Selected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis l

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dc.contributor.authorAydemir T.
dc.date.accessioned2024-07-22T08:21:00Z
dc.date.available2024-07-22T08:21:00Z
dc.date.issued2010
dc.description.abstractPolyphenol oxidase from Rosmarinus officinalis L. (PPO, EC 1:14:18.1) was extracted and partially purified by using (NH4)2SO 4 precipitation and dialysis. Stable and highly active PPO extracts were obtained using 0.5% (w/v) PEG and 0.5% (w/v) Triton X-100 in 0.1 M phosphate buffer 7.0. KM values were found to be as 14.3 mM for catechol. Four isoenzymes of Rosemary PPO were detected by PAGE with DL-dopa substrate. The enzyme was strongly inhibited by dithiotreitol, sodium metasulfite, sodium thiosulfate, ascorbic acid, and L-cysteine. Metal ions Ca++, Mg++, and Mn++ were poor inhibitors of rosemary PPO at 10 Mm. Copyright © Taylor & Francis Group, LLC.
dc.identifier.DOI-ID10.1080/10942910802641993
dc.identifier.issn15322386
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/18420
dc.language.isoEnglish
dc.subjectRosmarinus officinalis
dc.subjectCalcium
dc.subjectDialysis
dc.subjectKetones
dc.subjectManganese
dc.subjectManganese compounds
dc.subjectMetal ions
dc.subjectMetal refining
dc.subjectOrganic acids
dc.subjectPhenols
dc.subjectPolyethylene glycols
dc.subjectSmelting
dc.subjectAscorbic acids
dc.subjectHeat inactivation
dc.subjectKinetic properties
dc.subjectL-cysteine
dc.subjectPH stability
dc.subjectPhosphate buffers
dc.subjectPolyphenol oxidase
dc.subjectPoor inhibitors
dc.subjectRosmarinus officinalis
dc.subjectSodium thiosulfate
dc.subjectTriton X-100
dc.subjectpH effects
dc.titleSelected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis l
dc.typeArticle

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