Glutathione S-transferases (GSTs) play an important role in phase II
of detoxification to protect cells in response to oxidative stress
generated by exogenous toxicants. Despite their important role in
defense, studies on invertebrate GSTs have mainly focused on identification
and characterization. Here, we isolated omega and sigma classes of
GSTs from the freshwater rotifer Brachionus calyciflorus and the marine rotifer Brachionus koreanus and
explored their antioxidant function in response to metal-induced oxidative
stress. The recombinant Bc- and Bk-GSTs were successfully transformed
and expressed in Escherichia coli. Their antioxidant
potential was characterized by measuring kinetic properties and enzymatic
activity in response to pH, temperature, and chemical inhibitor. In
addition, a disk diffusion assay, reactive oxygen species assay, and
morphological analysis revealed that GST transformed
into E. coli significantly protected cells from oxidative
stress induced by H2O2 and metals (Hg, Cd, Cu,
and Zn). Stronger antioxidant activity was exhibited by GST-S compared
to GST-O in both rotifers, suggesting that GST-S plays a prominent
function as an antioxidant defense mechanism in Brachionus spp. Overall, our study clearly shows the antioxidant role of Bk-
and Bc-GSTs in E. coli and provides a greater understanding
of GST class-specific and interspecific detoxification in rotifer Brachionus spp.