Citation
Gan Bee Koon, . and Mohd Arif Syed, . and Mohd Yunus Abdul Shukor, . and Nor Aripin Shamaan, . and Siti Aqlima Ahmad, . (2011) Characterisation of phenol hydroxylase from phenol-degrading Acinetobacter sp. strain AQ5SNOL 1. [Proceedings Paper]
Abstract
Phenol has been widely used in the manufacture of pesticides chemicals and plastics and in industries such as petroleum refining. Phenol effluents and wastes that are discharged onto land and into rivers have exposed the environment to the potential toxic effects of this pollutant. Bacteria have the ability to convert phenol into nontoxic intermediates in either anaerobic or aerobic conditions. Under aerobic conditions the first step in the phenol-degrading pathway is the monohydroxylation of the ortho position of the aromatic ring. The enzyme responsible for this reaction is phenol hydroxylase. In this study phenol hydroxylase from Acinetobacter sp. strain AQ5NOL 1 was purified by about 211 fold by ion exchange chromatography using DEAE-Sepharose DEAE-Sephadex and Q-Sepharose and Zorbax R Bioseries GF-250 gel filtration. The enzyme has a molecular weight of 50 kDA as determined by SDS-PAGE. The apparent Km and Vmax values of phenol hydroxylase with phenol as substrate were 13.4 M and 2.5 mole / min / mg respectively. The optimum pH and temperature maximum for enzyme activities were between 7 to 7.5 and 20C respectively and this enzyme was stable at -20C for 36 days.
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Abstract
Phenol has been widely used in the manufacture of pesticides chemicals and plastics and in industries such as petroleum refining. Phenol effluents and wastes that are discharged onto land and into rivers have exposed the environment to the potential toxic effects of this pollutant. Bacteria have the ability to convert phenol into nontoxic intermediates in either anaerobic or aerobic conditions. Under aerobic conditions the first step in the phenol-degrading pathway is the monohydroxylation of the ortho position of the aromatic ring. The enzyme responsible for this reaction is phenol hydroxylase. In this study phenol hydroxylase from Acinetobacter sp. strain AQ5NOL 1 was purified by about 211 fold by ion exchange chromatography using DEAE-Sepharose DEAE-Sephadex and Q-Sepharose and Zorbax R Bioseries GF-250 gel filtration. The enzyme has a molecular weight of 50 kDA as determined by SDS-PAGE. The apparent Km and Vmax values of phenol hydroxylase with phenol as substrate were 13.4 M and 2.5 mole / min / mg respectively. The optimum pH and temperature maximum for enzyme activities were between 7 to 7.5 and 20C respectively and this enzyme was stable at -20C for 36 days.
Additional Metadata
| Item Type: | Proceedings Paper |
|---|---|
| Additional Information: | Available at Perpustakaan Sultan Abdul Samad Universiti Putra Malaysia 43400 UPM Serdang Selangor Malaysia. QR22 M3I61 2011 vol.2 Call Number. |
| AGROVOC Term: | Acinetobacter |
| AGROVOC Term: | Biodegradation |
| AGROVOC Term: | Bioremediation |
| AGROVOC Term: | Microbial degradation |
| AGROVOC Term: | Phenols |
| AGROVOC Term: | Phenolic compounds |
| AGROVOC Term: | Microorganisms |
| AGROVOC Term: | Ion exchange chromatography |
| AGROVOC Term: | Gel filtration chromatography |
| AGROVOC Term: | HPLC |
| Geographical Term: | MALAYSIA |
| Depositing User: | Ms. Suzila Mohamad Kasim |
| Last Modified: | 24 Apr 2025 05:15 |
| URI: | http://webagris.upm.edu.my/id/eprint/13020 |
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