Heterologous expression and characterization of man gene from Bacillus Subtilis in Pichia Pastoris

2008 ◽  
Vol 3 (1) ◽  
pp. 26-31 ◽  
Author(s):  
Yu Qiao ◽  
Xiaobing Chen ◽  
Hongbiao Ding ◽  
Ming Yue
2017 ◽  
Vol 30 (8) ◽  
pp. 571-571 ◽  
Author(s):  
Svetlana A Korban ◽  
Kirill S Bobrov ◽  
Maria A Maynskova ◽  
Stanislav N Naryzhny ◽  
Olga L Vlasova ◽  
...  

2018 ◽  
Vol 28 (12) ◽  
pp. 2057-2063 ◽  
Author(s):  
Wang Bo ◽  
Ying Yan ◽  
Jing Xu ◽  
Xiaoyan Fu ◽  
Hongjuan Han ◽  
...  

2001 ◽  
Vol 14 (5) ◽  
pp. 675-677 ◽  
Author(s):  
J. Patrick Martinez ◽  
Sean A. Ottum ◽  
Shaukat Ali ◽  
Leonard J. Francl ◽  
Lynda M. Ciuffetti

The ToxB gene was cloned and characterized from a race 5 isolate of Pyrenophora tritici-repentis from North Dakota. ToxB contains a 261-bp open reading frame that encodes a 23 amino acid putative signal peptide and a 64 amino acid host-selective toxin, Ptr ToxB. Analysis of Ptr ToxB from heterologous expression in Pichia pastoris confirms that ToxB encodes a host-selective toxin.


2018 ◽  
Vol 120 ◽  
pp. 657-664 ◽  
Author(s):  
Xin Cui ◽  
Yuechen Jiang ◽  
Liuyi Chang ◽  
Lei Meng ◽  
Junhong Yu ◽  
...  

2020 ◽  
Vol 147 ◽  
pp. 890-897 ◽  
Author(s):  
Zhikuan Wang ◽  
Xiaoguang Li ◽  
Jiewei Tian ◽  
Yiwen Chu ◽  
Yongqiang Tian

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Jiayun Qiao ◽  
Yunhe Cao

AbstractTwo chimeric genes, XynA-Bs-Glu-1 and XynA-Bs-Glu-2, encoding Aspergillus sulphureus β-xylanase (XynA, 26 kDa) and Bacillus subtilis β-1,3-1,4-glucanase (Bs-Glu, 30 kDa), were constructed via in-fusion by different linkers and expressed successfully in Pichia pastoris. The fusion protein (50 kDa) exhibited both β-xylanase and β-1,3-1,4-glucanase activities. Compared with parental enzymes, the moiety activities were decreased in fermentation supernatants. Parental XynA and Bs-Glu were superior to corresponding moieties in each fusion enzymes because of lower Kn higher kcat. Despite some variations, common optima were generally 50°C and pH 3.4 for the XynA moiety and parent, and 40°C and pH 6.4 for the Bs-Glu counterparts. Thus, the fusion enzyme XynA-Bs-Glu-1 and XynA-Bs-Glu-2 were bifunctional.


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