Expression and characterization of Bacillus subtilis PY22 α-amylase in Pichia pastoris

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

In-fusion expression and characterization of β-xylanase and β-1,3-1,4-glucanase in Pichia pastoris

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Jiayun Qiao ◽  
Yunhe Cao
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Fusion Protein ◽  
Fusion Expression ◽  
Chimeric Genes ◽  
Fusion Enzyme ◽  
Fusion Enzymes ◽  
Aspergillus Sulphureus

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.

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
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Heterologous Expression

Cloning, Expression, and Characterization of β-mannanase from Bacillus subtilis MAFIC-S11 in Pichia pastoris

2013 ◽  
Vol 169 (8) ◽  
pp. 2326-2340 ◽  
Author(s):  
Junnan Lv ◽  
Yiqun Chen ◽  
Honglei Pei ◽  
Wenhan Yang ◽  
Zhimin Li ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris

Overexpression and Biochemical Characterization of a Thermostable Phytase from Bacillus subtilis US417 in Pichia pastoris

2014 ◽  
Vol 56 (9) ◽  
pp. 839-848 ◽  
Author(s):  
Aïda Hmida-Sayari ◽  
Fatma Elgharbi ◽  
Ameny Farhat ◽  
Hatem Rekik ◽  
Karine Blondeau ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Biochemical Characterization

Codon optimization, expression and characterization of Bacillus subtilis MA139 β-1,3-1,4-glucanase in Pichia pastoris

Biologia ◽  
2010 ◽  
Vol 65 (2) ◽  
Author(s):  
Jiayun Qiao ◽  
Bo Zhang ◽  
Yiqun Chen ◽  
Yunhe Cao
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Codon Bias ◽  
De Novo ◽  
Alcohol Oxidase ◽  
Methanol Induction ◽  
Chemical Reagents ◽  
Prospective Application ◽  
High Level

Abstractβ-1,3-1,4-Glucanase has been broadly used in feed and brewing industries. According to the codon bias of Pichia pastoris, the Bacillus subtilis MA139 β-1,3-1,4-glucanase gene was de novo synthesized and expressed in P. pastoris X-33 strain under the control of the alcohol oxidase 1 promoter. In a 10-L fermentor, the β-1,3-1,4-glucanase was overexpressed with a yield of 15,000 U/mL by methanol induction for 96 h. The recombinant β-1,3-1,4-glucanase exhibited optimal activity at 40°C and pH 6.4. The activity of the recombinant β-1,3-1,4-glucanase was not significantly affected by various metal ions and chemical reagents. To our knowledge, the expression of this β-1,3-1,4-glucanase from Bacillus sp. in P. pastoris is in relatively high level compared to previous reports. These biochemical characteristics suggest that the recombinant β-1,3-1,4-glucanase has a prospective application in feed and brewing industries.

scholarly journals Sequence and characterization of Bacillus subtilis CheW.

1992 ◽  
Vol 267 (17) ◽  
pp. 12055-12060
Author(s):  
D.W. Hanlon ◽  
L.M. Márquez-Magaña ◽  
P.B. Carpenter ◽  
M.J. Chamberlin ◽  
G.W. Ordal
Keyword(s):  
Bacillus Subtilis
Sign in / Sign up

Export Citation Format

Share Document