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Lyase activities of heterologous CpcS and CpcT for phycocyanin holo-beta-subunit from Arthrospira platensis in Escherichia coli

文献类型: 外文期刊

作者: Yi Junjie 1 ; Xu Di 1 ; Zang Xiaonan 1 ; Yuan Dingyang 2 ; Zhao Bingran 2 ; Tang Li 2 ; Tan Yanning 2 ; Zhang Xuecheng 1 ;

作者机构: 1.Ocean Univ China, Minist Educ, Key Lab Marine Genet & Breeding, Qingdao 266003, Peoples R China

2.Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha 410125, Hunan, Peoples R China

关键词: Arthrospira;CpcB;phycocyanobilin lyase;CpcS;CpcT

期刊名称:JOURNAL OF OCEAN UNIVERSITY OF CHINA ( 影响因子:0.913; 五年影响因子:1.012 )

ISSN: 1672-5182

年卷期: 2014 年 13 卷 3 期

页码:

收录情况: SCI

摘要: Arthrospira platensis is an economically important cyanobacterium; and it has been used widely in food and pharmaceutical industries. The phycocyanin (PC) from A. platensis is extremely valuable in medicine and molecular biology due to its antioxidation and anti-tumoring activity and applicability as fluorescence protein tag. In present study, two recombinant plasmids, one contained the phycocyanobilin (PCB)-producing genes (hox1 and pcyA) while the other contained the phycobiliprotein gene (cpcB) and the lyase gene (either cpcS/U or cpcT), were constructed and synchronically transferred into E. coli in order to test the the activities of relevant lyases for catalysing PCB addition to CpcB during synthesizing fluorescent PC holo-beta-subunit (beta-PC) of A. platensis. As was evidenced by the fluorescence emitted at a peak specific for PC, CpcB was successfully synthesized in E. coli, to which co-expressed PCBs attached though at a relatively low efficiency. The results showed that the attachment of PCBs to CpcB were carried out mainly by co-expressed CpcS/U but CpcB also showed some autocatalytic activity. Currently, no CpcT activity was detected in this E. coli expression system. Further studies will be conducted to improve the efficiency of fluorescent PC synthesis in E. coli.

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