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

• Main Authors: Pumas C., Peerapornpisal Y., Vacharapiyasophon P., Leelapornpisid P., Boonchum W., Ishii M., Khanongnuch C.
• Format: Article
• Language: English
• Published: 2014
• Online Access: http://www.scopus.com/inward/record.url?eid=2-s2.0-84857434681&partnerID=40&md5=dda94aefedf01b4dd95db5e7d7e096f9; http://cmuir.cmu.ac.th/handle/6653943832/6836
• Institution: Chiang Mai University

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.