Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6

Xylanase is one of industrial enzymes with diverse applications including the paper-bleaching industry and feed additives. Here, a strain having xylanolytic activity and identified as Bacillus sonorensis T6 was isolated from soil. A secretory enzyme was identified by mass-spectrometry as a xylanase...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2022-03, Vol.17 (3), p.e0265647-e0265647
Main Authors: Kiribayeva, Assel, Mukanov, Birzhan, Silayev, Dmitriy, Akishev, Zhiger, Ramankulov, Yerlan, Khassenov, Bekbolat
Format: Article
Language:English
Subjects:
Additives
Analysis
Bacillus
Bacillus sonorensis
Bacteria
Biology and Life Sciences
Biotechnology
Bleaching
Cellulose
Chromatography
Cloning
Cloning, Molecular
E coli
Endo-1,4-beta Xylanases - metabolism
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Feed additives
Feed industry
Food additives
Gene expression
Glycosidases
Glycosyl hydrolase
Hydrogen-Ion Concentration
Hydrolase
Identification and classification
Mass spectrometry
Medicine and Health Sciences
Microorganisms
Molecular weight
pH effects
Physical Sciences
Pichia - genetics
Pichia - metabolism
Plasmids
Proteins
Recombinant Proteins - metabolism
Research and Analysis Methods
Scientific imaging
Spectrometry
Temperature
Thermal stability
Xylanase
Xylanases
Yeast
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63
cites cdi_FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63
container_end_page e0265647
container_issue 3
container_start_page e0265647
container_title PloS one
container_volume 17
creator Kiribayeva, Assel
Mukanov, Birzhan
Silayev, Dmitriy
Akishev, Zhiger
Ramankulov, Yerlan
Khassenov, Bekbolat
description Xylanase is one of industrial enzymes with diverse applications including the paper-bleaching industry and feed additives. Here, a strain having xylanolytic activity and identified as Bacillus sonorensis T6 was isolated from soil. A secretory enzyme was identified by mass-spectrometry as a xylanase of glycosyl hydrolase family 11, with a molecular weight of 23.3 kDa. The xylanase gene of Bacillus sonorensis T6 was cloned and expressed in Escherichia coli (yielding an enzyme designated as rXynT6-E) and in Pichia pastoris (yielding rXynT6-P). The recombinant xylanases were found to have optimal activity at 47-55°C and pH 6.0-7.0. The recombinant xylanase expressed in P. pastoris has 40% higher thermal stability than that expressed in E. coli. The recombinant xylanases retained 100% of activity after 10 h incubation in the pH range 3-11 and 68% of activity after 1 h at pH 2.0. The xylanase activities of rXynT6-E and rXynT6-P under optimal conditions were 1030.2 and 873.8 U/mg, respectively. The good stability in a wide range of pH and moderate temperatures may make the xylanase from Bacillus sonorensis T6 useful for various biotechnological applications, e.g., as an enzyme additive in the feed industry.
doi_str_mv 10.1371/journal.pone.0265647
format article
fullrecord <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_2640287241</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A697151906</galeid><doaj_id>oai_doaj_org_article_b0f559c0629344a4a39354a7f595cde4</doaj_id><sourcerecordid>A697151906</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63</originalsourceid><addsrcrecordid>eNqNk22L1DAQx4so3nn6DUQLgijcrnlo0uaNcC4-LBwc6OnbME3T3SzZZE1a2fPTm7q9Yyv3QvIiYfKb_2QmM1n2HKM5piV-t_F9cGDnO-_0HBHOeFE-yE6xoGTGCaIPj84n2ZMYNwgxWnH-ODuhjIiKMXyayYX1zrjVea73u6BjNN6d5-CaXK0hgOp0ML-hS9bctznkQSu_rY0D1-X7GwsOos7b4Lf5B1DG2j7m0TsftIsm5tf8afaoBRv1s3E_y75_-ni9-DK7vPq8XFxczhSjZTlTCCquaV2rUuiSspQhqZloEGZaKMEYKmlDgFYU2gYLrrkoMEJCIw6UKk7PspcH3Z31UY61iZLwApGqJAVOxPJANB42chfMFsKN9GDkX4MPKwmhM8pqWaOWMaEQJ4IWBRRABWUFlC0TTDW6SFrvx2h9vdWN0q4LYCei0xtn1nLlf8lKkJTM8Nw3o0DwP3sdO7k1UWmbCqp9f3i3EJgKktBX_6D3ZzdSK0gJGNf6FFcNovKCixIzLNAQdn4PlVajt0alRmpNsk8c3k4cEtPpfbeCPka5_Pb1_9mrH1P29RG71mC7dfS2HxotTsHiAKrgYwy6vSsyRnKYg9tqyGEO5DgHye3F8QfdOd02Pv0DWD4BhQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2640287241</pqid></control><display><type>article</type><title>Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6</title><source>Open Access: PubMed Central</source><source>Publicly Available Content Database</source><creator>Kiribayeva, Assel ; Mukanov, Birzhan ; Silayev, Dmitriy ; Akishev, Zhiger ; Ramankulov, Yerlan ; Khassenov, Bekbolat</creator><contributor>Bhatia, Shashi Kant</contributor><creatorcontrib>Kiribayeva, Assel ; Mukanov, Birzhan ; Silayev, Dmitriy ; Akishev, Zhiger ; Ramankulov, Yerlan ; Khassenov, Bekbolat ; Bhatia, Shashi Kant</creatorcontrib><description>Xylanase is one of industrial enzymes with diverse applications including the paper-bleaching industry and feed additives. Here, a strain having xylanolytic activity and identified as Bacillus sonorensis T6 was isolated from soil. A secretory enzyme was identified by mass-spectrometry as a xylanase of glycosyl hydrolase family 11, with a molecular weight of 23.3 kDa. The xylanase gene of Bacillus sonorensis T6 was cloned and expressed in Escherichia coli (yielding an enzyme designated as rXynT6-E) and in Pichia pastoris (yielding rXynT6-P). The recombinant xylanases were found to have optimal activity at 47-55°C and pH 6.0-7.0. The recombinant xylanase expressed in P. pastoris has 40% higher thermal stability than that expressed in E. coli. The recombinant xylanases retained 100% of activity after 10 h incubation in the pH range 3-11 and 68% of activity after 1 h at pH 2.0. The xylanase activities of rXynT6-E and rXynT6-P under optimal conditions were 1030.2 and 873.8 U/mg, respectively. The good stability in a wide range of pH and moderate temperatures may make the xylanase from Bacillus sonorensis T6 useful for various biotechnological applications, e.g., as an enzyme additive in the feed industry.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0265647</identifier><identifier>PMID: 35298551</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Additives ; Analysis ; Bacillus ; Bacillus sonorensis ; Bacteria ; Biology and Life Sciences ; Biotechnology ; Bleaching ; Cellulose ; Chromatography ; Cloning ; Cloning, Molecular ; E coli ; Endo-1,4-beta Xylanases - metabolism ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Feed additives ; Feed industry ; Food additives ; Gene expression ; Glycosidases ; Glycosyl hydrolase ; Hydrogen-Ion Concentration ; Hydrolase ; Identification and classification ; Mass spectrometry ; Medicine and Health Sciences ; Microorganisms ; Molecular weight ; pH effects ; Physical Sciences ; Pichia - genetics ; Pichia - metabolism ; Plasmids ; Proteins ; Recombinant Proteins - metabolism ; Research and Analysis Methods ; Scientific imaging ; Spectrometry ; Temperature ; Thermal stability ; Xylanase ; Xylanases ; Yeast</subject><ispartof>PloS one, 2022-03, Vol.17 (3), p.e0265647-e0265647</ispartof><rights>COPYRIGHT 2022 Public Library of Science</rights><rights>2022 Kiribayeva et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 Kiribayeva et al 2022 Kiribayeva et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63</citedby><cites>FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63</cites><orcidid>0000-0002-8293-2340 ; 0000-0001-9943-1625</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2640287241/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2640287241?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,315,733,786,790,891,25783,27957,27958,37047,37048,44625,53827,53829,75483</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35298551$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bhatia, Shashi Kant</contributor><creatorcontrib>Kiribayeva, Assel</creatorcontrib><creatorcontrib>Mukanov, Birzhan</creatorcontrib><creatorcontrib>Silayev, Dmitriy</creatorcontrib><creatorcontrib>Akishev, Zhiger</creatorcontrib><creatorcontrib>Ramankulov, Yerlan</creatorcontrib><creatorcontrib>Khassenov, Bekbolat</creatorcontrib><title>Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Xylanase is one of industrial enzymes with diverse applications including the paper-bleaching industry and feed additives. Here, a strain having xylanolytic activity and identified as Bacillus sonorensis T6 was isolated from soil. A secretory enzyme was identified by mass-spectrometry as a xylanase of glycosyl hydrolase family 11, with a molecular weight of 23.3 kDa. The xylanase gene of Bacillus sonorensis T6 was cloned and expressed in Escherichia coli (yielding an enzyme designated as rXynT6-E) and in Pichia pastoris (yielding rXynT6-P). The recombinant xylanases were found to have optimal activity at 47-55°C and pH 6.0-7.0. The recombinant xylanase expressed in P. pastoris has 40% higher thermal stability than that expressed in E. coli. The recombinant xylanases retained 100% of activity after 10 h incubation in the pH range 3-11 and 68% of activity after 1 h at pH 2.0. The xylanase activities of rXynT6-E and rXynT6-P under optimal conditions were 1030.2 and 873.8 U/mg, respectively. The good stability in a wide range of pH and moderate temperatures may make the xylanase from Bacillus sonorensis T6 useful for various biotechnological applications, e.g., as an enzyme additive in the feed industry.