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Chromium(VI) reduction in Streptomyces sp. M7 mediated by a novel Old Yellow Enzyme

Old Yellow Enzymes play key roles in several cellular processes and have become an important family of enzymes with biotechnological potential. One of the major challenges of biotechnology consists of the bioremediation of co-polluted soils with organic and inorganic compounds. In co-contaminated ar...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2019-06, Vol.103 (12), p.5015-5022
Main Authors: Sineli, Pedro E., Guerrero, Daiana S., Alvarez, Analia, Dávila Costa, José Sebastián
Format: Article
Language:English
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Summary:Old Yellow Enzymes play key roles in several cellular processes and have become an important family of enzymes with biotechnological potential. One of the major challenges of biotechnology consists of the bioremediation of co-polluted soils with organic and inorganic compounds. In co-contaminated areas, chromium normally exists in its more toxic and carcinogenic form Cr(VI). Microorganisms can reduce this metal to the insoluble and less toxic Cr(III). Streptomyces sp. M7 is a strain able to efficiently bioremediate polluted soils with γ-hexachlorocyclohexane and Cr(VI). The complete degradation pathway for γ-hexachlorocyclohexane was recently elucidated in this strain. In the present work, we confirmed the ability of Streptomyces sp. M7 to eliminate a high percentage of Cr(VI) from a synthetic culture medium. After a transcriptional study in the presence of Cr(VI), we also report the molecular cloning of a gene coding for an Old Yellow Enzyme with chromate reductase activity. Our results suggest that the elimination of Cr(VI) by Streptomyces sp. M7 is directly related to the activity of this Old Yellow Enzyme. The importance of our work is in identifying for the first time an Old Yellow Enzyme with chromate reductase activity in Streptomyces and Actinobacteria. Finding this enzyme helps understand chromium homeostasis in Streptomyces sp. M7, in addition to opening a new research window related to Old Yellow Enzymes from Actinobacteria.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-019-09841-9