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

doi:10.1016/j.bej.2009.08.006

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	Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli
	Liu, Shaofang 1,2; Chen, Huaxin 1; Qin, Song 1; Zhang, Weijie 1,2; Guan, Xiangyu 3; Lu, Yandu 2,4
刊名	BIOCHEMICAL ENGINEERING JOURNAL
	2009-12-15
卷号	48 期号:1 页码:58-64
关键词	Maltose-binding Protein Phycocyanin-alpha Subunit Protein Engineering Recombinant Protein Chromatography Recombinant Protein Production
ISSN号	1369-703X
DOI	10.1016/j.bej.2009.08.006
文献子类	Article
英文摘要	C-phycocyanin (Cpc) is one of the phycobiliproteins with highly fluorescent and various pharmacological activities Holo-Cpc-alpha Subunit (holo-CpcA) expressed in Escherichia colt 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 anti 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 (C) 2009 Elsevier B V. All rights reserved; C-phycocyanin (Cpc) is one of the phycobiliproteins with highly fluorescent and various pharmacological activities Holo-Cpc-alpha Subunit (holo-CpcA) expressed in Escherichia colt 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 anti 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 (C) 2009 Elsevier B V. All rights reserved
学科主题	Biotechnology & Applied Microbiology ; Engineering, Chemical
URL标识	查看原文
语种	英语
WOS记录号	WOS:000274349900009
公开日期	2010-12-22
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/2977]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.China Univ Geosci, Sch Marine Sci, Beijing 100083, Peoples R China 4.Chinese Acad Sci, Yantai Inst Costal Zone Res Sustainable Dev, Yantai 264003, Peoples R China
推荐引用方式 GB/T 7714	Liu, Shaofang,Chen, Huaxin,Qin, Song,et al. Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli[J]. BIOCHEMICAL ENGINEERING JOURNAL,2009,48(1):58-64.
APA	Liu, Shaofang,Chen, Huaxin,Qin, Song,Zhang, Weijie,Guan, Xiangyu,&Lu, Yandu.(2009).Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli.BIOCHEMICAL ENGINEERING JOURNAL,48(1),58-64.
MLA	Liu, Shaofang,et al."Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli".BIOCHEMICAL ENGINEERING JOURNAL 48.1(2009):58-64.