Purification and characterization of a thermostable phycoerythrin from hot spring cyanobacterium leptolyngbya sp. KC45

Abstract

This study aimed to understand characteristics of thermostable phycoerythrin from hot spring cyanobacteria Leptolyngbya sp. KC45. Phycoerythrin was purified with the purification index at 17.38 of A565/A280 ratio and demonstrated as two protein bands of 21 and 18 kDa under SDS-PAGE analysis. The native protein was assumed to be hexamer with a molecular mass of approximately 235 kDa based on the results from gel filtration. N-terminal amino acid sequences shared the highest percent of identities with Fremyella diplosiphon Fd33 at 100% and 90% for α- and β-subunit, respectively. Phycoerythrin and 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity remained at approximately 80% of the original level after being heated at 60°C for 30 min, indicating that it can be considered as the promising thermostable phycoerythrin. © 2012 Friends Science Publishers.