PURIFICATION AND CHARACTERIZATION OF ϒ-
HEXACHLOROCYCLOHEXANE (HCH) DEHYDROCHLORINASE
FROM BURKHOLDERIA PSEUDOMALLEI T4
I.M. MANDAPPA, H.M. RAJASHEKARA MURTHY, P.R. RAMASARMA, M.S. THAKUR AND H.K.MANONMANI
Abstract
Bacterial isolates belonging to HCH -degrading microbial consortium were screened
individually for HCH - dehydrochlorinase activity. Among these, the cell free extract of Burkholderia
pseudomallei T4 showed higher ϒ-HCH- dehydrochlorinase activity. The enzyme was purified to apparent
homogeneity using Sephorose 6B gel permeation chromatography with 4.8 fold purification. The purity
was confirmed using SDS - PAGE, capillary electrophoresis and HPLC. The enzyme had pH optimum of
6.0 and temperature optimum of 28 oC and was stable for 2 h. The Km and Vmax values of the enzyme
were 2.162 and 39.52, respectively. Molecular weight of the enzyme was ∼32 KDa on SDS- PAGE. The
enzyme was found to be a glycoprotein with mannose forming the carbohydrate backbone. The
enzyme appeared to be a metallo protein containing Zn, Mg and Ca. The enzyme was inhibited by
monovalent and divalent cations. The purified enzyme showed reactivity with all isomers of HCH
except α-isomer and was not reactive against other halo aromatic derivatives. Serine and tryptophan
residues were present in the active site. The N-terminal sequence was found to be AIGRVHNA.
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