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metadata.conference.dc.title: Characterization of Polyphenol Oxidase from Zyzyphus spina-christi from Iraq
metadata.conference.dc.contributor.*: S. Al-Jassabi
Ali Saad
T.R. Satyakeerthy
M.S. Abdullah
metadata.conference.dc.subject: Polyphenol Oxidase
Zyzyphus Spina Christi
Catechol 2013
metadata.conference.dc.publisher: IDOSI Publications
metadata.conference.dc.description.abstract: Polyphenol 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 acid
metadata.conference.dc.description: Published in Middle-East Journal of Scientific Research 14 (2): 155-160, 2013. Full text also available at
metadata.conference.dc.identifier.uri: DOI: 10.5829/idosi.mejsr.2013.14.2.7373
metadata.conference.dc.identifier.issn: Middle-East Journal of Scientific Research
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