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TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading Fungus Thielavia terrestris Co3Bag1, and Its Application in Enzymatic Hydrolysis of Agroindustrial Derivatives
The biomass-degrading thermophilic ascomycete fungus Co3Bag1 produces TtCel7A, a native bifunctional cellulase/xylanase GH7 family. The purified TtCel7A, with an estimated molecular weight of 71 kDa, was biochemically characterized. TtCel7A displayed an optimal pH of 5.5 for both activities and an o...
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Published in: | Journal of fungi (Basel) 2023-01, Vol.9 (2), p.152 |
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description | The biomass-degrading thermophilic ascomycete fungus
Co3Bag1 produces TtCel7A, a native bifunctional cellulase/xylanase GH7 family. The purified TtCel7A, with an estimated molecular weight of 71 kDa, was biochemically characterized. TtCel7A displayed an optimal pH of 5.5 for both activities and an optimal temperature of 60 and 50 °C for cellulolytic and xylanolytic activities, respectively. The half-lives determined for cellulase activity were 140, 106, and 41 min at 50, 60, and 70 °C, respectively, whereas the half-lives observed for xylanase activity were 24, 10, and 1.4 h at 50, 60, and 70 °C, respectively. The
and V
values were 3.12 mg/mL and 50 U/mg for cellulase activity and 0.17 mg/mL and 42.75 U/mg for xylanase activity. Circular dichroism analysis suggests changes in the secondary structure of TtCel7A in the presence of CMC as the substrate, whereas no modifications were observed with beechwood xylan. TtCel7A displayed the excellent capability to hydrolyze CMC, beechwood xylan, and complex substrates such as oat bran, wheat bran, and sugarcane bagasse, with glucose and cellobiose being the main products released; also, slightly less endo cellulase and xylanase activities were observed. Thus, suggesting TtCel7A has an exo- and endomode of action. Based on the characteristics of the enzyme, it might be considered a good candidate for industrial applications. |
doi_str_mv | 10.3390/jof9020152 |
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Co3Bag1 produces TtCel7A, a native bifunctional cellulase/xylanase GH7 family. The purified TtCel7A, with an estimated molecular weight of 71 kDa, was biochemically characterized. TtCel7A displayed an optimal pH of 5.5 for both activities and an optimal temperature of 60 and 50 °C for cellulolytic and xylanolytic activities, respectively. The half-lives determined for cellulase activity were 140, 106, and 41 min at 50, 60, and 70 °C, respectively, whereas the half-lives observed for xylanase activity were 24, 10, and 1.4 h at 50, 60, and 70 °C, respectively. The
and V
values were 3.12 mg/mL and 50 U/mg for cellulase activity and 0.17 mg/mL and 42.75 U/mg for xylanase activity. Circular dichroism analysis suggests changes in the secondary structure of TtCel7A in the presence of CMC as the substrate, whereas no modifications were observed with beechwood xylan. TtCel7A displayed the excellent capability to hydrolyze CMC, beechwood xylan, and complex substrates such as oat bran, wheat bran, and sugarcane bagasse, with glucose and cellobiose being the main products released; also, slightly less endo cellulase and xylanase activities were observed. Thus, suggesting TtCel7A has an exo- and endomode of action. Based on the characteristics of the enzyme, it might be considered a good candidate for industrial applications.</description><identifier>ISSN: 2309-608X</identifier><identifier>EISSN: 2309-608X</identifier><identifier>DOI: 10.3390/jof9020152</identifier><identifier>PMID: 36836267</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Bagasse ; bifunctional enzyme ; Biomass ; Carbohydrates ; Cellobiose ; Cellulase ; cellulase/xylanase ; Cellulose ; Circular dichroism ; Enzymes ; exoglucanase ; Fungi ; Glucose ; Glycerol ; Industrial applications ; Lignocellulose ; Microorganisms ; Molecular weight ; Protein structure ; Proteins ; purification ; Secondary structure ; Sugarcane ; thermostability ; Thielavia terrestris ; Xylan</subject><ispartof>Journal of fungi (Basel), 2023-01, Vol.9 (2), p.152</ispartof><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-2f2e577939e9f32f17ba8d5d7e1d08e214865ddb42719618f9148c4a79d785b23</citedby><cites>FETCH-LOGICAL-c472t-2f2e577939e9f32f17ba8d5d7e1d08e214865ddb42719618f9148c4a79d785b23</cites><orcidid>0000-0002-8263-2671</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2779515965/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2779515965?