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

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dc.contributor.authorAhmad, SAen_US
dc.contributor.authorShamaan, NAen_US
dc.contributor.authorSyed, MAen_US
dc.contributor.authorKhalid, Aen_US
dc.contributor.authorAb Rahman, NAen_US
dc.contributor.authorKhalil, KAen_US
dc.contributor.authorDahalan, FAen_US
dc.contributor.authorShukor, MYen_US
dc.date.accessioned2024-05-29T03:25:35Z
dc.date.available2024-05-29T03:25:35Z
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((R)), DEAE-Sephadex((R)), Q-Sepharose((R)) and Zorbax((R)) 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 degrees C and 7- 7.5, respectively. The apparent K-m and V-max values of phenol hydroxylase with phenol as the substrate were 13.4 mu M and 2.5 mu mol min(-1) mg(-1), respectively. The enzyme was stable at -20 degrees C for 36 days.
dc.identifier.doi10.1007/s12210-016-0554-2
dc.identifier.epage9
dc.identifier.isbn1720-0776
dc.identifier.issn2037-4631
dc.identifier.issue1
dc.identifier.scopusWOS:000394371100001
dc.identifier.spage1
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/11987
dc.identifier.volume28
dc.languageEnglish
dc.publisherSpringer-Verlag Italia Srlen_US
dc.relation.ispartofRendiconti Lincei-Scienze Fisiche E Naturali
dc.sourceWeb Of Science (ISI)
dc.subjectPurificationen_US
dc.subjectCharacterizationen_US
dc.subjectPhenol hydroxylaseen_US
dc.subjectAcinetobacter sp.en_US
dc.titleMeta-cleavage pathway of phenol degradation by Acinetobacter sp strain AQ5NOL 1
dc.typeArticleen_US
dspace.entity.typePublication

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