purification and characterization of esterase enzyme from aspergillus versicolor

Esterase is a biotechnologically important enzyme as it hydrolyzes water-soluble short-chain fatty acid esters. we tried to isolate and purify the esterase enzyme from aspergillus versicolor in this investigation. the enzyme was purified with ammonium sulfate precipitation, dialysis, and column chromatography. the enzyme was salted out, with maximum specific activity at 60 to 70 percent of saturation during precipitation. the column chromatography was performed with sephadex g-75 to purify the esterase from aspergillus versicolor and was able to achieve the purification fold of 6.9 nm. the partially purified enzyme was analyzed in sds-page and showed a single 32-kda band. the partially purified esterase enzyme was checked for its optimum conditions for maximal enzyme activity. this enzyme has a huge industrial potential which makes a significant contribution to eco-friendly approaches such as textile, food, and agrochemical industries as well as for bioremediation.