Isolation, purification and immobilization of sulfide oxidase from Alcaligenes faecalis

D.Thulasi; R. Saraswathy; M. Muralidhar

Volume : VII, Issue : VIII, August - 2017

Isolation, purification and immobilization of sulfide oxidase from Alcaligenes faecalis

D. Thulasi, R. Saraswathy, M. Muralidhar

Abstract :

Sulfide oxidase is the enzyme involved in sulfide pathway which catalyzes the conversion of toxic form of sulfide to non toxic sulfate. In this study, an attempt was made to isolate and purify sulfide oxidase from Alcaligenes faecalis and its activity was measured. The isolated enzyme was purified using acetone precipitation and ion exchange chromatography. Column purified extracts registered sulfide oxidase activity of 39 µm/hr/mg of protein and the purification was increased up to 65 fold. The optimum sulfide oxidase activity was found in pH (6– 8), salinity (10–30 ppt) and temperature (30 & 35 ^◦C). In addition to this, chitosan beads were prepared for the immobilization of sulfide oxidase. Further, experiments to evaluate the capacity of the immobilized enzyme to remove sulfide with more emphasis on stability in field conditions would provide useful information to mitigate sulfide from aquaculture ponds.