Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase
We have isolated a lipolytic halotolerant bacterium, designated as CJ3, that was identified as a Staphylococcus sp. Culture conditions were optimized and the highest extracellular lipase production amounting to 5U/ml was achieved after 24h of cultivation. The extracellular lipase was purified 24-fold...
Gespeichert in:
| Veröffentlicht in: | International journal of biological macromolecules 2013-06, Vol.57, p.232-237 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 237 |
|---|---|
| container_issue | |
| container_start_page | 232 |
| container_title | International journal of biological macromolecules |
| container_volume | 57 |
| creator | Daoud, Lobna Kamoun, Jannet Ali, Madiha Bou Jallouli, Raida Bradai, Rim Mechichi, Tahar Gargouri, Youssef Ali, Yassine Ben Aloulou, Ahmed |
| description | We have isolated a lipolytic halotolerant bacterium, designated as CJ3, that was identified as a Staphylococcus sp. Culture conditions were optimized and the highest extracellular lipase production amounting to 5U/ml was achieved after 24h of cultivation. The extracellular lipase was purified 24-fold by ammonium sulfate precipitation and a Sephacryl S-200 chromatography, and its molecular mass was found to be around 38kDa, as revealed by SDS-PAGE and gel filtration. The lipase substrate specificity was investigated using short (tributyrin) and long (olive oil) chain triglyceride substrates. The lipase was inhibited by submicellar concentrations of Triton X-100, and maximum specific activities were found to be 802U/mg on tributyrin and 260U/mg on olive oil at pH 8.0 and 45°C. The lipase was fairly stable in the pH range from 6.0 to 9.0, and about 69% of its activity was retained after incubation at 45°C for 60min. The enzyme showed a high tolerance to a wide range of salt concentration and a good stability in organic solvents, especially in long-chain alcohols. |
| doi_str_mv | 10.1016/j.ijbiomac.2013.03.018 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1505349915</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0141813013001013</els_id><sourcerecordid>1505349915</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425t-9c1c1a1dbfffb65fe2b59782b8cee06979d7e8b809f888dc68fce1fcd44fa4c33</originalsourceid><addsrcrecordid>eNqFkU9r3DAQxUVpabZpv0LqYy92NbbllW4toX8CgRbSnIU8HmW12JYryaXpp68WJ7kGBgaG33szzGPsAngFHLqPx8ode-cng1XNoal4LpAv2A7kXpWc8-Yl23FooZTQ8DP2JsZjnnYC5Gt2VjeC87aRO3b3cw3OOjTJ-bkw81BkVzzQlEdjgQcTDCYK7t8GeFuY4mBGn_xIwcypuElmOdyPHj3iGou4VAX9TVlF47iOJhSjW0ykt-yVNWOkdw_9nN1-_fLr8nt5_ePb1eXn6xLbWqRSISAYGHprbd8JS3Uv1F7WvUQi3qm9GvYke8mVlVIO2EmLBBaHtrWmxaY5Zx823yX43yvFpCcXT7eYmfwaNQgumlYpEM-jTSsE1FKpjHYbisHHGMjqJbjJhHsNXJ_y0Ef9mIc-5aF5LpBZePGwY-0nGp5kjwFk4P0GWOO1uQsu6tub7NDlsISq6zYTnzaC8tv-OAo6oqMZaXCBMOnBu-eu-A8fTatE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1345512899</pqid></control><display><type>article</type><title>Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Daoud, Lobna ; Kamoun, Jannet ; Ali, Madiha Bou ; Jallouli, Raida ; Bradai, Rim ; Mechichi, Tahar ; Gargouri, Youssef ; Ali, Yassine Ben ; Aloulou, Ahmed</creator><creatorcontrib>Daoud, Lobna ; Kamoun, Jannet ; Ali, Madiha Bou ; Jallouli, Raida ; Bradai, Rim ; Mechichi, Tahar ; Gargouri, Youssef ; Ali, Yassine Ben ; Aloulou, Ahmed</creatorcontrib><description>We have isolated a lipolytic halotolerant bacterium, designated as CJ3, that was identified as a Staphylococcus sp. Culture conditions were optimized and the highest extracellular lipase production amounting to 5U/ml was achieved after 24h of cultivation. The extracellular lipase was purified 24-fold by ammonium sulfate precipitation and a Sephacryl S-200 chromatography, and its molecular mass was found to be around 38kDa, as revealed by SDS-PAGE and gel filtration. The lipase substrate specificity was investigated using short (tributyrin) and long (olive oil) chain triglyceride substrates. The lipase was inhibited by submicellar concentrations of Triton X-100, and maximum specific activities were found to be 802U/mg on tributyrin and 260U/mg on olive oil at pH 8.0 and 45°C. The lipase was fairly stable in the pH range from 6.0 to 9.0, and about 69% of its activity was retained after incubation at 45°C for 60min. The enzyme showed a high tolerance to a wide range of salt concentration and a good stability in organic solvents, especially in long-chain alcohols.