Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris
In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from Aspergillus cervinus, and the endoglucanase Egh12 from Thielavia terrestris combining activity on linear β-glucan and branched xyloglucan. Egh12 fr...
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creator | Rykov, Sergey V. Selimzyanova, Alina I. Nikolaeva, Alena Y. Lazarenko, Vladimir A. Tsurin, Nikita V. Akentyev, Philipp I. Zverlov, Vladimir V. Liebl, Wolfgang Schwarz, Wolfgang H. Berezina, Oksana V. |
description | In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from
Aspergillus cervinus,
and the endoglucanase Egh12 from
Thielavia terrestris
combining activity on linear β-glucan and branched xyloglucan. Egh12 from
T. terrestris
was produced in
Pichia pastoris
, purified, and characterized as a thermostable enzyme with maximal activity at 70 ºC and a half-life time of 138 min at 65 °C. We for the first time demonstrated that the GH12 endoglucanases Egh12 and Bgh12A, but not the strict xyloglucanase Xgh12B, hydrolyzed (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides and had transglycosylase activity on (1,3)-β-D-glucooligosaccharides. Phylogenetic analysis indicated that Egh12 from
T. terrestris
and Bgh12A from
A. cervinus
are more related than Bgh12A and Xgh12B isolated from one strain. The X-ray structure of Bgh12A was determined with 2.17 Å resolution and compared with 3D-homology models of Egh12 and Xgh12B. The enzymes have a β-jelly roll structure with a catalytic cleft running across the protein. Comparative analysis and a docking study demonstrated the importance of endoglucanase-specific loop 1 partly covering the catalytic cleft for correct placement of the linear substrates. Variability in substrate specificity between the GH12 endoglucanases is determined by non-conservative residues in structural loops framing the catalytic cleft. A residue responsible for the thermostability of Egh12 was predicted. The key structural elements and residues described in this study may serve as potential targets for modification aimed at the improvement of enzymatic properties.
Key points
• Thermostable endoglucanase Egh12 from T. terrestris was produced in P. pastoris, purified, and characterized
• The X-ray structure of GH12 endoglucanase Bgh12A from A. cervinus was resolved
• GH12 endoglucanases, but not GH12 xyloglucanases, hydrolyze (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides |
doi_str_mv | 10.1007/s00253-022-11811-7 |
format | Article |
fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_2626229331</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A695121922</galeid><sourcerecordid>A695121922</sourcerecordid><originalsourceid>FETCH-LOGICAL-c508t-a1917761115f1ba234a846bb74dbc7d2238922f13e1652c75c84e6cf844e91043</originalsourceid><addsrcrecordid>eNp9kk1u1TAQxyMEoo_CBVggS2xYkOKxEydh91qVFqkSm1ZiZzmOnbpykocdV3o77sAxuBUnYdIUKhDCs_DXbz48_mfZS6BHQGn1LlLKSp5TxnKAGiCvHmUbKDjLqYDicbahUJV5VTb1QfYsxhtKgdVCPM0OeAmsEWWxyb5fjSkm5UlMbZyDmg2JO6OdddrNe-JGcnZOrBqc3xNg7wkySc8pmB9fv9k06tlNI1Gj8vvoIpks6X3SuI8mkuP-GtgWbzvyeVkeExumgWwxQeid9ykSbcKtwwre3lGnC7VCl9fOeHXrFJlNCAbTuvg8e2KVj-bF_XyYXX04vTw5zy8-nX082V7kuqT1nCtooKoEAJQWWsV4oepCtG1VdK2uOsZ43TBmgRsQJdNVqevCCG3rojAN0IIfZm_WuLswfUmYWw4uauO9Gs2UomQCjTWcA6Kv_0JvphSwHQvFcTT4Mw9Ur7yRbrQTdlovQeVWNPgXgAUhdfQPCq0zg9PTaKzD8z8c2OqgwxRjMFbughtU2EugclGIXBUiUSHyTiGyQqdX9xWndjDdb5dfkkCAr0DEq7E34eFJ_wn7E8LSxbQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2633339118</pqid></control><display><type>article</type><title>Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Rykov, Sergey V. ; Selimzyanova, Alina I. ; Nikolaeva, Alena Y. ; Lazarenko, Vladimir A. ; Tsurin, Nikita V. ; Akentyev, Philipp I. ; Zverlov, Vladimir V. ; Liebl, Wolfgang ; Schwarz, Wolfgang H. ; Berezina, Oksana V.</creator><creatorcontrib>Rykov, Sergey V. ; Selimzyanova, Alina I. ; Nikolaeva, Alena Y. ; Lazarenko, Vladimir A. ; Tsurin, Nikita V. ; Akentyev, Philipp I. ; Zverlov, Vladimir V. ; Liebl, Wolfgang ; Schwarz, Wolfgang H. ; Berezina, Oksana V.</creatorcontrib><description>In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from
