Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions
The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography i...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2000-05, Vol.48 (5), p.1537-1541 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Rodríguez-López, Jose Neptuno Espín, Juan Carlos del Amor, Francisco Tudela, José Martínez, Vicente Cerdá, Antonio García-Cánovas, Francisco |
| description | The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate. Keywords: Melon; peroxidase; salinity; peroxidase isoenzyme; enzyme kinetics. |
| doi_str_mv | 10.1021/jf9905774 |
| format | Article |
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Cultivated under Different Salinity Conditions</title><source>MEDLINE</source><source>ACS Publications</source><creator>Rodríguez-López, Jose Neptuno ; Espín, Juan Carlos ; del Amor, Francisco ; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio ; García-Cánovas, Francisco</creator><creatorcontrib>Rodríguez-López, Jose Neptuno ; Espín, Juan Carlos ; del Amor, Francisco ; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio ; García-Cánovas, Francisco</creatorcontrib><description>The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate. Keywords: Melon; peroxidase; salinity; peroxidase isoenzyme; enzyme kinetics.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf9905774</identifier><identifier>PMID: 10820055</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Agronomy. Soil science and plant productions ; Biological and medical sciences ; Cucurbitaceae - enzymology ; Economic plant physiology ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Kinetics ; Nutrition. Photosynthesis. Respiration. Metabolism ; Peroxidases - isolation & purification ; Peroxidases - metabolism ; Sodium Chloride - chemistry</subject><ispartof>Journal of agricultural and food chemistry, 2000-05, Vol.48 (5), p.1537-1541</ispartof><rights>Copyright © 2000 American Chemical Society</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a378t-887348303364e48d497aa6960b8ce35dabdb9b1aa1dffe5958d002c8da3239a33</citedby><cites>FETCH-LOGICAL-a378t-887348303364e48d497aa6960b8ce35dabdb9b1aa1dffe5958d002c8da3239a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf9905774$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf9905774$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1366119$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10820055$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodríguez-López, Jose Neptuno</creatorcontrib><creatorcontrib>Espín, Juan Carlos</creatorcontrib><creatorcontrib>del Amor, Francisco</creatorcontrib><creatorcontrib>Tudela, José</creatorcontrib><creatorcontrib>Martínez, Vicente</creatorcontrib><creatorcontrib>Cerdá, Antonio</creatorcontrib><creatorcontrib>García-Cánovas, Francisco</creatorcontrib><title>Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate. Keywords: Melon; peroxidase; salinity; peroxidase isoenzyme; enzyme kinetics.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Biological and medical sciences</subject><subject>Cucurbitaceae - enzymology</subject><subject>Economic plant physiology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Nutrition. Photosynthesis. Respiration. Metabolism</subject><subject>Peroxidases - isolation & purification</subject><subject>Peroxidases - metabolism</subject><subject>Sodium Chloride - chemistry</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1u1DAUBWALUdGhsOAFkBeA6CLFjuPEXpbw04pBjDTD2rqxHeEhcYrtoLYPwTPjKqPCoivbOp-urw5CLyg5o6Sk7_a9lIQ3TfUIrSgvScEpFY_RiuSwELymx-hpjHtCiOANeYKOKRElIZyv0J_NHFzvNCQ3eQze4C_O2-Q0bn9AAJ1scLdLOPU5x-c-33O8sWG6dgaixX2YRvzVDtm8bWc9jy7iMT_x-uwUt_OQ3G9I1uDZGxvwB9f3Nlif8BYG5126we3kjbv7Iz5DRz0M0T4_nCfo-6ePu_aiWH_7fNmerwtgjUiFEA2rBCOM1ZWthKlkA1DLmnRCW8YNdKaTHQWgJn_GJRcmd6GFAVYyCYydoDfL3Ksw_ZptTCovre0wgLfTHFVDaSlFTTM8XaAOU4zB9uoquBHCjaJE3ZWv7svP9uVh6NyN1vwnl7YzeHUAEDUMfQCvXfznWF1TKjMrFuZistf3MYSfqm5Yw9Vus1Wt2Aqy27xXF9m_XjzoqPbTHHyu7oH9_gJB5Kf7</recordid><startdate>20000501</startdate><enddate>20000501</enddate><creator>Rodríguez-López, Jose Neptuno</creator><creator>Espín, Juan Carlos</creator><creator>del Amor, Francisco</creator><creator>Tudela, José</creator><creator>Martínez, Vicente</creator><creator>Cerdá, Antonio</creator><creator>García-Cánovas, Francisco</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20000501</creationdate><title>Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions</title><author>Rodríguez-López, Jose Neptuno ; Espín, Juan Carlos ; del Amor, Francisco ; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio ; García-Cánovas, Francisco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a378t-887348303364e48d497aa6960b8ce35dabdb9b1aa1dffe5958d002c8da3239a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Agronomy. Soil science and plant productions</topic><topic>Biological and medical sciences</topic><topic>Cucurbitaceae - enzymology</topic><topic>Economic plant physiology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Nutrition. Photosynthesis. Respiration. Metabolism</topic><topic>Peroxidases - isolation & purification</topic><topic>Peroxidases - metabolism</topic><topic>Sodium Chloride - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodríguez-López, Jose Neptuno</creatorcontrib><creatorcontrib>Espín, Juan Carlos</creatorcontrib><creatorcontrib>del Amor, Francisco</creatorcontrib><creatorcontrib>Tudela, José</creatorcontrib><creatorcontrib>Martínez, Vicente</creatorcontrib><creatorcontrib>Cerdá, Antonio</creatorcontrib><creatorcontrib>García-Cánovas, Francisco</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodríguez-López, Jose Neptuno</au><au>Espín, Juan Carlos</au><au>del Amor, Francisco</au><au>Tudela, José</au><au>Martínez, Vicente</au><au>Cerdá, Antonio</au><au>García-Cánovas, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2000-05-01</date><risdate>2000</risdate><volume>48</volume><issue>5</issue><spage>1537</spage><epage>1541</epage><pages>1537-1541</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The partial characterization of an anionic peroxidase in melon fruit is described. Four melon peroxidase (MPX) isoenzymes were detected in crude extracts after isoelectric focusing. The major MPX isoenzyme (pI = 3.7) was partially purified by including hydrophobic and anion-exchange chromatography in the purification scheme. The sample obtained was used to characterize MPX. This peroxidase did not show activity on ascorbic acid but oxidized guaiacol at a high rate, showing an optimum pH of 5.5 when acting on this last reducing substrate. Melon fruits grown under highly saline conditions showed slightly increased levels of this anionic isoenzyme. Kinetic studies using 2,2‘-azinobis(3-ethylbenzothiazolinesulfonic acid) (ABTS) as reducing substrate showed that increased salinity in the growth medium did not modify the kinetic parameters of melon peroxidase on both hydrogen peroxide and reducing substrate. Keywords: Melon; peroxidase; salinity; peroxidase isoenzyme; enzyme kinetics.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>10820055</pmid><doi>10.1021/jf9905774</doi><tpages>5</tpages></addata></record> |
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| subjects | Agronomy. Soil science and plant productions Biological and medical sciences Cucurbitaceae - enzymology Economic plant physiology Enzymes Fundamental and applied biological sciences. Psychology Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Nutrition. Photosynthesis. Respiration. Metabolism Peroxidases - isolation & purification Peroxidases - metabolism Sodium Chloride - chemistry |
| title | Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions |
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