Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli
S-thanatin, a small antimicrobial peptide with 21 amino acid residues, was expressed as a fusion protein containing thrombin cleavage site in Escherichia coli BL21 (DE3). To reduce the production cost, immobilization of thrombin in polyacrylamide gel for cleavage was studied in this work. The immobi...
Gespeichert in:
| Veröffentlicht in: | Applied microbiology and biotechnology 2011-10, Vol.92 (1), p.85-93 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 93 |
|---|---|
| container_issue | 1 |
| container_start_page | 85 |
| container_title | Applied microbiology and biotechnology |
| container_volume | 92 |
| creator | Wu, Guoqiu Deng, Xuepeng Li, Xiaofang Wang, Xiyong Wang, Shenglan Xu, Hanmei |
| description | S-thanatin, a small antimicrobial peptide with 21 amino acid residues, was expressed as a fusion protein containing thrombin cleavage site in
Escherichia coli
BL21 (DE3). To reduce the production cost, immobilization of thrombin in polyacrylamide gel for cleavage was studied in this work. The immobilized thrombin exhibited excellent activity within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity could remain above 75% after ten times of usage. Tricine–SDS–PAGE result showed that the immobilized thrombin could cleave the S-thanatin fusion protein effectively. After cleavage, recombinant S-thanatin was purified by preparative reversed-phase high-performance liquid chromatography and mass spectrum showed that the molecular weight (2,448.86) was close to the theoretical value (2,448.98). After purification, about 7 mg of S-thanatin was obtained from 1 l of culture and the recombinant exhibited excellent bioactivity to
E. coli
ATCC 25922, with the minimum inhibitory concentration of 12 μg/ml. The purification method could be applied to prepare other peptides with similar properties at low cost. |
| doi_str_mv | 10.1007/s00253-011-3379-z |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_907170654</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A614152784</galeid><sourcerecordid>A614152784</sourcerecordid><originalsourceid>FETCH-LOGICAL-c463t-f3408558c2b40a89f0381f1aaed1c2268b80014f578e343cdc225351852cc0193</originalsourceid><addsrcrecordid>eNqFkl1rFDEUhoModq3-AG9ksIh4MTWfM5nLpVQtFASrt4ZMJtlNmUnGZAbq_nrPMlvLiiK5CDl53vORvAi9JPicYFy_zxhTwUpMSMlY3ZS7R2hFOKMlrgh_jFaY1KKsRSNP0LOcbzEmVFbVU3RCSSVEUzcr9H09jr03evIxFNEVfhhi63u_s10xbVMcWh8KF1MxptjN5h67KaetDqAKhb0bk80ZeDhcZrO1yZut14WJvX-OnjjdZ_visJ-ibx8uv158Kq8_f7y6WF-XhldsKh3jWAohDW051rJxmEniiNa2I4bSSrYSmudO1NIyzkwHQcEEkYIag0nDTtHbJS-0-WO2eVKDz8b2vQ42zlk1uCY1rgT_Lyllw7mQTAL5-g_yNs4pwBgAyaqBliuAzhZoo3urfHBxStrsU6o1fAIRtJb7oud_oWB1dvAmBus8xI8E744EwEz2btroOWd1dfPlmCULa1LMOVmnxuQHnX4qgtXeJ2rxiQKfqL1P1A40rw6zze1gu9-Ke2MA8OYA6Gx075IOxucHjgsYn9bA0YXLcBU2Nj080r-r_wKWNtHq</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>888694086</pqid></control><display><type>article</type><title>Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Wu, Guoqiu ; Deng, Xuepeng ; Li, Xiaofang ; Wang, Xiyong ; Wang, Shenglan ; Xu, Hanmei</creator><creatorcontrib>Wu, Guoqiu ; Deng, Xuepeng ; Li, Xiaofang ; Wang, Xiyong ; Wang, Shenglan ; Xu, Hanmei</creatorcontrib><description>S-thanatin, a small antimicrobial peptide with 21 amino acid residues, was expressed as a fusion protein containing thrombin cleavage site in
Escherichia coli
BL21 (DE3). To reduce the production cost, immobilization of thrombin in polyacrylamide gel for cleavage was studied in this work. The immobilized thrombin exhibited excellent activity within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity could remain above 75% after ten times of usage. Tricine–SDS–PAGE result showed that the immobilized thrombin could cleave the S-thanatin fusion protein effectively. After cleavage, recombinant S-thanatin was purified by preparative reversed-phase high-performance liquid chromatography and mass spectrum showed that the molecular weight (2,448.86) was close to the theoretical value (2,448.98). After purification, about 7 mg of S-thanatin was obtained from 1 l of culture and the recombinant exhibited excellent bioactivity to
E. coli
ATCC 25922, with the minimum inhibitory concentration of 12 μg/ml. The purification method could be applied to prepare other peptides with similar properties at low cost.