Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii
The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 k...
Gespeichert in:
| Veröffentlicht in: | Applied biochemistry and biotechnology 2013-12, Vol.171 (8), p.2040-2052 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2052 |
|---|---|
| container_issue | 8 |
| container_start_page | 2040 |
| container_title | Applied biochemistry and biotechnology |
| container_volume | 171 |
| creator | Chandel, Meenakshi Azmi, Wamik |
| description | The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified tyrosine phenol lyase showed maximum activity in borate buffer (0.05 M at pH 8.5) at 45 °C after 20 min of incubation. The K ₘ and V ₘₐₓ values of purified enzyme were found to be 0.446 mm and 0.342 mM/min/mg. This enzyme exhibits t ₁/₂ of 10, 52 and 130 min at 55, 45 and 35 °C, respectively. The N-terminal amino acid sequence was determined as MET-ASN-TYR-PRO-ALA-GLU-PRO-PHE-ARG-ILE-TRP-TRP-VAL-GLY. |
| doi_str_mv | 10.1007/s12010-013-0491-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1490707928</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1490707928</sourcerecordid><originalsourceid>FETCH-LOGICAL-c426t-733d0bce9f5cd1740b82810ca72f3b28149b021e191680ecfa6799f0ecd869bf3</originalsourceid><addsrcrecordid>eNp9kE2LFDEQhoMo7rj6A7xogwheWquqP5Icl8EvGHDB2XNIp5PdLD3JmnQfxl9v1h4_8OCpisrzvql6GXuO8BYB-LuMBAg1YFNDK7GWD9gGu07WQBIfsg0Qb2oiIc_Yk5xvAZBExx-zM2qBiHOxYfvLJXnnjZ59DJUOY7W90Umb2Sb_fR1GV-2PKWYfbHV5Y0Ocqt1RZ1u5FA_V1s8pDj8FZWCXMHr_lD1yesr22ames6sP7_fbT_Xuy8fP24tdbVrq55o3zQiDsdJ1ZkTewiBIIBjNyTVDaVs5AKFFib0Aa5zuuZSudKPo5eCac_Zm9b1L8dti86wOPhs7TTrYuGRVDIADlyQK-uof9DYuKZTtCtUj70oaVChcKVPuzck6dZf8QaejQlD3kas1clUiV_eRK1k0L07Oy3Cw42_Fr4wL8PoE6Gz05JIOxuc_nIAOBbSFo5XL5Slc2_TXiv_5_eUqcjoqfZ2K8dXXArUA0FHfNs0Pe-yhFw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1461757782</pqid></control><display><type>article</type><title>Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Chandel, Meenakshi ; Azmi, Wamik</creator><creatorcontrib>Chandel, Meenakshi ; Azmi, Wamik</creatorcontrib><description>The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified tyrosine phenol lyase showed maximum activity in borate buffer (0.05 M at pH 8.5) at 45 °C after 20 min of incubation. The K ₘ and V ₘₐₓ values of purified enzyme were found to be 0.446 mm and 0.342 mM/min/mg. This enzyme exhibits t ₁/₂ of 10, 52 and 130 min at 55, 45 and 35 °C, respectively. The N-terminal amino acid sequence was determined as MET-ASN-TYR-PRO-ALA-GLU-PRO-PHE-ARG-ILE-TRP-TRP-VAL-GLY.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-013-0491-9</identifier><identifier>PMID: 24022778</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Amino acids ; Ammonium ; ammonium sulfate ; Biochemistry ; Biological and medical sciences ; Biotechnology ; carbon-carbon lyases ; Chemistry ; Chemistry and Materials Science ; Chromatography ; Citrobacter freundii ; Citrobacter freundii - enzymology ; Dipeptides - chemistry ; Enzymes ; Fundamental and applied biological sciences. Psychology ; hydrophobic bonding ; Kinetics ; Molecular Weight ; phenol ; Phenols ; polyacrylamide gel electrophoresis ; sodium dodecyl sulfate ; Sulfates ; tyrosine ; Tyrosine Phenol-Lyase - chemistry ; Tyrosine Phenol-Lyase - isolation & purification</subject><ispartof>Applied biochemistry and biotechnology, 2013-12, Vol.171 (8), p.2040-2052</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-733d0bce9f5cd1740b82810ca72f3b28149b021e191680ecfa6799f0ecd869bf3</citedby><cites>FETCH-LOGICAL-c426t-733d0bce9f5cd1740b82810ca72f3b28149b021e191680ecfa6799f0ecd869bf3</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/s12010-013-0491-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-013-0491-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28051804$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24022778$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chandel, Meenakshi</creatorcontrib><creatorcontrib>Azmi, Wamik</creatorcontrib><title>Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified tyrosine phenol lyase showed maximum activity in borate buffer (0.05 M at pH 8.5) at 45 °C after 20 min of incubation. The K ₘ and V ₘₐₓ values of purified enzyme were found to be 0.446 mm and 0.342 mM/min/mg. This enzyme exhibits t ₁/₂ of 10, 52 and 130 min at 55, 45 and 35 °C, respectively. The N-terminal amino acid sequence was determined as MET-ASN-TYR-PRO-ALA-GLU-PRO-PHE-ARG-ILE-TRP-TRP-VAL-GLY.