Determination of carbonic anhydrase enzyme activity in halophilic/halotolerant bacteria

Abstract

In the present study, esterase and hydratase activities of carbonic anhydrase (CA) enzyme of twenty-one halophilic/halotolerant bacterial isolates were investigated. According to the obtained data, ten isolates possess both esterase and hydratase activity, whereas six isolates possess only hydratase activity. The highest esterase activity was obtained from Halomonas neptunia (EM23), Bacillus pumilus (EM3) and Bacillus sp. (EM21), whereas the highest hydratase activity was obtained from Bacillus sp. (EM21), Bacillus sp. (EM13) and Halobacillus sp. (EM7), respectively. Two amino acids (l-cysteine and l-glutamic acid) and an herbicide (Simazine) were tested on CA of two bacterial isolates (EM21 and EM23). According to the obtained results in amino acids and herbicide applications, l-cysteine and simazine activated CA, whereas l-glutamic acid inhibited the CA activities of two bacterial isolates. In this paper, we have reported the CA activities in Gram positive bacteria for the first time. As CAs are important in all organisms including microorganisms, the determination of the presence of CAs and illustrating their functions in microorganisms is of vital importance in protecting the health of human being and nature.