Characterization of a uronate dehydrogenase from Thermobispora bispora for production of glucaric acid from hemicellulose substrate
A thermostable uronate dehydrogenase Tb-UDH from Thermobispora bispora was over-expressed in Escherichia coli using the T7 polymerase expression system. The Tb-UDH was purified by metal affinity chromatography, and gave a single band on SDS-PAGE. The maximum activity on glucuronic acid was found at...
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| Veröffentlicht in: | World journal of microbiology & biotechnology 2018-07, Vol.34 (7), p.102-13, Article 102 |
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| creator | Li, Yaxian Xue, Yemin Cao, Zhigang Zhou, Tao Alnadari, Fawze |
| description | A thermostable uronate dehydrogenase Tb-UDH from
Thermobispora bispora
was over-expressed in
Escherichia coli
using the T7 polymerase expression system. The Tb-UDH was purified by metal affinity chromatography, and gave a single band on SDS-PAGE. The maximum activity on glucuronic acid was found at 60 °C and pH 7.0. The purified enzyme retained over 58% of its activity after holding a pH ranging from 7.0 to 7.5 for 1 h at 60 °C. The
K
m
and
V
max
values of the purified Tb-UDH for Glucuronic acid (GluUA) were 0.165 mM and 117.7 U mg
−1
, respectively, those for galacturonic acid (GalUA) were 0.115 mM and 104.2 U mg
−1
, respectively, and those for NAD
+
were 0.120 mM and 133.3 U mg
−1
, respectively; the turnover number (
k
cat
) with GluUA as a substrate was higher than that with GalUA; however, the Michaelis constant (
K
m
) for GalUA was lower than that for GluUA. After 60 min of incubation at 50 °C, Tb-UDH exhibited a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from breech xylans formed by xylanase and α-glucuronidase. This work shows that biocatalytic routes have great potential for the conversion of hemicellulose substrate into value-added products derived from renewable biomass.
TOC Graphic
(A) The structure of the xylan is described and the site of action of the xylan degrading enzyme is indicated. (B) The effect of substrate concentration on recombinant Tb-UDH activity when galacturonic acid was used as substrate. (C) SDS-PAGE analysis of E. coli BL21 (DE3) harboring pET-20b(+) and pET-20b-Tb-UDH. (D) Oxidative conversion of glucuronic acid from a beechwood xylan to glucaric acid |
| doi_str_mv | 10.1007/s11274-018-2486-8 |
| format | Article |
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Thermobispora bispora
was over-expressed in
Escherichia coli
using the T7 polymerase expression system. The Tb-UDH was purified by metal affinity chromatography, and gave a single band on SDS-PAGE. The maximum activity on glucuronic acid was found at 60 °C and pH 7.0. The purified enzyme retained over 58% of its activity after holding a pH ranging from 7.0 to 7.5 for 1 h at 60 °C. The
K
m
and
V
max
values of the purified Tb-UDH for Glucuronic acid (GluUA) were 0.165 mM and 117.7 U mg
−1
, respectively, those for galacturonic acid (GalUA) were 0.115 mM and 104.2 U mg
−1
, respectively, and those for NAD
+
were 0.120 mM and 133.3 U mg
−1
, respectively; the turnover number (
k
cat
) with GluUA as a substrate was higher than that with GalUA; however, the Michaelis constant (
K
m
) for GalUA was lower than that for GluUA. After 60 min of incubation at 50 °C, Tb-UDH exhibited a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from breech xylans formed by xylanase and α-glucuronidase. This work shows that biocatalytic routes have great potential for the conversion of hemicellulose substrate into value-added products derived from renewable biomass.
