Purification and Biochemical Characterization of Lipase from Ficus carica Latex of Tunisian East Coast Zidi Variety
Lipase from Ficus carica L. (Moraceae) latex of the Zidi variety was purified 80.5-fold with 68.5 % recovery using silica gel chromatography. The molecular weight of the enzyme was 29 kDa as determined by SDS-PAGE. High lipolytic activity was found in the crude extract during the fruit ripening proc...
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| Veröffentlicht in: | Journal of the American Oil Chemists' Society 2012-10, Vol.89 (10), p.1847-1855 |
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| creator | Lazreg-Aref, Houda Mosbah, Habib Fekih, Abdelwaheb Mars, Massoud Said, Khaled |
| description | Lipase from Ficus carica L. (Moraceae) latex of the Zidi variety was purified 80.5-fold with 68.5 % recovery using silica gel chromatography. The molecular weight of the enzyme was 29 kDa as determined by SDS-PAGE. High lipolytic activity was found in the crude extract during the fruit ripening process. The activity of purified lipase (ZL) seemed to depend strongly on chain length and showed a preference to long chain triacylglycerols. Indeed, ZL specific activity was 370.3 UI/mg using olive oil as a substrate at 45 °C and pH 5.5. In contrast, activity towards short chain triacylglycerols (tributyrin) was 12-fold lower (32 UI/mg). The enzyme was quite stable in the pH range 4–8, and thermally stable at 60 °C displaying t 1/2 about 90 min using olive oil as a substrate. The values of K m app and V m were found to be 14.3 mM and 294.1 μmol/min/mg, respectively. ZL activity was strongly reduced by Fe2+, Mg2+ and Zn2+, while significantly increased by Ca2+ and Cu2+. The enzyme was stimulated by sodium dodecyl sulfate, and Tween-80, while Triton X-100 and EDTA had a slight inhibitory effect. No Effect was observed in addition of PMSF and iodoacetic acid. |
| doi_str_mv | 10.1007/s11746-012-2095-x |
| format | Article |
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(Moraceae) latex of the Zidi variety was purified 80.5-fold with 68.5 % recovery using silica gel chromatography. The molecular weight of the enzyme was 29 kDa as determined by SDS-PAGE. High lipolytic activity was found in the crude extract during the fruit ripening process. The activity of purified lipase (ZL) seemed to depend strongly on chain length and showed a preference to long chain triacylglycerols. Indeed, ZL specific activity was 370.3 UI/mg using olive oil as a substrate at 45 °C and pH 5.5. In contrast, activity towards short chain triacylglycerols (tributyrin) was 12-fold lower (32 UI/mg). The enzyme was quite stable in the pH range 4–8, and thermally stable at 60 °C displaying t 1/2 about 90 min using olive oil as a substrate. The values of K m app and V m were found to be 14.3 mM and 294.1 μmol/min/mg, respectively. ZL activity was strongly reduced by Fe2+, Mg2+ and Zn2+, while significantly increased by Ca2+ and Cu2+. The enzyme was stimulated by sodium dodecyl sulfate, and Tween-80, while Triton X-100 and EDTA had a slight inhibitory effect. No Effect was observed in addition of PMSF and iodoacetic acid.</description><identifier>ISSN: 0003-021X</identifier><identifier>EISSN: 1558-9331</identifier><identifier>DOI: 10.1007/s11746-012-2095-x</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Agriculture ; Biochemistry ; Biological and medical sciences ; Biomaterials ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; EDTA (chelating agent) ; Fat industries ; Ficus carica ; Food industries ; Food Science ; Fundamental and applied biological sciences. Psychology ; Industrial Chemistry/Chemical Engineering ; iodoacetic acid ; Kinetics ; Latex ; Lipids ; long chain triacylglycerols ; magnesium ; Metal ions ; molecular weight ; Olive oil ; Original Paper ; Plant lipase ; polyacrylamide gel electrophoresis ; ripening ; SDS‐PAGE ; short chain triacylglycerols ; Silica ; silica gel ; sodium dodecyl sulfate ; Substrate specificity ; Substrates ; Surfactants ; triacylglycerol lipase ; zinc</subject><ispartof>Journal of the American Oil Chemists' Society, 2012-10, Vol.89 (10), p.1847-1855</ispartof><rights>AOCS 2012</rights><rights>2012 American Oil Chemists' Society (AOCS)</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4427-c61f2afce56eeb1eb6ef8c06588aaf39bf65a8cbd67598523fc1f804088e92d53</citedby><cites>FETCH-LOGICAL-c4427-c61f2afce56eeb1eb6ef8c06588aaf39bf65a8cbd67598523fc1f804088e92d53</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/s11746-012-2095-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11746-012-2095-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,1414,27911,27912,41475,42544,45561,45562,51306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26437102$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Lazreg-Aref, Houda</creatorcontrib><creatorcontrib>Mosbah, Habib</creatorcontrib><creatorcontrib>Fekih, Abdelwaheb</creatorcontrib><creatorcontrib>Mars, Massoud</creatorcontrib><creatorcontrib>Said, Khaled</creatorcontrib><title>Purification and Biochemical Characterization of Lipase from Ficus carica Latex of Tunisian East Coast Zidi Variety</title><title>Journal of the American Oil Chemists' Society</title><addtitle>J Am Oil Chem Soc</addtitle><description>Lipase from Ficus carica L. (Moraceae) latex of the Zidi variety was purified 80.5-fold with 68.5 % recovery using