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36836267$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>López-López, Azucena</creatorcontrib><creatorcontrib>Santiago-Hernández, Alejandro</creatorcontrib><creatorcontrib>Cayetano-Cruz, Maribel</creatorcontrib><creatorcontrib>García-Huante, Yolanda</creatorcontrib><creatorcontrib>Campos, Jorge E</creatorcontrib><creatorcontrib>Bustos-Jaimes, Ismael</creatorcontrib><creatorcontrib>Marsch-Moreno, Rodolfo</creatorcontrib><creatorcontrib>Cano-Ramírez, Claudia</creatorcontrib><creatorcontrib>Benitez-Cardoza, Claudia G</creatorcontrib><creatorcontrib>Hidalgo-Lara, María Eugenia</creatorcontrib><title>TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading Fungus Thielavia terrestris Co3Bag1, and Its Application in Enzymatic Hydrolysis of Agroindustrial Derivatives</title><title>Journal of fungi (Basel)</title><addtitle>J Fungi (Basel)</addtitle><description>The biomass-degrading thermophilic ascomycete fungus
Co3Bag1 produces TtCel7A, a native bifunctional cellulase/xylanase GH7 family. The purified TtCel7A, with an estimated molecular weight of 71 kDa, was biochemically characterized. TtCel7A displayed an optimal pH of 5.5 for both activities and an optimal temperature of 60 and 50 °C for cellulolytic and xylanolytic activities, respectively. The half-lives determined for cellulase activity were 140, 106, and 41 min at 50, 60, and 70 °C, respectively, whereas the half-lives observed for xylanase activity were 24, 10, and 1.4 h at 50, 60, and 70 °C, respectively. The
and V
values were 3.12 mg/mL and 50 U/mg for cellulase activity and 0.17 mg/mL and 42.75 U/mg for xylanase activity. Circular dichroism analysis suggests changes in the secondary structure of TtCel7A in the presence of CMC as the substrate, whereas no modifications were observed with beechwood xylan. TtCel7A displayed the excellent capability to hydrolyze CMC, beechwood xylan, and complex substrates such as oat bran, wheat bran, and sugarcane bagasse, with glucose and cellobiose being the main products released; also, slightly less endo cellulase and xylanase activities were observed. Thus, suggesting TtCel7A has an exo- and endomode of action. Based on the characteristics of the enzyme, it might be considered a good candidate for industrial applications.</description><subject>Bagasse</subject><subject>bifunctional enzyme</subject><subject>Biomass</subject><subject>Carbohydrates</subject><subject>Cellobiose</subject><subject>Cellulase</subject><subject>cellulase/xylanase</subject><subject>Cellulose</subject><subject>Circular dichroism</subject><subject>Enzymes</subject><subject>exoglucanase</subject><subject>Fungi</subject><subject>Glucose</subject><subject>Glycerol</subject><subject>Industrial applications</subject><subject>Lignocellulose</subject><subject>Microorganisms</subject><subject>Molecular weight</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>purification</subject><subject>Secondary structure</subject><subject>Sugarcane</subject><subject>thermostability</subject><subject>Thielavia terrestris</subject><subject>Xylan</subject><issn>2309-608X</issn><issn>2309-608X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNplkstuEzEYRkcIRKvSDQ-ALLFBiFBfxmObBVKapjRSBZsgdTdybM_EkcdO7ZmI9HX7IjhNKC2sfDs-_mz_RfEWwc-ECHi2Co2AGCKKXxTHmEAxqiC_efmkf1ScprSCMDO8EoK8Lo5IxUmFK3Zc3M_7iXFs_AWMwXfZ240B86WJXVgvrbMKnNtm8Kq3wUsHMukGF5I5u9k66WUyYPortG5Qh1ETQwf65X-O0MmURhemjVJb34LLwbdDypQ1Tm6sBL2J0aQ-2gQmgZzLFn0C0msw6xMYr9fZIncZgPVg6u-2XR4pcLXVMbhtyptCA8ZtDNbrYWfJWS9MtJuHC6U3xatGumROD-1J8fNyOp9cja5_fJtNxtcjVTLcj3CDDWVMEGFEQ3CD2EJyTTUzSENuMCp5RbVelJghUSHeiDyjSsmEZpwuMDkpZnuvDnJVr6PtZNzWQdr6YSLEtpYxB3emNghiwriGDItSSc0hq6CiUJCqwlQtsuvr3rUeFp3Ryvg-SvdM-nzF22Xdhk0tcjTKyiz4cBDEcDvkt607m1T-QOlNGFKNGYf5UEFJRt__g67CEPOH7ygmKKKiopn6uKdUDClF0zyGQbDelWL9txQz_O5p_Ef0T-GR3zsG3eA</recordid><startdate>20230123</startdate><enddate>20230123</enddate><creator>López-López, Azucena</creator><creator>Santiago-Hernández, Alejandro</creator><creator>Cayetano-Cruz, Maribel</creator><creator>García-Huante, Yolanda</creator><creator>Campos, Jorge E</creator><creator>Bustos-Jaimes, Ismael</creator><creator>Marsch-Moreno, Rodolfo</creator><creator>Cano-Ramírez, Claudia</creator><creator>Benitez-Cardoza, Claudia G</creator><creator>Hidalgo-Lara, María Eugenia</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-8263-2671</orcidid></search><sort><creationdate>20230123</creationdate><title>TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading Fungus Thielavia terrestris Co3Bag1, and Its Application in Enzymatic Hydrolysis of Agroindustrial Derivatives</title><author>López-López, Azucena ; Santiago-Hernández, Alejandro ; Cayetano-Cruz, Maribel ; García-Huante, Yolanda ; Campos, Jorge E ; Bustos-Jaimes, Ismael ; Marsch-Moreno, Rodolfo ; Cano-Ramírez, Claudia ; Benitez-Cardoza, Claudia G ; Hidalgo-Lara, María Eugenia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472t-2f2e577939e9f32f17ba8d5d7e1d08e214865ddb42719618f9148c4a79d785b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Bagasse</topic><topic>bifunctional enzyme</topic><topic>Biomass</topic><topic>Carbohydrates</topic><topic>Cellobiose</topic><topic>Cellulase</topic><topic>cellulase/xylanase</topic><topic>Cellulose</topic><topic>Circular dichroism</topic><topic>Enzymes</topic><topic>exoglucanase</topic><topic>Fungi</topic><topic>Glucose</topic><topic>Glycerol</topic><topic>Industrial applications</topic><topic>Lignocellulose</topic><topic>Microorganisms</topic><topic>Molecular weight</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>purification</topic><topic>Secondary structure</topic><topic>Sugarcane</topic><topic>thermostability</topic><topic>Thielavia terrestris</topic><topic>Xylan</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>López-López, Azucena</creatorcontrib><creatorcontrib>Santiago-Hernández, Alejandro</creatorcontrib><creatorcontrib>Cayetano-Cruz, Maribel</creatorcontrib><creatorcontrib>García-Huante, Yolanda</creatorcontrib><creatorcontrib>Campos, Jorge E</creatorcontrib><creatorcontrib>Bustos-Jaimes, Ismael</creatorcontrib><creatorcontrib>Marsch-Moreno, Rodolfo</creatorcontrib><creatorcontrib>Cano-Ramírez, Claudia</creatorcontrib><creatorcontrib>Benitez-Cardoza, Claudia G</creatorcontrib><creatorcontrib>Hidalgo-Lara, María Eugenia</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>ProQuest Biological Science Journals</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Journal of fungi (Basel)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>López-López, Azucena</au><au>Santiago-Hernández, Alejandro</au><au>Cayetano-Cruz, Maribel</au><au>García-Huante, Yolanda</au><au>Campos, Jorge E</au><au>Bustos-Jaimes, Ismael</au><au>Marsch-Moreno, Rodolfo</au><au>Cano-Ramírez, Claudia</au><au>Benitez-Cardoza, Claudia G</au><au>Hidalgo-Lara, María Eugenia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading Fungus Thielavia terrestris Co3Bag1, and Its Application in Enzymatic Hydrolysis of Agroindustrial Derivatives</atitle><jtitle>Journal of fungi (Basel)</jtitle><addtitle>J Fungi (Basel)</addtitle><date>2023-01-23</date><risdate>2023</risdate><volume>9</volume><issue>2</issue><spage>152</spage><pages>152-</pages><issn>2309-608X</issn><eissn>2309-608X</eissn><abstract>The biomass-degrading thermophilic ascomycete fungus
Co3Bag1 produces TtCel7A, a native bifunctional cellulase/xylanase GH7 family. The purified TtCel7A, with an estimated molecular weight of 71 kDa, was biochemically characterized. TtCel7A displayed an optimal pH of 5.5 for both activities and an optimal temperature of 60 and 50 °C for cellulolytic and xylanolytic activities, respectively. The half-lives determined for cellulase activity were 140, 106, and 41 min at 50, 60, and 70 °C, respectively, whereas the half-lives observed for xylanase activity were 24, 10, and 1.4 h at 50, 60, and 70 °C, respectively. The
and V
values were 3.12 mg/mL and 50 U/mg for cellulase activity and 0.17 mg/mL and 42.75 U/mg for xylanase activity. Circular dichroism analysis suggests changes in the secondary structure of TtCel7A in the presence of CMC as the substrate, whereas no modifications were observed with beechwood xylan. TtCel7A displayed the excellent capability to hydrolyze CMC, beechwood xylan, and complex substrates such as oat bran, wheat bran, and sugarcane bagasse, with glucose and cellobiose being the main products released; also, slightly less endo cellulase and xylanase activities were observed. Thus, suggesting TtCel7A has an exo- and endomode of action. Based on the characteristics of the enzyme, it might be considered a good candidate for industrial applications.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36836267</pmid><doi>10.3390/jof9020152</doi><orcidid>https://orcid.org/0000-0002-8263-2671</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Bagasse bifunctional enzyme Biomass Carbohydrates Cellobiose Cellulase cellulase/xylanase Cellulose Circular dichroism Enzymes exoglucanase Fungi Glucose Glycerol Industrial applications Lignocellulose Microorganisms Molecular weight Protein structure Proteins purification Secondary structure Sugarcane thermostability Thielavia terrestris Xylan |
title | TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading Fungus Thielavia terrestris Co3Bag1, and Its Application in Enzymatic Hydrolysis of Agroindustrial Derivatives |
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