Specific dechlorinase activity on lindane degradation by Streptomyces sp. M7

CUOZZO, S.A.; ABATE, C.M; ROLLAN, G. C; AMOROSO M.J

WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY

SPRIMGER

Lugar: NUEVA YORK; Año: 2008

0959-3993

Synthesis of dechlorinase in Streptomyces sp. M7 was induced when the microorganism was grown in the presence of lindane (g-HCH) as the only carbon source. Activity of cells grown with lindane was about four and half times higher compared to cells grown with glucose. Maximum dechlorinase activity was observed at 30 ºC in alkaline conditions pH (7.9) and the enzyme did not show cation dependency. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed one differential band with a molecular weight similar to serum albumin (Mr 66,200), which corresponded to polynucleotide phosphorylase, an enzyme that plays an important role in the regulation system and could be involved in the regulation of the dechlorinase gene. Were present in the cell-free extracts γ-pentachlorocyclohexene (γ-PCCH) and 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN), both being products of the dechlorinase activity. This is the first time that the presence of an enzyme with dechlorinase activity has been demonstrated in an actinomycete strain isolated in Tucumán, Argentina. Characteristics of this enzyme revealed that Streptomyces sp. M7 could be useful in bioremediation of soil or as a biosensor in the future.