Aspergillus cervinus,
and the endoglucanase Egh12 from
Thielavia terrestris
combining activity on linear β-glucan and branched xyloglucan. Egh12 from
T. terrestris
was produced in
Pichia pastoris
, purified, and characterized as a thermostable enzyme with maximal activity at 70 ºC and a half-life time of 138 min at 65 °C. We for the first time demonstrated that the GH12 endoglucanases Egh12 and Bgh12A, but not the strict xyloglucanase Xgh12B, hydrolyzed (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides and had transglycosylase activity on (1,3)-β-D-glucooligosaccharides. Phylogenetic analysis indicated that Egh12 from
T. terrestris
and Bgh12A from
A. cervinus
are more related than Bgh12A and Xgh12B isolated from one strain. The X-ray structure of Bgh12A was determined with 2.17 Å resolution and compared with 3D-homology models of Egh12 and Xgh12B. The enzymes have a β-jelly roll structure with a catalytic cleft running across the protein. Comparative analysis and a docking study demonstrated the importance of endoglucanase-specific loop 1 partly covering the catalytic cleft for correct placement of the linear substrates. Variability in substrate specificity between the GH12 endoglucanases is determined by non-conservative residues in structural loops framing the catalytic cleft. A residue responsible for the thermostability of Egh12 was predicted. The key structural elements and residues described in this study may serve as potential targets for modification aimed at the improvement of enzymatic properties.
Key points
• Thermostable endoglucanase Egh12 from T. terrestris was produced in P. pastoris, purified, and characterized
• The X-ray structure of GH12 endoglucanase Bgh12A from A. cervinus was resolved
• GH12 endoglucanases, but not GH12 xyloglucanases, hydrolyze (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-022-11811-7</identifier><identifier>PMID: 35129654</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Ascomycota ; Aspergillus ; Aspergillus cervinus ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Cellulase - metabolism ; Comparative analysis ; Endoglucanase ; Enzymes ; Function analysis ; Fungi ; Glucan ; Homology ; Life Sciences ; Linkages ; Microbial enzymes ; Microbial Genetics and Genomics ; Microbiology ; Phylogeny ; Physiological aspects ; Pichia pastoris ; Residues ; Sordariales - metabolism ; Structural members ; Structure ; Structure-function relationships ; Substrate Specificity ; Substrates ; Substrates (Biochemistry) ; Thermal stability ; Thielavia terrestri ; Three dimensional models ; Xyloglucan ; Xyloglucanase ; β-Glucan</subject><ispartof>Applied microbiology and biotechnology, 2022-02, Vol.106 (4), p.1493-1509</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2022</rights><rights>2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><rights>COPYRIGHT 2022 Springer</rights><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2022.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-a1917761115f1ba234a846bb74dbc7d2238922f13e1652c75c84e6cf844e91043</citedby><cites>FETCH-LOGICAL-c508t-a1917761115f1ba234a846bb74dbc7d2238922f13e1652c75c84e6cf844e91043</cites><orcidid>0000-0003-4868-0589</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-022-11811-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-022-11811-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35129654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rykov, Sergey V.