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-011-3379-z</identifier><identifier>PMID: 21655979</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino acids ; Antibiotics ; Antimicrobial agents ; Antimicrobial Cationic Peptides - genetics ; Antimicrobial Cationic Peptides - isolation & purification ; Antimicrobial Cationic Peptides - metabolism ; Biological activity ; Biological and medical sciences ; Biotechnological Products and Process Engineering ; Biotechnology ; Chromatography ; Cloning ; E coli ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Enzymes ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Ethylenediaminetetraacetic acid ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; High performance liquid chromatography ; Hydrogen-Ion Concentration ; Life Sciences ; Liquid chromatography ; Microbial Genetics and Genomics ; Microbial Sensitivity Tests ; Microbiology ; Molecular Weight ; Peptides ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - metabolism ; Studies ; Temperature ; Thrombin ; Thrombin - chemistry ; Thrombin - metabolism</subject><ispartof>Applied microbiology and biotechnology, 2011-10, Vol.92 (1), p.85-93</ispartof><rights>Springer-Verlag 2011</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2011 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-f3408558c2b40a89f0381f1aaed1c2268b80014f578e343cdc225351852cc0193</citedby><cites>FETCH-LOGICAL-c463t-f3408558c2b40a89f0381f1aaed1c2268b80014f578e343cdc225351852cc0193</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/s00253-011-3379-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-011-3379-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24540827$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21655979$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Guoqiu</creatorcontrib><creatorcontrib>Deng, Xuepeng</creatorcontrib><creatorcontrib>Li, Xiaofang</creatorcontrib><creatorcontrib>Wang, Xiyong</creatorcontrib><creatorcontrib>Wang, Shenglan</creatorcontrib><creatorcontrib>Xu, Hanmei</creatorcontrib><title>Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>S-thanatin, a small antimicrobial peptide with 21 amino acid residues, was expressed as a fusion protein containing thrombin cleavage site in
Escherichia coli
BL21 (DE3). To reduce the production cost, immobilization of thrombin in polyacrylamide gel for cleavage was studied in this work. The immobilized thrombin exhibited excellent activity within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity could remain above 75% after ten times of usage. Tricine–SDS–PAGE result showed that the immobilized thrombin could cleave the S-thanatin fusion protein effectively. After cleavage, recombinant S-thanatin was purified by preparative reversed-phase high-performance liquid chromatography and mass spectrum showed that the molecular weight (2,448.86) was close to the theoretical value (2,448.98). After purification, about 7 mg of S-thanatin was obtained from 1 l of culture and the recombinant exhibited excellent bioactivity to
E. coli
ATCC 25922, with the minimum inhibitory concentration of 12 μg/ml. The purification method could be applied to prepare other peptides with similar properties at low cost.</description><subject>Amino acids</subject><subject>Antibiotics</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial Cationic Peptides - genetics</subject><subject>Antimicrobial Cationic Peptides - isolation & purification</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Biological activity</subject><subject>Biological and medical sciences</subject><subject>Biotechnological Products and Process Engineering</subject><subject>Biotechnology</subject><subject>Chromatography</subject><subject>Cloning</subject><subject>E coli</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>High performance liquid chromatography</subject><subject>Hydrogen-Ion Concentration</subject><subject>Life Sciences</subject><subject>Liquid chromatography</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Studies</subject><subject>Temperature</subject><subject>Thrombin</subject><subject>Thrombin - chemistry</subject><subject>Thrombin - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</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>eNqFkl1rFDEUhoModq3-AG9ksIh4MTWfM5nLpVQtFASrt4ZMJtlNmUnGZAbq_nrPMlvLiiK5CDl53vORvAi9JPicYFy_zxhTwUpMSMlY3ZS7R2hFOKMlrgh_jFaY1KKsRSNP0LOcbzEmVFbVU3RCSSVEUzcr9H09jr03evIxFNEVfhhi63u_s10xbVMcWh8KF1MxptjN5h67KaetDqAKhb0bk80ZeDhcZrO1yZut14WJvX-OnjjdZ_visJ-ibx8uv158Kq8_f7y6WF-XhldsKh3jWAohDW051rJxmEniiNa2I4bSSrYSmudO1NIyzkwHQcEEkYIag0nDTtHbJS-0-WO2eVKDz8b2vQ42zlk1uCY1rgT_Lyllw7mQTAL5-g_yNs4pwBgAyaqBliuAzhZoo3urfHBxStrsU6o1fAIRtJb7oud_oWB1dvAmBus8xI8E744EwEz2btroOWd1dfPlmCULa1LMOVmnxuQHnX4qgtXeJ2rxiQKfqL1P1A40rw6zze1gu9-Ke2MA8OYA6Gx075IOxucHjgsYn9bA0YXLcBU2Nj080r-r_wKWNtHq</recordid><startdate>20111001</startdate><enddate>20111001</enddate><creator>Wu, Guoqiu</creator><creator>Deng, Xuepeng</creator><creator>Li, Xiaofang</creator><creator>Wang, Xiyong</creator><creator>Wang, Shenglan</creator><creator>Xu, Hanmei</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20111001</creationdate><title>Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli</title><author>Wu, Guoqiu ; Deng, Xuepeng ; Li, Xiaofang ; Wang, Xiyong ; Wang, Shenglan ; Xu, Hanmei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-f3408558c2b40a89f0381f1aaed1c2268b80014f578e343cdc225351852cc0193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Antibiotics</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial