Please use this identifier to cite or link to this item: http://148.72.244.84/xmlui/handle/xmlui/12593
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dc.contributor.authorIkbaal M.Salmaan-
dc.date.accessioned2024-03-14T06:26:37Z-
dc.date.available2024-03-14T06:26:37Z-
dc.date.issued2010-
dc.identifier.issn2222-8373-
dc.identifier.urihttp://148.72.244.84:8080/xmlui/handle/xmlui/12593-
dc.description.abstractErwinia carotovora (7) isolates were obtained out of 20 spoilt potato samples from local market of Baquba city .The isolates that gave higher Pectinolytic activity was selected to purify pectin lyase through three stages of purification including (ethanol precipitation, ion- exchange chromatography by DEAE – Sepharose and gel filtration by Sephadex G50 with 63.9- fold purification , 69.5U / mg specific activity and 30% recovery.The purified enzyme was characterized :the molecular weight was about 29 KDa by gel filtration chromatography .The temperature for maximum activity was 60c° and maximal activity was observed at pH 8.5 .Some metallic ions such as Ca+ and Mg+2 increased Pectin lyase activity to 140 and 133 % respectively .while the other metals such as Co+2 ,Hg+2 ,Ni+2 Zn+2and Sn+2 inhabited enzyme activity.Therefor ,This research leads to increase interest by using Pectin lyase in the current biotechnological application .en_US
dc.language.isoenen_US
dc.publisherUniversity of Diyalaen_US
dc.titlePurification and characterization of extra cellular Pectin lyase from Erwinia carotovora isolate from spoilt potatoesen_US
dc.typeArticleen_US
Appears in Collections:مجلة ديالى للعلوم الاكاديمية / Academic Science Journal (Acad. Sci. J.)

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