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Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
4054 206 2009 7 PDF Available
Title
Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli
Abstract

C-phycocyanin (Cpc) is one of the phycobiliproteins with highly fluorescent and various pharmacological activities. Holo-Cpc-α subunit (holo-CpcA) expressed in Escherichia coli resulted in low yield and tended to aggregate after purification. In this study, we constructed a new plasmid coding holo-CpcA fused with hexahistidine and maltose-binding protein tag, which designated as HMCpcA, to improve its solubility and stability without the impairment of its spectra and fluorescent properties. HMCpcA was significantly more stable over time and a wider range of pH as compared to holo-CpcA. In addition, both the solubility and yields of HMCpcA increase significantly. We here provided an example to demonstrate that MBP could also improve the stability of the protein it fused while it has been reported as a soluble fusion partner before. This novel fluorescent protein will facilitate the large-scale production and be potentially applicable for the development of fluorescent probes, as well as antioxidant agents.

Keywords
Maltose-binding protein; Phycocyanin-α subunit; Protein engineering; Recombinant protein; Chromatography; Recombinant protein production
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Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 48, Issue 1, 15 December 2009, Pages 58–64
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us