Secretory expression and characterization of a novel thermo-stable, salt-tolerant endo-1,4-β-mannanase of Bacillus subtilis WD23 by Pichia pastoris

2014 ◽  
Vol 240 (4) ◽  
pp. 671-677 ◽  
Author(s):  
Huiling Li ◽  
Zuyan Liu ◽  
Chunlei Wang ◽  
Shichen Huang ◽  
Min Zhao
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.


2010 ◽  
Vol 64 (3-4) ◽  
pp. 129-134 ◽  
Author(s):  
Barçın Karakaş ◽  
Mehmet İnan ◽  
Muharrem Certel

2008 ◽  
Vol 3 (1) ◽  
pp. 26-31 ◽  
Author(s):  
Yu Qiao ◽  
Xiaobing Chen ◽  
Hongbiao Ding ◽  
Ming Yue

2019 ◽  
Vol 50 (8) ◽  
pp. 2240-2250
Author(s):  
Chin‐Yen Tsai ◽  
Kuang‐Teng Wang ◽  
Yu‐Sheng Wu ◽  
Shinn‐Ping Yeh ◽  
Tsung‐Meng Wu

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