TOC Graphic
(A) The structure of the xylan is described and the site of action of the xylan degrading enzyme is indicated. (B) The effect of substrate concentration on recombinant Tb-UDH activity when galacturonic acid was used as substrate. (C) SDS-PAGE analysis of E. coli BL21 (DE3) harboring pET-20b(+) and pET-20b-Tb-UDH. (D) Oxidative conversion of glucuronic acid from a beechwood xylan to glucaric acid</description><identifier>ISSN: 0959-3993</identifier><identifier>EISSN: 1573-0972</identifier><identifier>DOI: 10.1007/s11274-018-2486-8</identifier><identifier>PMID: 29936649</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Acids ; Affinity chromatography ; Applied Microbiology ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Conversion ; Conversion ratio ; Dehydrogenase ; Dehydrogenases ; E coli ; Environmental Engineering/Biotechnology ; Enzymes ; Gel electrophoresis ; Glucaric acid ; Hemicellulose ; Hydrolysates ; Life Sciences ; Microbiology ; NAD ; Organic chemistry ; Original Paper ; pH effects ; Reagents ; Sodium lauryl sulfate ; Substrates ; Thermobispora bispora ; Uronate dehydrogenase ; Xylan ; Xylanase</subject><ispartof>World journal of microbiology & biotechnology, 2018-07, Vol.34 (7), p.102-13, Article 102</ispartof><rights>Springer Nature B.V. 2018</rights><rights>World Journal of Microbiology and Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-4b592d8c5ae4ab2448122e1cba627f46db3eaa254f4abaf5953f09779fe810743</citedby><cites>FETCH-LOGICAL-c409t-4b592d8c5ae4ab2448122e1cba627f46db3eaa254f4abaf5953f09779fe810743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11274-018-2486-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11274-018-2486-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29936649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yaxian</creatorcontrib><creatorcontrib>Xue, Yemin</creatorcontrib><creatorcontrib>Cao, Zhigang</creatorcontrib><creatorcontrib>Zhou, Tao</creatorcontrib><creatorcontrib>Alnadari, Fawze</creatorcontrib><title>Characterization of a uronate dehydrogenase from Thermobispora bispora for production of glucaric acid from hemicellulose substrate</title><title>World journal of microbiology & biotechnology</title><addtitle>World J Microbiol Biotechnol</addtitle><addtitle>World J Microbiol Biotechnol</addtitle><description>A thermostable uronate dehydrogenase Tb-UDH from
Thermobispora bispora
was over-expressed in
Escherichia coli
using the T7 polymerase expression system. The Tb-UDH was purified by metal affinity chromatography, and gave a single band on SDS-PAGE. The maximum activity on glucuronic acid was found at 60 °C and pH 7.0. The purified enzyme retained over 58% of its activity after holding a pH ranging from 7.0 to 7.5 for 1 h at 60 °C. The
K
m
and
V
max
values of the purified Tb-UDH for Glucuronic acid (GluUA) were 0.165 mM and 117.7 U mg
−1
, respectively, those for galacturonic acid (GalUA) were 0.115 mM and 104.2 U mg
−1
, respectively, and those for NAD
+
were 0.120 mM and 133.3 U mg
−1
, respectively; the turnover number (
k
cat
) with GluUA as a substrate was higher than that with GalUA; however, the Michaelis constant (
K
m
) for GalUA was lower than that for GluUA. After 60 min of incubation at 50 °C, Tb-UDH exhibited a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from breech xylans formed by xylanase and α-glucuronidase. This work shows that biocatalytic routes have great potential for the conversion of hemicellulose substrate into value-added products derived from renewable biomass.
TOC Graphic
(A) The structure of the xylan is described and the site of action of the xylan degrading enzyme is indicated. (B) The effect of substrate concentration on recombinant Tb-UDH activity when galacturonic acid was used as substrate. (C) SDS-PAGE analysis of E. coli BL21 (DE3) harboring pET-20b(+) and pET-20b-Tb-UDH. (D) Oxidative conversion of glucuronic acid from a beechwood xylan to glucaric acid</description><subject>Acids</subject><subject>Affinity chromatography</subject><subject>Applied Microbiology</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Conversion</subject><subject>Conversion ratio</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>E coli</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Enzymes</subject><subject>Gel electrophoresis</subject><subject>Glucaric acid</subject><subject>Hemicellulose</subject><subject>Hydrolysates</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>NAD</subject><subject>Organic chemistry</subject><subject>Original Paper</subject><subject>pH effects</subject><subject>Reagents</subject><subject>Sodium lauryl sulfate</subject><subject>Substrates</subject><subject>Thermobispora bispora</subject><subject>Uronate dehydrogenase</subject><subject>Xylan</subject><subject>Xylanase</subject><issn>0959-3993</issn><issn>1573-0972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU9r3DAQxUVJaTZpP0AvRZBLL271z7Z0DEvaFAK9pGcxlke7Dra1laxDeu0XjxZnGyjkNKD5vTcPPUI-cvaFM9Z-TZyLVlWM60oo3VT6DdnwupUVM604IxtmalNJY-Q5uUjpgbGiMvIdORflrWmU2ZC_2z1EcAvG4Q8sQ5hp8BRojmGGBWmP-8c-hh3OkJD6GCZ6v8c4hW5IhxCBnqYPkR5i6LM7mezG7CAOjoIb-lW6x2lwOI55DMUt5S4tsVx5T956GBN-eJ6X5Ne3m_vtbXX38_uP7fVd5RQzS6W62oheuxpQQSeU0lwI5K6DRrReNX0nEUDUypc1-NrU0pePaI1HzVmr5CX5vPqWoL8zpsVOQzrmgRlDTlaw2jAltWwKevUf-hBynEu6I6WFaYRhheIr5WJIKaK3hzhMEB8tZ_bYkF0bsqUhe2zI6qL59Oycuwn7f4pTJQUQK5DKat5hfDn9uusT5hCeeA</recordid><startdate>20180701</startdate><enddate>20180701</enddate><creator>Li, 