Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorChayakorn Pumasen_US
dc.contributor.authorYuwadee Peerapornpisalen_US
dc.contributor.authorPanmuk Vacharapiyasophonen_US
dc.contributor.authorPimporn Leelapornpisiden_US
dc.contributor.authorWalailuck Boonchumen_US
dc.contributor.authorMasaharu Ishiien_US
dc.contributor.authorChartchai Khanongnuchen_US
dc.description.abstractThis 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.en_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.titlePurification and characterization of a thermostable phycoerythrin from hot spring cyanobacterium leptolyngbya sp. KC45en_US
article.title.sourcetitleInternational Journal of Agriculture and Biologyen_US
article.volume14en_US Mai Universityen_US School of Agricultural and Life Sciences The University of Tokyoen_US
Appears in Collections:CMUL: Journal Articles

Files in This Item:
There are no files associated with this item.

Items in CMUIR are protected by copyright, with all rights reserved, unless otherwise indicated.