%0 Journal Article
%T Fusion Expression of D-amino Acid Oxidase from Trignoposis variabilis with Maltose Binding Protein and Vitreoscilla Hemoglobin<br>D-氨基酸氧化酶与麦芽糖结合蛋白和透明颤菌血红蛋白的融合表达
%A Huimin Yu
%A Xianfeng M
%A Hui Luo
%A Cheng Wen
%A Zhongyao Shen
%A <br>于慧敏
%A 马现锋
%A 罗晖
%A 文程
%A 沈忠耀
%J 微生物学报
%D 2008
%I 
%X D-amino acid oxidase (DAAO) is one of important industrial enzymes. To increase the solubility and activity of the TvDAAO from Trignoposis variabilis expressed in recombinant Escherichia coli (E. coli), a maltose binding protein (MBP) and Vitreoscilla hemoglobin (VHb) was introduced to fuse with N-terminal of the TvDAAO, respectively. Fusion protein of MBP-TvDAAO was constitutively expressed in JM105/pMKC-DAAO and inductively expressed in JM105/pMKL-DAAO. With respect to the control strain of BL21 (DE3)/pET-DAAO without MBP fusion, the constitutive fusion expression obtained 28% of soluble protein with 3.7 folds of solubility improvement. As for the inductive fusion expression, corresponding results changed to 17% and 1.8 folds, respectively. However, the DAAO activity significantly decreased in the MBP-fusing expression. Fusion protein of VHb-TvDAAO was constructed and inductively expressed in BL21 (DE3)/pET-VDAAO. Its DAAO activity highly reached 3.24 u/mL in flask culture, about 90% increase in contrast to the control without VHb.
%K D-amino acid oxidase (DAAO)
%K maltose binding protein (MBP)
%K Vitreoscilla Hemoglobin (VHb)
%K fusion expression<br>D-氨基酸氧化酶
%K 大肠杆菌麦芽糖结合蛋白
%K 透明颤菌血红蛋白
%K 融合表达
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=FEF5E9F4D086E2125FB735AE6CB759F1&yid=67289AFF6305E306&vid=B91E8C6D6FE990DB&iid=B31275AF3241DB2D&sid=F0CB1CC137DFCF2D&eid=9F481C73BF82C48F&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=0