silica gel chromatography. The molecular weight of the enzyme was 29 kDa as determined by SDS-PAGE. High lipolytic activity was found in the crude extract during the fruit ripening process. The activity of purified lipase (ZL) seemed to depend strongly on chain length and showed a preference to long chain triacylglycerols. Indeed, ZL specific activity was 370.3 UI/mg using olive oil as a substrate at 45 °C and pH 5.5. In contrast, activity towards short chain triacylglycerols (tributyrin) was 12-fold lower (32 UI/mg). The enzyme was quite stable in the pH range 4–8, and thermally stable at 60 °C displaying t 1/2 about 90 min using olive oil as a substrate. The values of K m app and V m were found to be 14.3 mM and 294.1 μmol/min/mg, respectively. ZL activity was strongly reduced by Fe2+, Mg2+ and Zn2+, while significantly increased by Ca2+ and Cu2+. The enzyme was stimulated by sodium dodecyl sulfate, and Tween-80, while Triton X-100 and EDTA had a slight inhibitory effect. No Effect was observed in addition of PMSF and iodoacetic acid.</description><subject>Agriculture</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomaterials</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>EDTA (chelating agent)</subject><subject>Fat industries</subject><subject>Ficus carica</subject><subject>Food industries</subject><subject>Food Science</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Industrial Chemistry/Chemical Engineering</topic><topic>iodoacetic acid</topic><topic>Kinetics</topic><topic>Latex</topic><topic>Lipids</topic><topic>long chain triacylglycerols</topic><topic>magnesium</topic><topic>Metal ions</topic><topic>molecular weight</topic><topic>Olive oil</topic><topic>Original Paper</topic><topic>Plant lipase</topic><topic>polyacrylamide gel electrophoresis</topic><topic>ripening</topic><topic>SDS‐PAGE</topic><topic>short chain triacylglycerols</topic><topic>Silica</topic><topic>silica gel</topic><topic>sodium dodecyl sulfate</topic><topic>Substrate specificity</topic><topic>Substrates</topic><topic>Surfactants</topic><topic>triacylglycerol lipase</topic><topic>zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lazreg-Aref, Houda</creatorcontrib><creatorcontrib>Mosbah, Habib</creatorcontrib><creatorcontrib>Fekih, Abdelwaheb</creatorcontrib><creatorcontrib>Mars, Massoud</creatorcontrib><creatorcontrib>Said, Khaled</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Research Library (Corporate)</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</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><jtitle>Journal of the American Oil Chemists' Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lazreg-Aref, Houda</au><au>Mosbah, Habib</au><au>Fekih, Abdelwaheb</au><au>Mars, Massoud</au><au>Said, Khaled</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Biochemical Characterization of Lipase from Ficus carica Latex of Tunisian East Coast Zidi Variety</atitle><jtitle>Journal of the American Oil Chemists' Society</jtitle><stitle>J Am Oil Chem Soc</stitle><date>2012-10</date><risdate>2012</risdate><volume>89</volume><issue>10</issue><spage>1847</spage><epage>1855</epage><pages>1847-1855</pages><issn>0003-021X</issn><eissn>1558-9331</eissn><abstract>Lipase from Ficus carica L. (Moraceae) latex of the Zidi variety was purified 80.5-fold with 68.5 % recovery using silica gel chromatography. The molecular weight of the enzyme was 29 kDa as determined by SDS-PAGE. High lipolytic activity was found in the crude extract during the fruit ripening process. The activity of purified lipase (ZL) seemed to depend strongly on chain length and showed a preference to long chain triacylglycerols. Indeed, ZL specific activity was 370.3 UI/mg using olive oil as a substrate at 45 °C and pH 5.5. In contrast, activity towards short chain triacylglycerols (tributyrin) was 12-fold lower (32 UI/mg). The enzyme was quite stable in the pH range 4–8, and thermally stable at 60 °C displaying t 1/2 about 90 min using olive oil as a substrate. The values of K m app and V m were found to be 14.3 mM and 294.1 μmol/min/mg, respectively. ZL activity was strongly reduced by Fe2+, Mg2+ and Zn2+, while significantly increased by Ca2+ and Cu2+. The enzyme was stimulated by sodium dodecyl sulfate, and Tween-80, while Triton X-100 and EDTA had a slight inhibitory effect. No Effect was observed in addition of PMSF and iodoacetic acid.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><doi>10.1007/s11746-012-2095-x</doi><tpages>9</tpages></addata></record> |
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| subjects | Agriculture Biochemistry Biological and medical sciences Biomaterials Biotechnology Chemistry Chemistry and Materials Science EDTA (chelating agent) Fat industries Ficus carica Food industries Food Science Fundamental and applied biological sciences. Psychology Industrial Chemistry/Chemical Engineering iodoacetic acid Kinetics Latex Lipids long chain triacylglycerols magnesium Metal ions molecular weight Olive oil Original Paper Plant lipase polyacrylamide gel electrophoresis ripening SDS‐PAGE short chain triacylglycerols Silica silica gel sodium dodecyl sulfate Substrate specificity Substrates Surfactants triacylglycerol lipase zinc |
| title | Purification and Biochemical Characterization of Lipase from Ficus carica Latex of Tunisian East Coast Zidi Variety |
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