Effect of organic solvents, temperature and EDTA on activity and stability of halophilic .ALPHA.-amylase from Haloarcula sp. S-1

Abstract

More than 80% of residual halophilic α-amylase (crude and purified) activity from strain S-1 was observed in the presence of various organic solvents. More than 78% remaining activity was detected after incubation for 120 hr in the presence of styrene, toluene, benzene or chloroform. Enzyme activity and stability with chloroform were higher than that without chloroform at the low or high temperature, and enzyme activity was higher in the presence of chloroform than one without chloroform when EDTA (5-15 mM) was added.