Change in catalase activity was examined in leaves of rice plant exposed to salinity. Depending on the method of preparation of crude protein extract from leaf and the constituents of the assay medium, a significant difference in enzyme activity was recorded. Inclusion of sorbitol or mannitol or sucrose in the extraction and enzyme assay medium enhanced the enzyme activity in salt-stressed samples by nearly 1.5-1.8 fold, compared to the activity found in unstressed plants, which otherwise showed a 50% declined activity in leaf extract prepared in buffer solution and assayed in a medium depleted of these sugars. In view of the accumulation of osmolytes under saline condition, these observations suggest that the catalase activity is modulated by the osmolytes and maintains a high rate of hydrogen peroxide scavenging property in vivo and serves as the major antioxidant enzyme to scavenge the salt-induced formation of peroxide. Therefore, the salt-stress induced appearance of low activity of the enzyme under normal buffer extraction and assay conditions, as reported in literature may represent an apparent than for its real in vivo activity.
Expression of plant proteins in E. coli is frequently unsuccessful, but soluble and functional rice catalase-B can be produced in E. coli when it is co-expressed with the chaperone GroEL/ES. The rice catalase exhibited properties typical for a catalase including the decomposition of H(2)O(2) and inhibition by aminotriazole, a specific inhibitor for plant and animal catalases. This achievement records for first time the successful expression of a both native and variant rice plant catalase in bacterial cytosol suggesting that it may be an option to be considered for the expression of other plant proteins in E. coli.
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