Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/51295
Title: Purification and characterization of a thermostable phycoerythrin from hot spring cyanobacterium leptolyngbya sp. KC45
Authors: Chayakorn Pumas
Yuwadee Peerapornpisal
Panmuk Vacharapiyasophon
Pimporn Leelapornpisid
Walailuck Boonchum
Masaharu Ishii
Chartchai Khanongnuch
Keywords: Agricultural and Biological Sciences
Issue Date: 28-Feb-2012
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84857434681&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/51295
ISSN: 18149596
15608530
Appears in Collections:CMUL: Journal Articles

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