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2013.03.018</identifier><identifier>PMID: 23500438</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>ammonium sulfate ; bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - isolation & purification ; Characterization ; Chromatography, Gel ; gel chromatography ; Halotolerance ; Lipase ; Lipase - chemistry ; Lipase - isolation & purification ; Molecular Weight ; octoxynol ; Olea ; olive oil ; polyacrylamide gel electrophoresis ; Production ; Purification ; salt concentration ; salt tolerance ; solvents ; Staphylococcus ; Staphylococcus - enzymology ; substrate specificity ; Substrate Specificity - physiology ; triacylglycerols ; tributyrin ; Triglycerides - chemistry</subject><ispartof>International journal of biological macromolecules, 2013-06, Vol.57, p.232-237</ispartof><rights>2013 Elsevier B.V.</rights><rights>Copyright © 2013 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-9c1c1a1dbfffb65fe2b59782b8cee06979d7e8b809f888dc68fce1fcd44fa4c33</citedby><cites>FETCH-LOGICAL-c425t-9c1c1a1dbfffb65fe2b59782b8cee06979d7e8b809f888dc68fce1fcd44fa4c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141813013001013$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23500438$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Daoud, Lobna</creatorcontrib><creatorcontrib>Kamoun, Jannet</creatorcontrib><creatorcontrib>Ali, Madiha Bou</creatorcontrib><creatorcontrib>Jallouli, Raida</creatorcontrib><creatorcontrib>Bradai, Rim</creatorcontrib><creatorcontrib>Mechichi, Tahar</creatorcontrib><creatorcontrib>Gargouri, Youssef</creatorcontrib><creatorcontrib>Ali, Yassine Ben</creatorcontrib><creatorcontrib>Aloulou, Ahmed</creatorcontrib><title>Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>We have isolated a lipolytic halotolerant bacterium, designated as CJ3, that was identified as a Staphylococcus sp. Culture conditions were optimized and the highest extracellular lipase production amounting to 5U/ml was achieved after 24h of cultivation. The extracellular lipase was purified 24-fold by ammonium sulfate precipitation and a Sephacryl S-200 chromatography, and its molecular mass was found to be around 38kDa, as revealed by SDS-PAGE and gel filtration. The lipase substrate specificity was investigated using short (tributyrin) and long (olive oil) chain triglyceride substrates. The lipase was inhibited by submicellar concentrations of Triton X-100, and maximum specific activities were found to be 802U/mg on tributyrin and 260U/mg on olive oil at pH 8.0 and 45°C. The lipase was fairly stable in the pH range from 6.0 to 9.0, and about 69% of its activity was retained after incubation at 45°C for 60min. The enzyme showed a high tolerance to a wide range of salt concentration and a good stability in organic solvents, especially in long-chain alcohols.</description><subject>ammonium sulfate</subject><subject>bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Characterization</subject><subject>Chromatography, Gel</subject><subject>gel chromatography</subject><subject>Halotolerance</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - isolation & purification</subject><subject>Molecular Weight</subject><subject>octoxynol</subject><subject>Olea</subject><subject>olive oil</subject><subject>polyacrylamide gel electrophoresis</subject><subject>Production</subject><subject>Purification</subject><subject>salt concentration</subject><subject>salt tolerance</subject><subject>solvents</subject><subject>Staphylococcus</subject><subject>Staphylococcus - enzymology</subject><subject>substrate specificity</subject><subject>Substrate Specificity - physiology</subject><subject>triacylglycerols</subject><subject>tributyrin</subject><subject>Triglycerides - chemistry</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r3DAQxUVpabZpv0LqYy92NbbllW4toX8CgRbSnIU8HmW12JYryaXpp68WJ7kGBgaG33szzGPsAngFHLqPx8ode-cng1XNoal4LpAv2A7kXpWc8-Yl23FooZTQ8DP2JsZjnnYC5Gt2VjeC87aRO3b3cw3OOjTJ-bkw81BkVzzQlEdjgQcTDCYK7t8GeFuY4mBGn_xIwcypuElmOdyPHj3iGou4VAX9TVlF47iOJhSjW0ykt-yVNWOkdw_9nN1-_fLr8nt5_ePb1eXn6xLbWqRSISAYGHprbd8JS3Uv1F7WvUQi3qm9GvYke8mVlVIO2EmLBBaHtrWmxaY5Zx823yX43yvFpCcXT7eYmfwaNQgumlYpEM-jTSsE1FKpjHYbisHHGMjqJbjJhHsNXJ_y0Ef9mIc-5aF5LpBZePGwY-0nGp5kjwFk4P0GWOO1uQsu6tub7NDlsISq6zYTnzaC8tv-OAo6oqMZaXCBMOnBu-eu-A8fTatE</recordid><startdate>20130601</startdate><enddate>20130601</enddate><creator>Daoud, Lobna</creator><creator>Kamoun, Jannet</creator><creator>Ali, Madiha Bou</creator><creator>Jallouli, Raida</creator><creator>Bradai, Rim</creator><creator>Mechichi, Tahar</creator><creator>Gargouri, Youssef</creator><creator>Ali, Yassine Ben</creator><creator>Aloulou, Ahmed</creator><general>Elsevier B.V</general><scope>FBQ</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>7X8</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20130601</creationdate><title>Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase</title><author>Daoud, Lobna ; Kamoun, Jannet ; Ali, Madiha Bou ; Jallouli, Raida ; Bradai, Rim ; Mechichi, Tahar ; Gargouri, Youssef ; Ali, Yassine Ben ; Aloulou, Ahmed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-9c1c1a1dbfffb65fe2b59782b8cee06979d7e8b809f888dc68fce1fcd44fa4c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>ammonium sulfate</topic><topic>bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Characterization</topic><topic>Chromatography, Gel</topic><topic>gel chromatography</topic><topic>Halotolerance</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Lipase - isolation & purification</topic><topic>Molecular Weight</topic><topic>octoxynol</topic><topic>Olea</topic><topic>olive oil</topic><topic>polyacrylamide gel electrophoresis</topic><topic>Production</topic><topic>Purification</topic><topic>salt concentration</topic><topic>salt tolerance</topic><topic>solvents</topic><topic>Staphylococcus</topic><topic>Staphylococcus - enzymology</topic><topic>substrate specificity</topic><topic>Substrate Specificity - physiology</topic><topic>triacylglycerols</topic><topic>tributyrin</topic><topic>Triglycerides - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Daoud, Lobna</creatorcontrib><creatorcontrib>Kamoun, Jannet</creatorcontrib><creatorcontrib>Ali, Madiha Bou</creatorcontrib><creatorcontrib>Jallouli, Raida</creatorcontrib><creatorcontrib>Bradai, Rim</creatorcontrib><creatorcontrib>Mechichi, Tahar</creatorcontrib><creatorcontrib>Gargouri, Youssef</creatorcontrib><creatorcontrib>Ali, Yassine Ben</creatorcontrib><creatorcontrib>Aloulou, Ahmed</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Daoud, Lobna</au><au>Kamoun, Jannet</au><au>Ali, Madiha Bou</au><au>Jallouli, Raida</au><au>Bradai, Rim</au><au>Mechichi, Tahar</au><au>Gargouri, Youssef</au><au>Ali, Yassine Ben</au><au>Aloulou, Ahmed</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2013-06-01</date><risdate>2013</risdate><volume>57</volume><spage>232</spage><epage>237</epage><pages>232-237</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>We have isolated a lipolytic halotolerant bacterium, designated as CJ3, that was identified as a Staphylococcus sp. Culture conditions were optimized and the highest extracellular lipase production amounting to 5U/ml was achieved after 24h of cultivation. The extracellular lipase was purified 24-fold by ammonium sulfate precipitation and a Sephacryl S-200 chromatography, and its molecular mass was found to be around 38kDa, as revealed by SDS-PAGE and gel filtration. The lipase substrate specificity was investigated using short (tributyrin) and long (olive oil) chain triglyceride substrates. The lipase was inhibited by submicellar concentrations of Triton X-100, and maximum specific activities were found to be 802U/mg on tributyrin and 260U/mg on olive oil at pH 8.0 and 45°C. The lipase was fairly stable in the pH range from 6.0 to 9.0, and about 69% of its activity was retained after incubation at 45°C for 60min. The enzyme showed a high tolerance to a wide range of salt concentration and a good stability in organic solvents, especially in long-chain alcohols.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>23500438</pmid><doi>10.1016/j.ijbiomac.2013.03.018</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-8130 |
| ispartof | International journal of biological macromolecules, 2013-06, Vol.57, p.232-237 |
| issn | 0141-8130 1879-0003 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1505349915 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | ammonium sulfate bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Characterization Chromatography, Gel gel chromatography Halotolerance Lipase Lipase - chemistry Lipase - isolation & purification Molecular Weight octoxynol Olea olive oil polyacrylamide gel electrophoresis Production Purification salt concentration salt tolerance solvents Staphylococcus Staphylococcus - enzymology substrate specificity Substrate Specificity - physiology triacylglycerols tributyrin Triglycerides - chemistry |
| title | Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T06%3A05%3A35IST&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%20biochemical%20characterization%20of%20a%20halotolerant%20Staphylococcus%20sp.%20extracellular%20lipase&rft.jtitle=International%20journal%20of%20biological%20macromolecules&rft.au=Daoud,%20Lobna&rft.date=2013-06-01&rft.volume=57&rft.spage=232&rft.epage=237&rft.pages=232-237&rft.issn=0141-8130&rft.eissn=1879-0003&rft_id=info:doi/10.1016/j.ijbiomac.2013.03.018&rft_dat=%3Cproquest_cross%3E1505349915%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=1345512899&rft_id=info:pmid/23500438&rft_els_id=S0141813013001013&rfr_iscdi=true |