%0 Journal Article
%T Fusion expression of an extreme-thermostable xylanase B64 gene from Thermotoga maritima MSB8 in Escherichia coli<br>海栖热袍菌极耐高温木聚糖酶基因xynB64在大肠杆菌中的融合表达
%A SUN Tao
%A SHEN Ning
%A BAI Yu
%A LI Wen-Hao
%A WEI Ping
%A <br>孙涛
%A 申宁
%A 白羽
%A 李文豪
%A 韦萍
%J 微生物学通报
%D 2011
%I 
%X Xylanase B from thermophile bacteria Thermotoga maritima MSB8 has extreme-thermostability, which has potential widely application for feed, papermanufacture, energy, food and medicine industries. Recombinant pET28a(+)-xynB64 was induced and expressed in E. coli BL21(DE3), and the activity of recombinant XynB64 was very low. E. coli BL21-CodonPlus(DE3)-RIPL and Rosetta(DE3) both harbouring rare tRNAs were used to replace E. coli BL21(DE3) and the activity of recombinant XynB64 increased by 197% and 277%, respectively. However, some inclusion body was formed in E. coli Rosetta(DE3). Next, pET32a(+), pET42a(+), pET43.1a(+) and pMAL-c2X, which has the Trx, GST, Nus and MBP fusion tag respectively were used to replace pET28a(+) with E. coli Rosetta(DE3) as host. The activity of recombinant XynB64 produced by Rosetta(DE3)/pMAL-c2X-xynB64 was highest, which was equivalent to 88% of counterparts of Rosetta(DE3)/pET28a-xynB64. Meanwhile about 40 percent whole cell proteins of former were recombinant XynB64 with little inclusion body.
%K Thermostable xylanase
%K Rare codon
%K Fusion tag
%K Translation initiation region (TIR)<br>耐高温木聚糖酶
%K 稀有密码子
%K 融合标签
%K 翻译起始区
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=78024727B5F4EF6AA9CA8E605B5FC464&aid=AEC2A3F8CAFD3A6E4906E4DAE4FD9352&yid=9377ED8094509821&vid=16D8618C6164A3ED&iid=DF92D298D3FF1E6E&sid=602F518C16859E7D&eid=FB3C6F66BC48DD45&journal_id=0253-2654&journal_name=微生物学通报&referenced_num=0&reference_num=18