TY  - JOUR
N1  - Copyright of this article belongs to Elsevier.
ID  - open3285
UR  - https://www.sciencedirect.com/science/article/pii/S0269749124023303
A1  - Vasudeva, Gunjan
A1  - Sidhu, Chandni
A1  - Vaid, Kalyan
A1  - Priyadarshini, Pragya
A1  - Kumar, Vanish
A1  - Krishnan, Muthu
A1  - Singh, Balvinder
A1  - Pinnaka, Anil Kumar
Y1  - 2025///
N2  - The oxygenases are essential in the bioremediation of xenobiotic pollutants. To overcome cultivability constraints, this study aims to identify new potential extradiol dioxygenases using the functional metagenomics approach. RW1-4CC, a novel catechol 2,3-dioxygenase, was isolated using functional metagenomics approach, expressed in a heterologous system, and characterized thoroughly using state-of-the-art techniques. The serial truncation mutations of the C-terminal tail increase the catalytic efficiency of truncated proteins against the 2,3-dihydroxybiphenyl (2,3-DHB). RW1-4CC lose its 50 of activity at 60 °C, with its optimum temperature at 15 °C, whereas the truncated proteins were found to be more stable at extended temperature range, i.e., both RW1-4CC-A and RW1-4CC-B retained 50 of their activity at 75 °C, with their temperature optima at 55 °C and 65 °C, respectively. The molecular docking studies further confirmed the high binding affinity of truncated proteins for the 2,3-DHB than catechol. The molecular modeling analysis revealed the difference in iron-binding and substrate interacting environment of RW1-4CC and its truncated proteins. The efficiency of purified RW1-4CC to detect catechol was evaluated using a gold screen-printed electrode by cyclic voltammetry. RW1-4CC detected catechol in wastewater and artificial seawater up to the concentration of 100 μm, which makes it reliable for catechol detection.
PB  - Elsevier Science
JF  - Environmental Pollution
VL  - 367
KW  - Catechol 2
KW  - 3-dioxygenase
KW  -  Substrate-specificity
KW  -  Molecular modeling
KW  -  Biosensing
KW  -  functional metagenomics
TI  - Bioremediation of catecholic pollutants with novel oxygen-insensitive catechol 2,3-dioxygenase and its potential in biomonitoring of catechol in wastewater
ER  -