TY - JOUR
T1 - Chloroperoxidase-mediated transformation of highly halogenated monoaromatic compounds
AU - Longoria, Adriana
AU - Tinoco, Raunel
AU - Vázquez-Duhalt, Rafael
N1 - Funding Information:
This work was funded by Grant (SEMARNAT 2002-C01-1307) from the National Council of Science and Technology of Mexico (CONACyT). Authors thank to Prof. Michael A. Pickard for his critical reading of the manuscript.
PY - 2008/6
Y1 - 2008/6
N2 - Peroxidase transformations of widely distributed pollutants, tetra- and penta-chlorinated phenols and anilines, were studied using different peroxidases. Chloroperoxidase from Caldariomyces fumago was able to transform tetra- and penta-chlorinated phenols and anilines, while horseradish peroxidase, lignin peroxidase from Phanerochaete chrysosporium and versatile peroxidase from Bjerkandera adusta were able only to transform the halogenated phenols. Chloroperoxidase showed a specific activity on pentachlorophenol two orders of magnitude higher than lignin peroxidase and horseradish peroxidase, and one order of magnitude higher than versatile peroxidase. The main product from peroxidase oxidation in all cases was a polymeric and insoluble material. The insolubilization of halogenated phenols and anilines permits their removal, reduces their bioavailability, and thus reduces their environmental impact. The other minor products from the enzymatic transformation of highly chlorinated compounds were determined by mass spectrometry. Tetrachloroquinone, dimers and trimers of halogenated compounds were also identified. Chloroperoxidase was able to halogenate tetrachloroaniline to form pentachloroaniline.
AB - Peroxidase transformations of widely distributed pollutants, tetra- and penta-chlorinated phenols and anilines, were studied using different peroxidases. Chloroperoxidase from Caldariomyces fumago was able to transform tetra- and penta-chlorinated phenols and anilines, while horseradish peroxidase, lignin peroxidase from Phanerochaete chrysosporium and versatile peroxidase from Bjerkandera adusta were able only to transform the halogenated phenols. Chloroperoxidase showed a specific activity on pentachlorophenol two orders of magnitude higher than lignin peroxidase and horseradish peroxidase, and one order of magnitude higher than versatile peroxidase. The main product from peroxidase oxidation in all cases was a polymeric and insoluble material. The insolubilization of halogenated phenols and anilines permits their removal, reduces their bioavailability, and thus reduces their environmental impact. The other minor products from the enzymatic transformation of highly chlorinated compounds were determined by mass spectrometry. Tetrachloroquinone, dimers and trimers of halogenated compounds were also identified. Chloroperoxidase was able to halogenate tetrachloroaniline to form pentachloroaniline.
KW - Chloroperoxidase
KW - Halogenated compounds
KW - Pentachloroaniline
KW - Pentachlorophenol
KW - Tetrachloroaniline
KW - Tetrachlorophenol
UR - http://www.scopus.com/inward/record.url?scp=43649086451&partnerID=8YFLogxK
U2 - 10.1016/j.chemosphere.2008.03.006
DO - 10.1016/j.chemosphere.2008.03.006
M3 - Artículo
C2 - 18439646
AN - SCOPUS:43649086451
SN - 0045-6535
VL - 72
SP - 485
EP - 490
JO - Chemosphere
JF - Chemosphere
IS - 3
ER -