</creatorcontrib><creatorcontrib>Selimzyanova, Alina I.</creatorcontrib><creatorcontrib>Nikolaeva, Alena Y.</creatorcontrib><creatorcontrib>Lazarenko, Vladimir A.</creatorcontrib><creatorcontrib>Tsurin, Nikita V.</creatorcontrib><creatorcontrib>Akentyev, Philipp I.</creatorcontrib><creatorcontrib>Zverlov, Vladimir V.</creatorcontrib><creatorcontrib>Liebl, Wolfgang</creatorcontrib><creatorcontrib>Schwarz, Wolfgang H.</creatorcontrib><creatorcontrib>Berezina, Oksana V.</creatorcontrib><title>Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from
Aspergillus cervinus,
and the endoglucanase Egh12 from
Thielavia terrestris
combining activity on linear β-glucan and branched xyloglucan. Egh12 from
T. terrestris
was produced in
Pichia pastoris
, purified, and characterized as a thermostable enzyme with maximal activity at 70 ºC and a half-life time of 138 min at 65 °C. We for the first time demonstrated that the GH12 endoglucanases Egh12 and Bgh12A, but not the strict xyloglucanase Xgh12B, hydrolyzed (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides and had transglycosylase activity on (1,3)-β-D-glucooligosaccharides. Phylogenetic analysis indicated that Egh12 from
T. terrestris
and Bgh12A from
A. cervinus
are more related than Bgh12A and Xgh12B isolated from one strain. The X-ray structure of Bgh12A was determined with 2.17 Å resolution and compared with 3D-homology models of Egh12 and Xgh12B. The enzymes have a β-jelly roll structure with a catalytic cleft running across the protein. Comparative analysis and a docking study demonstrated the importance of endoglucanase-specific loop 1 partly covering the catalytic cleft for correct placement of the linear substrates. Variability in substrate specificity between the GH12 endoglucanases is determined by non-conservative residues in structural loops framing the catalytic cleft. A residue responsible for the thermostability of Egh12 was predicted. The key structural elements and residues described in this study may serve as potential targets for modification aimed at the improvement of enzymatic properties.
Key points
• Thermostable endoglucanase Egh12 from T. terrestris was produced in P. pastoris, purified, and characterized
• The X-ray structure of GH12 endoglucanase Bgh12A from A. cervinus was resolved
• GH12 endoglucanases, but not GH12 xyloglucanases, hydrolyze (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides</description><subject>Ascomycota</subject><subject>Aspergillus</subject><subject>Aspergillus cervinus</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Cellulase - metabolism</subject><subject>Comparative analysis</subject><subject>Endoglucanase</subject><subject>Enzymes</subject><subject>Function analysis</subject><subject>Fungi</subject><subject>Glucan</subject><subject>Homology</subject><subject>Life Sciences</subject><subject>Linkages</subject><subject>Microbial enzymes</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Phylogeny</subject><subject>Physiological aspects</subject><subject>Pichia pastoris</subject><subject>Residues</subject><subject>Sordariales - metabolism</subject><subject>Structural members</subject><subject>Structure</subject><subject>Structure-function relationships</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Substrates (Biochemistry)</subject><subject>Thermal stability</subject><subject>Thielavia terrestri</subject><subject>Three dimensional