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Ammonium</subject><subject>ammonium sulfate</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>carbon-carbon lyases</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography</subject><subject>Citrobacter freundii</subject><subject>Citrobacter freundii - enzymology</subject><subject>Dipeptides - chemistry</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hydrophobic bonding</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>phenol</subject><subject>Phenols</subject><subject>polyacrylamide gel electrophoresis</subject><subject>sodium dodecyl sulfate</subject><subject>Sulfates</subject><subject>tyrosine</subject><subject>Tyrosine Phenol-Lyase - chemistry</subject><subject>Tyrosine Phenol-Lyase - isolation & purification</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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>eNp9kE2LFDEQhoMo7rj6A7xogwheWquqP5Icl8EvGHDB2XNIp5PdLD3JmnQfxl9v1h4_8OCpisrzvql6GXuO8BYB-LuMBAg1YFNDK7GWD9gGu07WQBIfsg0Qb2oiIc_Yk5xvAZBExx-zM2qBiHOxYfvLJXnnjZ59DJUOY7W90Umb2Sb_fR1GV-2PKWYfbHV5Y0Ocqt1RZ1u5FA_V1s8pDj8FZWCXMHr_lD1yesr22ames6sP7_fbT_Xuy8fP24tdbVrq55o3zQiDsdJ1ZkTewiBIIBjNyTVDaVs5AKFFib0Aa5zuuZSudKPo5eCac_Zm9b1L8dti86wOPhs7TTrYuGRVDIADlyQK-uof9DYuKZTtCtUj70oaVChcKVPuzck6dZf8QaejQlD3kas1clUiV_eRK1k0L07Oy3Cw42_Fr4wL8PoE6Gz05JIOxuc_nIAOBbSFo5XL5Slc2_TXiv_5_eUqcjoqfZ2K8dXXArUA0FHfNs0Pe-yhFw</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>Chandel, Meenakshi</creator><creator>Azmi, Wamik</creator><general>Springer-Verlag</general><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</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>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>20131201</creationdate><title>Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii</title><author>Chandel, Meenakshi ; Azmi, Wamik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-733d0bce9f5cd1740b82810ca72f3b28149b021e191680ecfa6799f0ecd869bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>Ammonium</topic><topic>ammonium sulfate</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>carbon-carbon lyases</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography</topic><topic>Citrobacter freundii</topic><topic>Citrobacter freundii - enzymology</topic><topic>Dipeptides - chemistry</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hydrophobic bonding</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>phenol</topic><topic>Phenols</topic><topic>polyacrylamide gel electrophoresis</topic><topic>sodium dodecyl sulfate</topic><topic>Sulfates</topic><topic>tyrosine</topic><topic>Tyrosine Phenol-Lyase - chemistry</topic><topic>Tyrosine Phenol-Lyase - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chandel, Meenakshi</creatorcontrib><creatorcontrib>Azmi, Wamik</creatorcontrib><collection>AGRIS</collection><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>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chandel, Meenakshi</au><au>Azmi, Wamik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>171</volume><issue>8</issue><spage>2040</spage><epage>2052</epage><pages>2040-2052</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified tyrosine phenol lyase showed maximum activity in borate buffer (0.05 M at pH 8.5) at 45 °C after 20 min of incubation. The K ₘ and V ₘₐₓ values of purified enzyme were found to be 0.446 mm and 0.342 mM/min/mg. This enzyme exhibits t ₁/₂ of 10, 52 and 130 min at 55, 45 and 35 °C, respectively. The N-terminal amino acid sequence was determined as MET-ASN-TYR-PRO-ALA-GLU-PRO-PHE-ARG-ILE-TRP-TRP-VAL-GLY.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><pmid>24022778</pmid><doi>10.1007/s12010-013-0491-9</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0273-2289 |
| ispartof | Applied biochemistry and biotechnology, 2013-12, Vol.171 (8), p.2040-2052 |
| issn | 0273-2289 1559-0291 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1490707928 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Sequence amino acid sequences Amino acids Ammonium ammonium sulfate Biochemistry Biological and medical sciences Biotechnology carbon-carbon lyases Chemistry Chemistry and Materials Science Chromatography Citrobacter freundii Citrobacter freundii - enzymology Dipeptides - chemistry Enzymes Fundamental and applied biological sciences. Psychology hydrophobic bonding Kinetics Molecular Weight phenol Phenols polyacrylamide gel electrophoresis sodium dodecyl sulfate Sulfates tyrosine Tyrosine Phenol-Lyase - chemistry Tyrosine Phenol-Lyase - isolation & purification |
| title | Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T09%3A51%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Characterization%20of%20Tyrosine%20Phenol%20Lyase%20from%20Citrobacter%20freundii&rft.jtitle=Applied%20biochemistry%20and%20biotechnology&rft.au=Chandel,%20Meenakshi&rft.date=2013-12-01&rft.volume=171&rft.issue=8&rft.spage=2040&rft.epage=2052&rft.pages=2040-2052&rft.issn=0273-2289&rft.eissn=1559-0291&rft.coden=ABIBDL&rft_id=info:doi/10.1007/s12010-013-0491-9&rft_dat=%3Cproquest_cross%3E1490707928%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1461757782&rft_id=info:pmid/24022778&rfr_iscdi=true |