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of a uronate dehydrogenase from Thermobispora bispora for production of glucaric acid from hemicellulose substrate</title><author>Li, Yaxian ; Xue, Yemin ; Cao, Zhigang ; Zhou, Tao ; Alnadari, Fawze</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-4b592d8c5ae4ab2448122e1cba627f46db3eaa254f4abaf5953f09779fe810743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Acids</topic><topic>Affinity chromatography</topic><topic>Applied Microbiology</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Conversion</topic><topic>Conversion ratio</topic><topic>Dehydrogenase</topic><topic>Dehydrogenases</topic><topic>E coli</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Enzymes</topic><topic>Gel electrophoresis</topic><topic>Glucaric acid</topic><topic>Hemicellulose</topic><topic>Hydrolysates</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>NAD</topic><topic>Organic chemistry</topic><topic>Original Paper</topic><topic>pH effects</topic><topic>Reagents</topic><topic>Sodium lauryl sulfate</topic><topic>Substrates</topic><topic>Thermobispora bispora</topic><topic>Uronate dehydrogenase</topic><topic>Xylan</topic><topic>Xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yaxian</creatorcontrib><creatorcontrib>Xue, Yemin</creatorcontrib><creatorcontrib>Cao, Zhigang</creatorcontrib><creatorcontrib>Zhou, Tao</creatorcontrib><creatorcontrib>Alnadari, Fawze</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology 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BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</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 Basic</collection><collection>MEDLINE - Academic</collection><jtitle>World journal of microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yaxian</au><au>Xue, Yemin</au><au>Cao, Zhigang</au><au>Zhou, Tao</au><au>Alnadari, Fawze</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a uronate dehydrogenase from Thermobispora bispora for production of glucaric acid from hemicellulose substrate</atitle><jtitle>World journal of microbiology & biotechnology</jtitle><stitle>World J Microbiol Biotechnol</stitle><addtitle>World J Microbiol Biotechnol</addtitle><date>2018-07-01</date><risdate>2018</risdate><volume>34</volume><issue>7</issue><spage>102</spage><epage>13</epage><pages>102-13</pages><artnum>102</artnum><issn>0959-3993</issn><eissn>1573-0972</eissn><abstract>A thermostable uronate dehydrogenase Tb-UDH from
Thermobispora bispora
was over-expressed in
Escherichia coli
using the T7 polymerase expression system. The Tb-UDH was purified by metal affinity chromatography, and gave a single band on SDS-PAGE. The maximum activity on glucuronic acid was found at 60 °C and pH 7.0. The purified enzyme retained over 58% of its activity after holding a pH ranging from 7.0 to 7.5 for 1 h at 60 °C. The
K
m
and
V
max
values of the purified Tb-UDH for Glucuronic acid (GluUA) were 0.165 mM and 117.7 U mg
−1
, respectively, those for galacturonic acid (GalUA) were 0.115 mM and 104.2 U mg
−1
, respectively, and those for NAD
+
were 0.120 mM and 133.3 U mg
−1
, respectively; the turnover number (
k
cat
) with GluUA as a substrate was higher than that with GalUA; however, the Michaelis constant (
K
m
) for GalUA was lower than that for GluUA. After 60 min of incubation at 50 °C, Tb-UDH exhibited a conversion ratio for glucuronic acid to the glucaric acid of 84% on chemical reagent and 81.3% on hydrolysates from breech xylans formed by xylanase and α-glucuronidase. This work shows that biocatalytic routes have great potential for the conversion of hemicellulose substrate into value-added products derived from renewable biomass.
TOC Graphic
(A) The structure of the xylan is described and the site of action of the xylan degrading enzyme is indicated. (B) The effect of substrate concentration on recombinant Tb-UDH activity when galacturonic acid was used as substrate. (C) SDS-PAGE analysis of E. coli BL21 (DE3) harboring pET-20b(+) and pET-20b-Tb-UDH. (D) Oxidative conversion of glucuronic acid from a beechwood xylan to glucaric acid</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>29936649</pmid><doi>10.1007/s11274-018-2486-8</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0959-3993 |
| ispartof | World journal of microbiology & biotechnology, 2018-07, Vol.34 (7), p.102-13, Article 102 |
| issn | 0959-3993 1573-0972 |
| language | eng |
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| source | SpringerLink Journals - AutoHoldings |
| subjects | Acids Affinity chromatography Applied Microbiology Biochemistry Biomedical and Life Sciences Biotechnology Conversion Conversion ratio Dehydrogenase Dehydrogenases E coli Environmental Engineering/Biotechnology Enzymes Gel electrophoresis Glucaric acid Hemicellulose Hydrolysates Life Sciences Microbiology NAD Organic chemistry Original Paper pH effects Reagents Sodium lauryl sulfate Substrates Thermobispora bispora Uronate dehydrogenase Xylan Xylanase |
| title | Characterization of a uronate dehydrogenase from Thermobispora bispora for production of glucaric acid from hemicellulose substrate |
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