Publication:
Meta-cleavage pathway of phenol degradation by Acinetobacter sp. strain AQ5NOL 1

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dc.citedby7
dc.contributor.affiliationsFaculty of Medicine and Health Sciences
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.affiliationsUniversiti Kebangsaan Malaysia (UKM)
dc.contributor.affiliationsKompleks Pengajian Kejuruteraan Jejawi 3
dc.contributor.affiliationsUniversiti Teknologi MARA (UiTM)
dc.contributor.authorAhmad S.A.en_US
dc.contributor.authorShamaan N.A.en_US
dc.contributor.authorSyed M.A.en_US
dc.contributor.authorKhalid A.en_US
dc.contributor.authorAb Rahman N.A.en_US
dc.contributor.authorKhalil K.A.en_US
dc.contributor.authorDahalan F.A.en_US
dc.contributor.authorShukor M.Y.en_US
dc.date.accessioned2024-05-28T08:35:50Z
dc.date.available2024-05-28T08:35:50Z
dc.date.issued2017
dc.description.abstractThe characterization of bacterial enzymatic pathways of phenol metabolism is important to better understand phenol biodegradation. Phenol hydroxylase is the first enzyme involved in the oxidative metabolism of phenol, followed by further degradation via either meta- or ortho-pathways. In this study, the first known instance of phenol degradation via the meta-pathway by a member of the genus Acinetobacter (Acinetobacter sp. strain AQ5NOL 1) is reported. Phenol hydroxylase converts phenol to catechol, which is then converted via the meta-pathway to 2-hydroxymuconic semialdehyde by the catechol 2,3-dioxygenase enzyme. Phenol hydroxylase extracted from strain AQ5NOL 1 was fully purified using DEAE-Sepharose�, DEAE-Sephadex�, Q-Sepharose� and Zorbax� Bioseries GF-250 gel filtration and was demonstrated by SDS-PAGE to have a molecular weight of 50�kDa. The phenol hydroxylase was purified to about 210.51 fold. The optimum pH and temperature for enzyme activities are 20��C and 7�7.5, respectively. The apparent Km and Vmax values of phenol hydroxylase with phenol as the substrate were 13.4��M and 2.5��mol�min?1�mg?1, respectively. The enzyme was stable at ?20��C for 36�days. � 2016, Accademia Nazionale dei Lincei.
dc.description.natureFinalen_US
dc.identifier.doi10.1007/s12210-016-0554-2
dc.identifier.issn20374631
dc.identifier.issue1
dc.identifier.scopus2-s2.0-84978087101
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84978087101&doi=10.1007%2fs12210-016-0554-2&partnerID=40&md5=df47e5b3847e670c2bcf740bd922c7a2
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/9137
dc.identifier.volume28
dc.languageEnglish
dc.language.isoen_US
dc.publisherSpringer-Verlag Italia s.r.l.en_US
dc.relation.ispartofRendiconti Lincei
dc.sourceScopus
dc.subjectAcinetobacter spen_US
dc.subjectCharacterizationen_US
dc.subjectPhenol hydroxylaseen_US
dc.subjectPurificationen_US
dc.subjectCharacterizationen_US
dc.subjectEnzymesen_US
dc.subjectIon exchangeen_US
dc.subjectMetabolismen_US
dc.subjectPhenolsen_US
dc.subjectPhysiologyen_US
dc.subjectPurificationen_US
dc.subjectAcinetobacter spen_US
dc.subjectAcinetobactersen_US
dc.subjectEnzymatic pathwaysen_US
dc.subjectMeta-cleavage pathwayen_US
dc.subjectOxidative metabolismen_US
dc.subjectPhenol biodegradationen_US
dc.subjectPhenol degradationen_US
dc.subjectPhenol hydroxylaseen_US
dc.subjectBiodegradationen_US
dc.titleMeta-cleavage pathway of phenol degradation by Acinetobacter sp. strain AQ5NOL 1
dc.typeArticleen_US
dspace.entity.typePublication

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