models</subject><subject>Xyloglucan</subject><subject>Xyloglucanase</subject><subject>β-Glucan</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kk1u1TAQxyMEoo_CBVggS2xYkOKxEydh91qVFqkSm1ZiZzmOnbpykocdV3o77sAxuBUnYdIUKhDCs_DXbz48_mfZS6BHQGn1LlLKSp5TxnKAGiCvHmUbKDjLqYDicbahUJV5VTb1QfYsxhtKgdVCPM0OeAmsEWWxyb5fjSkm5UlMbZyDmg2JO6OdddrNe-JGcnZOrBqc3xNg7wkySc8pmB9fv9k06tlNI1Gj8vvoIpks6X3SuI8mkuP-GtgWbzvyeVkeExumgWwxQeid9ykSbcKtwwre3lGnC7VCl9fOeHXrFJlNCAbTuvg8e2KVj-bF_XyYXX04vTw5zy8-nX082V7kuqT1nCtooKoEAJQWWsV4oepCtG1VdK2uOsZ43TBmgRsQJdNVqevCCG3rojAN0IIfZm_WuLswfUmYWw4uauO9Gs2UomQCjTWcA6Kv_0JvphSwHQvFcTT4Mw9Ur7yRbrQTdlovQeVWNPgXgAUhdfQPCq0zg9PTaKzD8z8c2OqgwxRjMFbughtU2EugclGIXBUiUSHyTiGyQqdX9xWndjDdb5dfkkCAr0DEq7E34eFJ_wn7E8LSxbQ</recordid><startdate>20220201</startdate><enddate>20220201</enddate><creator>Rykov, Sergey V.</creator><creator>Selimzyanova, Alina I.</creator><creator>Nikolaeva, Alena Y.</creator><creator>Lazarenko, Vladimir A.</creator><creator>Tsurin, Nikita V.</creator><creator>Akentyev, Philipp I.</creator><creator>Zverlov, Vladimir V.</creator><creator>Liebl, Wolfgang</creator><creator>Schwarz, Wolfgang H.</creator><creator>Berezina, Oksana V.</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature 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substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris</title><author>Rykov, Sergey V. ; Selimzyanova, Alina I. ; Nikolaeva, Alena Y. ; Lazarenko, Vladimir A. ; Tsurin, Nikita V. ; Akentyev, Philipp I. ; Zverlov, Vladimir V. ; Liebl, Wolfgang ; Schwarz, Wolfgang H. ; Berezina, Oksana V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-a1917761115f1ba234a846bb74dbc7d2238922f13e1652c75c84e6cf844e91043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Ascomycota</topic><topic>Aspergillus</topic><topic>Aspergillus cervinus</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Cellulase - metabolism</topic><topic>Comparative analysis</topic><topic>Endoglucanase</topic><topic>Enzymes</topic><topic>Function analysis</topic><topic>Fungi</topic><topic>Glucan</topic><topic>Homology</topic><topic>Life Sciences</topic><topic>Linkages</topic><topic>Microbial enzymes</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Phylogeny</topic><topic>Physiological aspects</topic><topic>Pichia pastoris</topic><topic>Residues</topic><topic>Sordariales - metabolism</topic><topic>Structural members</topic><topic>Structure</topic><topic>Structure-function relationships</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Substrates (Biochemistry)</topic><topic>Thermal stability</topic><topic>Thielavia terrestri</topic><topic>Three dimensional models</topic><topic>Xyloglucan</topic><topic>Xyloglucanase</topic><topic>β-Glucan</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rykov, Sergey V.</creatorcontrib><creatorcontrib>Selimzyanova, Alina I.</creatorcontrib><creatorcontrib>Nikolaeva, Alena Y.</creatorcontrib><creatorcontrib>Lazarenko, Vladimir A.</creatorcontrib><creatorcontrib>Tsurin, Nikita V.</creatorcontrib><creatorcontrib>Akentyev, Philipp I.</creatorcontrib><creatorcontrib>Zverlov, Vladimir V.</creatorcontrib><creatorcontrib>Liebl, Wolfgang</creatorcontrib><creatorcontrib>Schwarz, Wolfgang H.</creatorcontrib><creatorcontrib>Berezina, Oksana V.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global 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biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rykov, Sergey V.</au><au>Selimzyanova, Alina I.</au><au>Nikolaeva, Alena Y.</au><au>Lazarenko, Vladimir A.</au><au>Tsurin, Nikita V.</au><au>Akentyev, Philipp I.</au><au>Zverlov, Vladimir V.</au><au>Liebl, Wolfgang</au><au>Schwarz, Wolfgang H.</au><au>Berezina, Oksana V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2022-02-01</date><risdate>2022</risdate><volume>106</volume><issue>4</issue><spage>1493</spage><epage>1509</epage><pages>1493-1509</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from
