NDLI: Cloning and Kinetic Properties of Catechol 2,3-dioxygenase from Novel Alkaliphilic BTEX-degrading Pseudomonas sp. HB01

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Cloning and Kinetic Properties of Catechol 2,3-dioxygenase from Novel Alkaliphilic BTEX-degrading Pseudomonas sp. HB01

Content Provider	Semantic Scholar
Author	Hassan, Hamdy A. Eldein, Zain
Copyright Year	2014
Abstract	Nowadays, there has been a special interest in isolation and characterization of alkaliphilic organisms for their ability to degrade aromatic compounds. Alkaliphilic strain, HB01, was isolated from soil in Kafr El Ziat Egypt around some chemical, insecticides, and pesticides producing factories. 16S rRNA gene sequence-based phylogeny suggested that strain HB01 is a member of the genus Pseudomonas. The focus of this study showed the capability of this strain for BTEX degradation at pH range from 9-11. Based on this analysis, it was hypothesized that BTEX is converted to phenol and then to catechol by phenol hydroxylase components. The resulting catechol undergoes ring cleavage via the meta pathway by Catechol 2,3-dioxygenase (C2,3O) to form 2-hydroxymuconic semialdehyde, which enters the tricarboxylic acid cycle. Catechol 2, 3-dioxygenase (C2,3O) was amplified and expressed in E. coli DH5α using pGEM ® -T Easy Vector, Kinetic properties of catechol 2,3 dioxygenase (C2,3O) from alkaliphilic Pseudomonas sp. HB01 were analyzed catechol and 2,3-Dihydroxybiphenyl could be identified as the preferred substrates. C2,3O from Pseudomonas sp. HB01 had been severely affected and its activity rapidly inactivated by 3- Chlorocatechol. This finding may be necessary in order to estimate the true potential of this strain to be applied in the remediation of BTEX contaminants or natural attenuation of alkaline BTEX contaminated sites. (Hamdy A. Hassan, Abu Bakr A. Zain Eldein and Nashwa MH Rizk. Cloning and Kinetic Properties of Catechol 2,3-dioxygenase from Novel Alkaliphilic BTEX-degrading Pseudomonas sp. HB01. Life Sci J 2014;11(2):376- 384). (ISSN:1097-8135). http://www.lifesciencesite.com. 52
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.lifesciencesite.com/lsj/life1102/052_23064life110214_376_384.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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