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http://hdl.handle.net/123456789/7752
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DC Field | Value | Language |
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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 |
Appears in Collections: | Journal Articles |
Files in This Item:
File | Description | Size | Format | |
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Characterisation of Polyphenol Oxidase from Zyzyphus Spina-Christi from Iraq.pdf | 256.35 kB | Adobe PDF | View/Open |
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