Anti-oxidant activity of holo- and apo-c-phycocyanin and their protective effects on human erythrocytes.

This study was conducted to investigate the anti-oxidant activity of the recombinant apo-c-phycocyanin (c-PC) ß-subunit compared to native c-PC purified from Spirulina sp. The gene encoding the ß-subunit of c-PC was successfully cloned and expressed in Escherichia coli. The anti-oxidant capacities of recombinant apo-c-PC(ß) and native c-PC were evaluated by measuring their Trolox equivalent antioxidant capacities and examining their protective effects on erythrocytes from normal and homozygous haemoglobin E individuals against peroxyl radicals and hydrogen peroxide. The results demonstrated that the anti-oxidant capacities are native c-PC≫Trolox>recombinant apo-c-PC(ß). Both anti-oxidant proteins can potentially protect erythrocytes from oxidative damage. Expression of c-PC in bacteria reduces the cost and time for protein production, and the recombinant protein could be further developed to obtain a more efficient protein for therapeutic purposes.