</description><subject>Additives</subject><subject>Analysis</subject><subject>Bacillus</subject><subject>Bacillus sonorensis</subject><subject>Bacteria</subject><subject>Biology and Life Sciences</subject><subject>Biotechnology</subject><subject>Bleaching</subject><subject>Cellulose</subject><subject>Chromatography</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Feed additives</subject><subject>Feed industry</subject><subject>Food additives</subject><subject>Gene expression</subject><subject>Glycosidases</subject><subject>Glycosyl hydrolase</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolase</subject><subject>Identification and classification</subject><subject>Mass spectrometry</subject><subject>Medicine and Health Sciences</subject><subject>Microorganisms</subject><subject>Molecular weight</subject><subject>pH effects</subject><subject>Physical Sciences</subject><subject>Pichia - genetics</subject><subject>Pichia - metabolism</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Research and Analysis Methods</subject><subject>Scientific imaging</subject><subject>Spectrometry</subject><subject>Temperature</subject><subject>Thermal stability</subject><subject>Xylanase</subject><subject>Xylanases</subject><subject>Yeast</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqNk22L1DAQx4so3nn6DUQLgijcrnlo0uaNcC4-LBwc6OnbME3T3SzZZE1a2fPTm7q9Yyv3QvIiYfKb_2QmM1n2HKM5piV-t_F9cGDnO-_0HBHOeFE-yE6xoGTGCaIPj84n2ZMYNwgxWnH-ODuhjIiKMXyayYX1zrjVea73u6BjNN6d5-CaXK0hgOp0ML-hS9bctznkQSu_rY0D1-X7GwsOos7b4Lf5B1DG2j7m0TsftIsm5tf8afaoBRv1s3E_y75_-ni9-DK7vPq8XFxczhSjZTlTCCquaV2rUuiSspQhqZloEGZaKMEYKmlDgFYU2gYLrrkoMEJCIw6UKk7PspcH3Z31UY61iZLwApGqJAVOxPJANB42chfMFsKN9GDkX4MPKwmhM8pqWaOWMaEQJ4IWBRRABWUFlC0TTDW6SFrvx2h9vdWN0q4LYCei0xtn1nLlf8lKkJTM8Nw3o0DwP3sdO7k1UWmbCqp9f3i3EJgKktBX_6D3ZzdSK0gJGNf6FFcNovKCixIzLNAQdn4PlVajt0alRmpNsk8c3k4cEtPpfbeCPka5_Pb1_9mrH1P29RG71mC7dfS2HxotTsHiAKrgYwy6vSsyRnKYg9tqyGEO5DgHye3F8QfdOd02Pv0DWD4BhQ</recordid><startdate>20220317</startdate><enddate>20220317</enddate><creator>Kiribayeva, Assel</creator><creator>Mukanov, Birzhan</creator><creator>Silayev, Dmitriy</creator><creator>Akishev, Zhiger</creator><creator>Ramankulov, Yerlan</creator><creator>Khassenov, Bekbolat</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-8293-2340</orcidid><orcidid>https://orcid.org/0000-0001-9943-1625</orcidid></search><sort><creationdate>20220317</creationdate><title>Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6</title><author>Kiribayeva, Assel ; Mukanov, Birzhan ; Silayev, Dmitriy ; Akishev, Zhiger ; Ramankulov, Yerlan ; Khassenov, Bekbolat</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Additives</topic><topic>Analysis</topic><topic>Bacillus</topic><topic>Bacillus sonorensis</topic><topic>Bacteria</topic><topic>Biology and Life Sciences</topic><topic>Biotechnology</topic><topic>Bleaching</topic><topic>Cellulose</topic><topic>Chromatography</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>E coli</topic><topic>Endo-1,4-beta Xylanases - metabolism</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Feed additives</topic><topic>Feed industry</topic><topic>Food additives</topic><topic>Gene expression</topic><topic>Glycosidases</topic><topic>Glycosyl hydrolase</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolase</topic><topic>Identification and classification</topic><topic>Mass spectrometry</topic><topic>Medicine and Health Sciences</topic><topic>Microorganisms</topic><topic>Molecular weight</topic><topic>pH effects</topic><topic>Physical Sciences</topic><topic>Pichia - genetics</topic><topic>Pichia - metabolism</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Research and Analysis Methods</topic><topic>Scientific imaging</topic><topic>Spectrometry</topic><topic>Temperature</topic><topic>Thermal stability</topic><topic>Xylanase</topic><topic>Xylanases</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kiribayeva, Assel</creatorcontrib><creatorcontrib>Mukanov, Birzhan</creatorcontrib><creatorcontrib>Silayev, Dmitriy</creatorcontrib><creatorcontrib>Akishev, Zhiger</creatorcontrib><creatorcontrib>Ramankulov, Yerlan</creatorcontrib><creatorcontrib>Khassenov, Bekbolat</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Opposing Viewpoints