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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ftdatacite:10.6084/m9.figshare.c.3994020 2023-05-15T16:59:28+02:00 High activity CAZyme cassette for improving biomass degradation in thermophiles Brunecky, Roman Daehwan Chung Sarai, Nicholas Hengge, Neal Russell, Jordan Young, Jenna Mittal, Ashutosh Patthra Pason Wall, Todd Vander Michener, William Shollenberger, Todd Westpheling, Janet Himmel, Michael Bomble, Yannick 2018 https://dx.doi.org/10.6084/m9.figshare.c.3994020 https://figshare.com/collections/High_activity_CAZyme_cassette_for_improving_biomass_degradation_in_thermophiles/3994020 unknown Figshare https://dx.doi.org/10.1186/s13068-018-1014-2 CC BY 4.0 https://creativecommons.org/licenses/by/4.0 CC-BY Biochemistry Microbiology FOS Biological sciences Genetics Pharmacology Biotechnology 59999 Environmental Sciences not elsewhere classified FOS Earth and related environmental sciences 39999 Chemical Sciences not elsewhere classified FOS Chemical sciences Science Policy 69999 Biological Sciences not elsewhere classified Cancer Collection article 2018 ftdatacite https://doi.org/10.6084/m9.figshare.c.3994020 https://doi.org/10.1186/s13068-018-1014-2 2021-11-05T12:55:41Z 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 exoproteome. In the future, this may lead to more simplified and efficient cellulolytic enzyme preparations or yield improvements when these enzymes are expressed in microorganisms engineered for consolidated bioprocessing. Article in Journal/Newspaper Kamchatka Siberia DataCite Metadata Store (German National Library of Science and Technology) |
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Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
unknown |
topic |
Biochemistry Microbiology FOS Biological sciences Genetics Pharmacology Biotechnology 59999 Environmental Sciences not elsewhere classified FOS Earth and related environmental sciences 39999 Chemical Sciences not elsewhere classified FOS Chemical sciences Science Policy 69999 Biological Sciences not elsewhere classified Cancer |
spellingShingle |
Biochemistry Microbiology FOS Biological sciences Genetics Pharmacology Biotechnology 59999 Environmental Sciences not elsewhere classified FOS Earth and related environmental sciences 39999 Chemical Sciences not elsewhere classified FOS Chemical sciences Science Policy 69999 Biological Sciences not elsewhere classified Cancer Brunecky, Roman Daehwan Chung Sarai, Nicholas Hengge, Neal Russell, Jordan Young, Jenna Mittal, Ashutosh Patthra Pason Wall, Todd Vander Michener, William Shollenberger, Todd Westpheling, Janet Himmel, Michael Bomble, Yannick High activity CAZyme cassette for improving biomass degradation in thermophiles |
topic_facet |
Biochemistry Microbiology FOS Biological sciences Genetics Pharmacology Biotechnology 59999 Environmental Sciences not elsewhere classified FOS Earth and related environmental sciences 39999 Chemical Sciences not elsewhere classified FOS Chemical sciences Science Policy 69999 Biological Sciences not elsewhere classified Cancer |
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 exoproteome. In the future, this may lead to more simplified and efficient cellulolytic enzyme preparations or yield improvements when these enzymes are expressed in microorganisms engineered for consolidated bioprocessing. |
format |
Article in Journal/Newspaper |
author |
Brunecky, Roman Daehwan Chung Sarai, Nicholas Hengge, Neal Russell, Jordan Young, Jenna Mittal, Ashutosh Patthra Pason Wall, Todd Vander Michener, William Shollenberger, Todd Westpheling, Janet Himmel, Michael Bomble, Yannick |
author_facet |
Brunecky, Roman Daehwan Chung Sarai, Nicholas Hengge, Neal Russell, Jordan Young, Jenna Mittal, Ashutosh Patthra Pason Wall, Todd Vander Michener, William Shollenberger, Todd Westpheling, Janet Himmel, Michael Bomble, Yannick |
author_sort |
Brunecky, Roman |
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 |
Figshare |
publishDate |
2018 |
url |
https://dx.doi.org/10.6084/m9.figshare.c.3994020 https://figshare.com/collections/High_activity_CAZyme_cassette_for_improving_biomass_degradation_in_thermophiles/3994020 |
genre |
Kamchatka Siberia |
genre_facet |
Kamchatka Siberia |
op_relation |
https://dx.doi.org/10.1186/s13068-018-1014-2 |
op_rights |
CC BY 4.0 https://creativecommons.org/licenses/by/4.0 |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.6084/m9.figshare.c.3994020 https://doi.org/10.1186/s13068-018-1014-2 |
_version_ |
1766051747972775936 |