Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)
The enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion-exchange chromatography (Q Sepharose) and filtration on Sephadex G-100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific a...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2007-08, Vol.87 (10), p.1845-1849 |
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| creator | Assis, S.A. de Martins, A.B.G Oliveira, O.M.M. de F |
| description | The enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion-exchange chromatography (Q Sepharose) and filtration on Sephadex G-100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific activity increased by 9.63% after 60 min incubation at 98 °C, while PME2 retained 66% of its specific activity under the same conditions. The K(m) values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL(-1), respectively. The V(max) value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 μmol min(-1) mg(-1) protein, respectively. |
| doi_str_mv | 10.1002/jsfa.2884 |
| format | Article |
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The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific activity increased by 9.63% after 60 min incubation at 98 °C, while PME2 retained 66% of its specific activity under the same conditions. The K(m) values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL(-1), respectively. The V(max) value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 μmol min(-1) mg(-1) protein, respectively.</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.2884</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>acerola ; Biochemistry ; Biological and medical sciences ; Chromatography ; enzyme activity ; enzyme kinetics ; Enzymes ; Food industries ; Food science ; Fruits ; Fundamental and applied biological sciences. Psychology ; heat stability ; isoenzymes ; isozymes ; kinetic characterization ; Malpighia glabra ; molecular weight ; pectinesterase ; pectinmethylesterase ; purification ; temperature ; tropical and subtropical fruits</subject><ispartof>Journal of the science of food and agriculture, 2007-08, Vol.87 (10), p.1845-1849</ispartof><rights>Copyright © 2007 Society of Chemical Industry</rights><rights>2007 INIST-CNRS</rights><rights>Copyright John Wiley and Sons, Limited Aug 15, 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4194-3bb2d681e10fb7ab103ca0832300d4642befd876ae098923510ccc223903e7bd3</citedby><cites>FETCH-LOGICAL-c4194-3bb2d681e10fb7ab103ca0832300d4642befd876ae098923510ccc223903e7bd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.2884$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.2884$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18897301$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Assis, S.A. de</creatorcontrib><creatorcontrib>Martins, A.B.G</creatorcontrib><creatorcontrib>Oliveira, O.M.M. de F</creatorcontrib><title>Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>The enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion-exchange chromatography (Q Sepharose) and filtration on Sephadex G-100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific activity increased by 9.63% after 60 min incubation at 98 °C, while PME2 retained 66% of its specific activity under the same conditions. The K(m) values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL(-1), respectively. The V(max) value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 μmol min(-1) mg(-1) protein, respectively.</description><subject>acerola</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>enzyme activity</subject><subject>enzyme kinetics</subject><subject>Enzymes</subject><subject>Food industries</subject><subject>Food science</subject><subject>Fruits</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>heat stability</subject><subject>isoenzymes</subject><subject>isozymes</subject><subject>kinetic characterization</subject><subject>Malpighia glabra</subject><subject>molecular weight</subject><subject>pectinesterase</subject><subject>pectinmethylesterase</subject><subject>purification</subject><subject>temperature</subject><subject>tropical and subtropical fruits</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp1kEFvEzEQhVcIJELLgV-AhUTVHjYd25td-1hFNKHalqJScULWrNdOHJzdYCcq4dfjaCOQkDiNNPO9N08vy95QGFMAdrmKFsdMiOJZNqIgqxyAwvNslG4sn9CCvcxexbgCACnLcpR9u98FZ53Gres7gl1L9BID6q0J7tew7C3ZGL11HVmb7XLvTUxHjIbY0K8JahN6j-T8Fv3GLZYOycJjE5DU44vT7IVFH83r4zzJHq8_fJnO8_rT7OP0qs51QWWR86ZhbSmooWCbChsKXCMIzjhAW5QFa4xtRVWiASkk4xMKWmvGuARuqqblJ9nZ4LsJ_Y9dCqjWLmrjPXam30XFpJSTquQJfPcPuOp3oUvZFGOsogw4TdDFAOnQxxiMVZvg1hj2ioI6tKwOLatDy4l9fzTEqNHbgJ128a9ACFlxOHheDtyT82b_f0N183B9dXTOB4VLff_8o8DwXZUVrybq691Mze7r6Xw6_6zqxL8deIu9wkVIKR4fWHoNIBgXqdPfy2yjZg</recordid><startdate>20070815</startdate><enddate>20070815</enddate><creator>Assis, S.A. de</creator><creator>Martins, A.B.G</creator><creator>Oliveira, O.M.M. de F</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><general>John Wiley and Sons, Limited</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope></search><sort><creationdate>20070815</creationdate><title>Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)</title><author>Assis, S.A. de ; Martins, A.B.G ; Oliveira, O.M.M. de F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4194-3bb2d681e10fb7ab103ca0832300d4642befd876ae098923510ccc223903e7bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>acerola</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography</topic><topic>enzyme activity</topic><topic>enzyme kinetics</topic><topic>Enzymes</topic><topic>Food industries</topic><topic>Food science</topic><topic>Fruits</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>heat stability</topic><topic>isoenzymes</topic><topic>isozymes</topic><topic>kinetic characterization</topic><topic>Malpighia glabra</topic><topic>molecular weight</topic><topic>pectinesterase</topic><topic>pectinmethylesterase</topic><topic>purification</topic><topic>temperature</topic><topic>tropical and subtropical fruits</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Assis, S.A. de</creatorcontrib><creatorcontrib>Martins, A.B.G</creatorcontrib><creatorcontrib>Oliveira, O.M.M. de F</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Assis, S.A. de</au><au>Martins, A.B.G</au><au>Oliveira, O.M.M. de F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>2007-08-15</date><risdate>2007</risdate><volume>87</volume><issue>10</issue><spage>1845</spage><epage>1849</epage><pages>1845-1849</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>The enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion-exchange chromatography (Q Sepharose) and filtration on Sephadex G-100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific activity increased by 9.63% after 60 min incubation at 98 °C, while PME2 retained 66% of its specific activity under the same conditions. The K(m) values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL(-1), respectively. The V(max) value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 μmol min(-1) mg(-1) protein, respectively.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><doi>10.1002/jsfa.2884</doi><tpages>5</tpages></addata></record> |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | acerola Biochemistry Biological and medical sciences Chromatography enzyme activity enzyme kinetics Enzymes Food industries Food science Fruits Fundamental and applied biological sciences. Psychology heat stability isoenzymes isozymes kinetic characterization Malpighia glabra molecular weight pectinesterase pectinmethylesterase purification temperature tropical and subtropical fruits |
| title | Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.) |
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