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
	2009-12-15
发表期刊	BIOCHEMICAL ENGINEERING JOURNAL
ISSN	1369-703X
卷号	48 期号:1 页码:58-64
文章类型	Article
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
关键词	Maltose-binding Protein Phycocyanin-alpha Subunit Protein Engineering Recombinant Protein Chromatography Recombinant Protein Production
学科领域	Biotechnology & Applied Microbiology ; Engineering, Chemical
DOI	10.1016/j.bej.2009.08.006
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000274349900009
引用统计	被引频次：17[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/2976
专题	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
第一作者单位	中国科学院海洋研究所
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.

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