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Nature’s Green Catalyst for Environmental Remediation, Clean Energy Production, and Sustainable Development
Published in Miguel A. Esteso, Ana Cristina Faria Ribeiro, A. K. Haghi, Chemistry and Chemical Engineering for Sustainable Development, 2020
Benny Thomas, Divya Mathew, K. S. Devaky
Halogenated compounds produced by both natural activities and man-made efforts are present everywhere in the soil. These compounds may be hazardous, toxic, mutagenic, or carcinogenic. Haloalkane dehalogenases are useful for the hydrolysis of carbon halogen bonds present in the various halogens containing contaminants and produce alcohol and halides.51 The active site of haloalkane dehalogenase is present between the main domains of an eight-stranded β-sheet helices. First haloalkane dehalogenase discovered from the bacterium Xanthobacter autotrophicus has the ability to degrade 1, 2-dichloroethane. Several dehalogenases have been cloned and characterized from Gram-positive and Gram-negative haloalkane degrading bacteria.
Lindane degradation by root epiphytic bacterium Achromobacter sp. strain A3 from Acorus calamus and characterization of associated proteins
Published in International Journal of Phytoremediation, 2019
Polypeptide band 1 of Achromobacter sp. strain A3 was identified as alpha/beta hydrolase fold-3 domain-containing protein. This protein has hydrolase activity and takes part in metabolic processes. Hydrolases catalyze the hydrolysis of various bonds. Here, in our study, the expression of this protein solely under the stress of lindane proves that it is involved in lindane hydrolysis. Other studies show that LinB from Sphingomonas paucimobilis UT26 is a haloalkane dehalogenase belonging to α/β-hydrolase family. These are microbial enzymes which catalyze the hydrolytic dechlorination reaction in the degradation of lindane. These enzymes play important role in bioremediation of contaminated areas, hence, can be used for the protection of the environment (Nagata et al. 1997; Kmunicek et al. 2005). Polypeptide band 2 was identified as extracellular solute-binding family protein. The molecular function of this protein is transporter activity, i.e., it enables the aimed movement of substances such as ions, macromolecules, and small molecules into or out of the cell. In gram-negative bacteria, solute binding proteins are dissolved in the periplasm and participate in transmembrane transport. In the present study, the expression of this protein solely under the stress of lindane demonstrates its role in transmembrane transport of lindane for utilization of lindane by bacteria. In Sphingomonas paucimobilis UT26, genes for ABC-transporter system are essential for utilization of lindane (Endo et al. 2007). It has also been found that periplasmic phosphate binding protein initiates the signal resulting in induction of phosphate regulon in enteric bacteria (Tam and Saier 1993).