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Mineralization of mono‐nitrophenols by Bjerkandera adusta and Lentinus squarrosulus and their extracellular ligninolytic enzymes
Author(s) -
Tripathi Astha,
Upadhyay R. C.,
Singh Surendra
Publication year - 2011
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201000436
Subject(s) - chemistry , laccase , bioremediation , manganese peroxidase , lignin peroxidase , food science , enzyme , environmental chemistry , biochemistry , biology , contamination , ecology
Nitroaromatic compounds constitute a major class of widely distributed environmental contaminants. Fifty fungal strains were screened for their potential to tolerance with 2‐nitrophenol, 3‐nitrophenol and 4‐nitrophenol on solid medium supplemented with 2% malt extract (MEA). Growth rate (mm/day) was determined at three concentrations (0.25, 0.5 and 1 mM) of all the three nitrophenols. From the fifty fungal strains only Bjerkandera adusta and Lentinus squarrosulus were able to tolerate all the three nitrophenols (NPs). These white‐rot fungi (WRF) were chosen for liquid medium studies for the mineralization of mono‐nitrophenols and ligninolytic enzyme activity at 0.25 mM concentration. Both varieties completely removed 2‐NP and 3‐NP while 4‐NP was hard to mineralize. AAO (Aryl Alcohol Oxidase) is the main oxidase enzyme in B. adusta while laccase plays important role in L. squarrosulus . MnP (Manganese peroxidase) is the main peroxidase enzyme in both varieties. These fungal strains were capable to degrade nitrophenols and could be used for bioremediation applications on large scale. (© 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)