Cloning and overexpression of raw starch digesting α-amylase gene from Bacillus subtilis strain AS01a in Escherichia coli and application of the purified recombinant α-amylase (AmyBS-I) in raw starch digestion and baking industry

2013 ◽  
Vol 97 ◽  
pp. 118-129 ◽  
Author(s):  
Jetendra K. Roy ◽  
Anjan Borah ◽  
Charu Lata Mahanta ◽  
Ashis K. Mukherjee
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Subtilis Strain ◽  
Starch Digestion ◽  
Amylase Gene ◽  
Raw Starch ◽  
Baking Industry

scholarly journals Construction of a stable expression system for endoglucanase in Bacillus subtilis 168M

2016 ◽  
Vol 14 (2) ◽  
pp. 347-351
Author(s):  
Phan Thị Tuyết Minh ◽  
Nguyễn Quốc Việt ◽  
Nguyễn Kim Thoa ◽  
Lê Gia Hy ◽  
Trần Đình Mấn
Keyword(s):  
Bacillus Subtilis ◽  
Expression System ◽  
Stable Expression ◽  
Subtilis Strain ◽  
Amylase Gene ◽  
Biomass Hydrolysis ◽  
Endoglucanase Activity ◽  
Reading Frame ◽  
Successful Design ◽  
Main Components

Beta-D-1,4-endoglucanase plays an important role in biomass hydrolysis, the microorganisms in nature can synthesize this enzyme at very low activity. Together with development of biotechnology, a low enzymatic activity problem has been overcome by using the recombinant method. Several expression systems for β-D-1,4-endoglucanase were designed for use of different cell lines. In this paper, we have constructed a stable expression system for β-D-1,4-endoglucanase gene in Bacillus subtilis 168M. Three main components including the promoter (180 bp) of α–amylase gene from the host strain B. subtilis 168M, the whole open reading frame of β-D-1,4-endoglucanase (1,500 bp) gene from B. amyloliquefacient VLSH08 strain, and the terminator (81 bp) of α–amylase gene from B. licheniformis 3BT2 strain, were reconstructed via megaprimer method. Subsequently, this new reconstitution was ligated into a modified pHT43 vector which was cleaved its own promoter and signal peptide fragment (AmyQ) and transformed into the compotent B. subtilis 168M. The recombinant B. subtilis 168M carrying pHT43[Bspr.endo.Blter] vector showed β-D-1,4-endoglucanase activity at 7 U/ml, 23 times higher than that of the wild type B. amyloliquefacient VLSH08 strain. The successful design and expression of the expression system β-D-1,4-endoglucanase isolated from B. amyloliquefacient strain VLSH08 in pHT43 vector carrying the promoter of the α- amylase gene from B. subtilis strain 168M and the terminator of the α-amylase gene from B. licheniformis strain 3BT2, actively contribute effectively expression of β-D-1,4-endoglucanase for use.

Cloning and expression raw starch digesting amylase gene from Cytophaga sp. in Escherichia coli

2000 ◽  
Vol 28 (5) ◽  
pp. A214-A214
Author(s):  
Chii-Ling Jeang ◽  
Li-Shien Chen ◽  
Ming-Yu Chen ◽  
Rong-Jen Shiau
Keyword(s):  
Escherichia Coli ◽  
Cloning And Expression ◽  
Amylase Gene ◽  
Raw Starch
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