Resource Center</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing &amp; Allied Health Database (ProQuest)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological &amp; Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health &amp; Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database (Proquest)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Advanced Technologies &amp; Aerospace Database‎ (1962 - current)</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>Meteorological &amp; Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing &amp; Allied Health Premium</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</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>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kiribayeva, Assel</au><au>Mukanov, Birzhan</au><au>Silayev, Dmitriy</au><au>Akishev, Zhiger</au><au>Ramankulov, Yerlan</au><au>Khassenov, Bekbolat</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2022-03-17</date><risdate>2022</risdate><volume>17</volume><issue>3</issue><spage>e0265647</spage><epage>e0265647</epage><pages>e0265647-e0265647</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><notes>Competing Interests: The authors have declared that no competing interests exist.</notes><abstract>Xylanase is one of industrial enzymes with diverse applications including the paper-bleaching industry and feed additives. Here, a strain having xylanolytic activity and identified as Bacillus sonorensis T6 was isolated from soil. A secretory enzyme was identified by mass-spectrometry as a xylanase of glycosyl hydrolase family 11, with a molecular weight of 23.3 kDa. The xylanase gene of Bacillus sonorensis T6 was cloned and expressed in Escherichia coli (yielding an enzyme designated as rXynT6-E) and in Pichia pastoris (yielding rXynT6-P). The recombinant xylanases were found to have optimal activity at 47-55°C and pH 6.0-7.0. The recombinant xylanase expressed in P. pastoris has 40% higher thermal stability than that expressed in E. coli. The recombinant xylanases retained 100% of activity after 10 h incubation in the pH range 3-11 and 68% of activity after 1 h at pH 2.0. The xylanase activities of rXynT6-E and rXynT6-P under optimal conditions were 1030.2 and 873.8 U/mg, respectively. The good stability in a wide range of pH and moderate temperatures may make the xylanase from Bacillus sonorensis T6 useful for various biotechnological applications, e.g., as an enzyme additive in the feed industry.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>35298551</pmid><doi>10.1371/journal.pone.0265647</doi><tpages>e0265647</tpages><orcidid>https://orcid.org/0000-0002-8293-2340</orcidid><orcidid>https://orcid.org/0000-0001-9943-1625</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1932-6203
ispartof PloS one, 2022-03, Vol.17 (3), p.e0265647-e0265647
issn 1932-6203
1932-6203
language eng
recordid cdi_plos_journals_2640287241
source Open Access: PubMed Central; Publicly Available Content Database
subjects Additives
Analysis
Bacillus
Bacillus sonorensis
Bacteria
Biology and Life Sciences
Biotechnology
Bleaching
Cellulose
Chromatography
Cloning
Cloning, Molecular
E coli
Endo-1,4-beta Xylanases - metabolism
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Feed additives
Feed industry
Food additives
Gene expression
Glycosidases
Glycosyl hydrolase
Hydrogen-Ion Concentration
Hydrolase
Identification and classification
Mass spectrometry
Medicine and Health Sciences
Microorganisms
Molecular weight
pH effects
Physical Sciences
Pichia - genetics
Pichia - metabolism
Plasmids
Proteins
Recombinant Proteins - metabolism
Research and Analysis Methods
Scientific imaging
Spectrometry
Temperature
Thermal stability
Xylanase
Xylanases
Yeast
title Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-21T22%3A46%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning,%20expression,%20and%20characterization%20of%20a%20recombinant%20xylanase%20from%20Bacillus%20sonorensis%20T6&rft.jtitle=PloS%20one&rft.au=Kiribayeva,%20Assel&rft.date=2022-03-17&rft.volume=17&rft.issue=3&rft.spage=e0265647&rft.epage=e0265647&rft.pages=e0265647-e0265647&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0265647&rft_dat=%3Cgale_plos_%3EA697151906%3C/gale_plos_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c5377-c0a86e3bbc79e7351372b59d015e9c955073d2a383afd196e6941009e06a33c63%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2640287241&rft_id=info:pmid/35298551&rft_galeid=A697151906&rfr_iscdi=true