Aspergillus cervinus,
and the endoglucanase Egh12 from
Thielavia terrestris
combining activity on linear β-glucan and branched xyloglucan. Egh12 from
T. terrestris
was produced in
Pichia pastoris
, purified, and characterized as a thermostable enzyme with maximal activity at 70 ºC and a half-life time of 138 min at 65 °C. We for the first time demonstrated that the GH12 endoglucanases Egh12 and Bgh12A, but not the strict xyloglucanase Xgh12B, hydrolyzed (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides and had transglycosylase activity on (1,3)-β-D-glucooligosaccharides. Phylogenetic analysis indicated that Egh12 from
T. terrestris
and Bgh12A from
A. cervinus
are more related than Bgh12A and Xgh12B isolated from one strain. The X-ray structure of Bgh12A was determined with 2.17 Å resolution and compared with 3D-homology models of Egh12 and Xgh12B. The enzymes have a β-jelly roll structure with a catalytic cleft running across the protein. Comparative analysis and a docking study demonstrated the importance of endoglucanase-specific loop 1 partly covering the catalytic cleft for correct placement of the linear substrates. Variability in substrate specificity between the GH12 endoglucanases is determined by non-conservative residues in structural loops framing the catalytic cleft. A residue responsible for the thermostability of Egh12 was predicted. The key structural elements and residues described in this study may serve as potential targets for modification aimed at the improvement of enzymatic properties.
Key points
• Thermostable endoglucanase Egh12 from T. terrestris was produced in P. pastoris, purified, and characterized
• The X-ray structure of GH12 endoglucanase Bgh12A from A. cervinus was resolved
• GH12 endoglucanases, but not GH12 xyloglucanases, hydrolyze (1,3)-β-linkages in (1,3;1,4)-β-D-glucooligosaccharides</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>35129654</pmid><doi>10.1007/s00253-022-11811-7</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0003-4868-0589</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0175-7598 |
ispartof | Applied microbiology and biotechnology, 2022-02, Vol.106 (4), p.1493-1509 |
issn | 0175-7598 1432-0614 |
language | eng |
recordid | cdi_proquest_miscellaneous_2626229331 |
source | MEDLINE; SpringerLink Journals |
subjects | Ascomycota Aspergillus Aspergillus cervinus Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Cellulase - metabolism Comparative analysis Endoglucanase Enzymes Function analysis Fungi Glucan Homology Life Sciences Linkages Microbial enzymes Microbial Genetics and Genomics Microbiology Phylogeny Physiological aspects Pichia pastoris Residues Sordariales - metabolism Structural members Structure Structure-function relationships Substrate Specificity Substrates Substrates (Biochemistry) Thermal stability Thielavia terrestri Three dimensional models Xyloglucan Xyloglucanase β-Glucan |
title | Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-24T02%3A54%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Unusual%20substrate%20specificity%20in%20GH%20family%2012:%20structure%E2%80%93function%20analysis%20of%20glucanases%20Bgh12A%20and%20Xgh12B%20from%20Aspergillus%20cervinus,%20and%20Egh12%20from%20Thielavia%20terrestris&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Rykov,%20Sergey%20V.&rft.date=2022-02-01&rft.volume=106&rft.issue=4&rft.spage=1493&rft.epage=1509&rft.pages=1493-1509&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-022-11811-7&rft_dat=%3Cgale_proqu%3EA695121922%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2633339118&rft_id=info:pmid/35129654&rft_galeid=A695121922&rfr_iscdi=true |