Characterization of Polyphenol Oxidase from Zyzyphus spina-christi from Iraq

S. Al-Jassabi; Ali Saad; T.R. Satyakeerthy; M.S. Abdullah; (UniKL RCMP)

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dc.contributor.author	S. Al-Jassabi
dc.contributor.author	Ali Saad
dc.contributor.author	T.R. Satyakeerthy
dc.contributor.author	M.S. Abdullah
dc.contributor.author	(UniKL RCMP)
dc.date.accessioned	2014-09-11T04:15:39Z
dc.date.available	2014-09-11T04:15:39Z
dc.date.issued	2013
dc.identifier.issn	Middle-East Journal of Scientific Research
dc.identifier.uri	DOI: 10.5829/idosi.mejsr.2013.14.2.7373
dc.identifier.uri	http://localhost/xmlui/handle/123456789/7752
dc.description	Published 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.pdf	en_US
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	en_US
dc.publisher	IDOSI Publications	en_US
dc.subject	Polyphenol Oxidase	en_US
dc.subject	Zyzyphus Spina Christi	en_US
dc.subject	Catechol	en_US
dc.title	Characterization of Polyphenol Oxidase from Zyzyphus spina-christi from Iraq	en_US