Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/7752
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dc.contributor.authorS. Al-Jassabi-
dc.contributor.authorAli Saad-
dc.contributor.authorT.R. Satyakeerthy-
dc.contributor.authorM.S. Abdullah-
dc.contributor.author(UniKL RCMP)-
dc.date.accessioned2014-09-11T04:15:39Z-
dc.date.available2014-09-11T04:15:39Z-
dc.date.issued2013-
dc.identifier.issnMiddle-East Journal of Scientific Research-
dc.identifier.uriDOI: 10.5829/idosi.mejsr.2013.14.2.7373-
dc.identifier.urihttp://localhost/xmlui/handle/123456789/7752-
dc.descriptionPublished in Middle-East Journal of Scientific Research 14 (2): 155-160, 2013. Full text also available at http://www.idosi.org/mejsr/mejsr14%282%2913/2.pdfen_US
dc.description.abstractPolyphenol oxidase (PPO) from Zyzyphus spina christi found in central part of Iraq was extracted and purified by (NH ) SO precipitation, ion-exchange chromatography and gel filtration chromatography. 42 4 The biochemical characteristics reveal that the PPO from Zyzyphus spina christi has higher affinity towards catechol ( K = 11.4mM and V = 16,400 U/ml min ) at an optimum pH of 5.8. The enzyme had an optimum M max 1 temperature of 37°C and was relatively stable up to 50°C for a period of 60 minutes with almost 80% activity remaining. Among the various PPO inhibitors tested, the most effective inhibitor for the enzyme with 10mM catechol as substrate was ascorbic aciden_US
dc.publisherIDOSI Publicationsen_US
dc.subjectPolyphenol Oxidaseen_US
dc.subjectZyzyphus Spina Christien_US
dc.subjectCatecholen_US
dc.titleCharacterization of Polyphenol Oxidase from Zyzyphus spina-christi from Iraqen_US
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