Cationic Peptides - genetics</topic><topic>Antimicrobial Cationic Peptides - isolation & purification</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Biological activity</topic><topic>Biological and medical sciences</topic><topic>Biotechnological Products and Process Engineering</topic><topic>Biotechnology</topic><topic>Chromatography</topic><topic>Cloning</topic><topic>E coli</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>High performance liquid chromatography</topic><topic>Hydrogen-Ion Concentration</topic><topic>Life Sciences</topic><topic>Liquid chromatography</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Studies</topic><topic>Temperature</topic><topic>Thrombin</topic><topic>Thrombin - chemistry</topic><topic>Thrombin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Guoqiu</creatorcontrib><creatorcontrib>Deng, Xuepeng</creatorcontrib><creatorcontrib>Li, Xiaofang</creatorcontrib><creatorcontrib>Wang, Xiyong</creatorcontrib><creatorcontrib>Wang, Shenglan</creatorcontrib><creatorcontrib>Xu, Hanmei</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</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 (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech 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>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Business Premium Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>One Business (ProQuest)</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><collection>Biotechnology Research Abstracts</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Guoqiu</au><au>Deng, Xuepeng</au><au>Li, Xiaofang</au><au>Wang, Xiyong</au><au>Wang, Shenglan</au><au>Xu, Hanmei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2011-10-01</date><risdate>2011</risdate><volume>92</volume><issue>1</issue><spage>85</spage><epage>93</epage><pages>85-93</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>S-thanatin, a small antimicrobial peptide with 21 amino acid residues, was expressed as a fusion protein containing thrombin cleavage site in
Escherichia coli
BL21 (DE3). To reduce the production cost, immobilization of thrombin in polyacrylamide gel for cleavage was studied in this work. The immobilized thrombin exhibited excellent activity within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity could remain above 75% after ten times of usage. Tricine–SDS–PAGE result showed that the immobilized thrombin could cleave the S-thanatin fusion protein effectively. After cleavage, recombinant S-thanatin was purified by preparative reversed-phase high-performance liquid chromatography and mass spectrum showed that the molecular weight (2,448.86) was close to the theoretical value (2,448.98). After purification, about 7 mg of S-thanatin was obtained from 1 l of culture and the recombinant exhibited excellent bioactivity to
E. coli
ATCC 25922, with the minimum inhibitory concentration of 12 μg/ml. The purification method could be applied to prepare other peptides with similar properties at low cost.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>21655979</pmid><doi>10.1007/s00253-011-3379-z</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2011-10, Vol.92 (1), p.85-93 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_907170654 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino acids Antibiotics Antimicrobial agents Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - isolation & purification Antimicrobial Cationic Peptides - metabolism Biological activity Biological and medical sciences Biotechnological Products and Process Engineering Biotechnology Chromatography Cloning E coli Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Escherichia coli Escherichia coli - genetics Ethylenediaminetetraacetic acid Fundamental and applied biological sciences. Psychology Gene Expression High performance liquid chromatography Hydrogen-Ion Concentration Life Sciences Liquid chromatography Microbial Genetics and Genomics Microbial Sensitivity Tests Microbiology Molecular Weight Peptides Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Studies Temperature Thrombin Thrombin - chemistry Thrombin - metabolism |
| title | Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T14%3A41%3A53IST&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=Application%20of%20immobilized%20thrombin%20for%20production%20of%20S-thanatin%20expressed%20in%20Escherichia%20coli&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Wu,%20Guoqiu&rft.date=2011-10-01&rft.volume=92&rft.issue=1&rft.spage=85&rft.epage=93&rft.pages=85-93&rft.issn=0175-7598&rft.eissn=1432-0614&rft.coden=AMBIDG&rft_id=info:doi/10.1007/s00253-011-3379-z&rft_dat=%3Cgale_proqu%3EA614152784%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=888694086&rft_id=info:pmid/21655979&rft_galeid=A614152784&rfr_iscdi=true |