of more efficient biomass degrading enzyme formulations and in turn, better cellulolytic industrial microorganisms. Results To advance the understanding of the C. bescii exoproteome we have expressed, purified, and tested four of the primary enzymes found in the exoproteome and we have found that the combination of three or four of the most highly expressed enzymes exhibit synergistic activity. We also demonstrated that discrete combinations of these enzymes mimic and even improve upon the activity of the whole C. bescii exoproteome, even though some of the enzymes lack significant activity on their own. Conclusions We have demonstrated that it is possible to replicate the cellulolytic activity of the native C. bescii exoproteome utilizing a minimal gene set, and that these minimal gene sets are more active than the whole ... Article in Journal/Newspaper Kamchatka Siberia Directory of Open Access Journals: DOAJ Articles Biotechnology for Biofuels 11 1 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Biofuels Biomass degrading enzymes Cellulose Biomass Thermophile Caldicellulosiruptor bescii Fuel TP315-360 Biotechnology TP248.13-248.65 |
spellingShingle |
Biofuels Biomass degrading enzymes Cellulose Biomass Thermophile Caldicellulosiruptor bescii Fuel TP315-360 Biotechnology TP248.13-248.65 Roman Brunecky Daehwan Chung Nicholas S. Sarai Neal Hengge Jordan F. Russell Jenna Young Ashutosh Mittal Patthra Pason Todd Vander Wall William Michener Todd Shollenberger Janet Westpheling Michael E. Himmel Yannick J. Bomble High activity CAZyme cassette for improving biomass degradation in thermophiles |
topic_facet |
Biofuels Biomass degrading enzymes Cellulose Biomass Thermophile Caldicellulosiruptor bescii Fuel TP315-360 Biotechnology TP248.13-248.65 |
description |
Abstract Background Thermophilic microorganisms and their enzymes offer several advantages for industrial application over their mesophilic counterparts. For example, a hyperthermophilic anaerobe, Caldicellulosiruptor bescii, was recently isolated from hot springs in Kamchatka, Siberia, and shown to have very high cellulolytic activity. Additionally, it is one of a few microorganisms being considered as viable candidates for consolidated bioprocessing applications. Moreover, C. bescii is capable of deconstructing plant biomass without enzymatic or chemical pretreatment. This ability is accomplished by the production and secretion of free, multi-modular and multi-functional enzymes, one of which, CbCel9A/Cel48A also known as CelA, is able to outperform enzymes found in commercial enzyme preparations. Furthermore, the complete C. bescii exoproteome is extremely thermostable and highly active at elevated temperatures, unlike commercial fungal cellulases. Therefore, understanding the functional diversity of enzymes in the C. bescii exoproteome and how inter-molecular synergy between them confers C. bescii with its high cellulolytic activity is an important endeavor to enable the production of more efficient biomass degrading enzyme formulations and in turn, better cellulolytic industrial microorganisms. Results To advance the understanding of the C. bescii exoproteome we have expressed, purified, and tested four of the primary enzymes found in the exoproteome and we have found that the combination of three or four of the most highly expressed enzymes exhibit synergistic activity. We also demonstrated that discrete combinations of these enzymes mimic and even improve upon the activity of the whole C. bescii exoproteome, even though some of the enzymes lack significant activity on their own. Conclusions We have demonstrated that it is possible to replicate the cellulolytic activity of the native C. bescii exoproteome utilizing a minimal gene set, and that these minimal gene sets are more active than the whole ... |
format |
Article in Journal/Newspaper |
author |
Roman Brunecky Daehwan Chung Nicholas S. Sarai Neal Hengge Jordan F. Russell Jenna Young Ashutosh Mittal Patthra Pason Todd Vander Wall William Michener Todd Shollenberger Janet Westpheling Michael E. Himmel Yannick J. Bomble |
author_facet |
Roman Brunecky Daehwan Chung Nicholas S. Sarai Neal Hengge Jordan F. Russell Jenna Young Ashutosh Mittal Patthra Pason Todd Vander Wall William Michener Todd Shollenberger Janet Westpheling Michael E. Himmel Yannick J. Bomble |
author_sort |
Roman Brunecky |
title |
High activity CAZyme cassette for improving biomass degradation in thermophiles |
title_short |
High activity CAZyme cassette for improving biomass degradation in thermophiles |
title_full |
High activity CAZyme cassette for improving biomass degradation in thermophiles |
title_fullStr |
High activity CAZyme cassette for improving biomass degradation in thermophiles |
title_full_unstemmed |
High activity CAZyme cassette for improving biomass degradation in thermophiles |
title_sort |
high activity cazyme cassette for improving biomass degradation in thermophiles |
publisher |
BMC |
publishDate |
2018 |
url |
https://doi.org/10.1186/s13068-018-1014-2 https://doaj.org/article/97f1d72c32114de4891a86d522dddfa2 |
genre |
Kamchatka Siberia |
genre_facet |
Kamchatka Siberia |
op_source |
Biotechnology for Biofuels, Vol 11, Iss 1, Pp 1-12 (2018) |
op_relation |
http://link.springer.com/article/10.1186/s13068-018-1014-2 https://doaj.org/toc/1754-6834 doi:10.1186/s13068-018-1014-2 1754-6834 https://doaj.org/article/97f1d72c32114de4891a86d522dddfa2 |
op_doi |
https://doi.org/10.1186/s13068-018-1014-2 |
container_title |
Biotechnology for Biofuels |
container_volume |
11 |
container_issue |
1 |
_version_ |
1766051726057537536 |