Purification and biochemical characterization of a thermostable, alkaliphilic, extracellular α-amylase from Bacillus subtilis DM-03, a strain isolated from the traditional fermented food of India

2004 ◽  
Vol 40 (3) ◽  
pp. 291 ◽  
Author(s):  
Robin Doley ◽  
Kishore Das ◽  
Ashis Kumar Mukherjee
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Fermented Food ◽  
Traditional Fermented Food

Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis

2017 ◽  
Vol 74 (12) ◽  
pp. 2319-2332 ◽  
Author(s):  
Meriem El Ghachi ◽  
Nicole Howe ◽  
Rodolphe Auger ◽  
Alexandre Lambion ◽  
Annick Guiseppi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Biochemical Characterization

Structural and biochemical characterization of SpoIIIAF, a component of a sporulation-essential channel in Bacillus subtilis

2018 ◽  
Vol 204 (1) ◽  
pp. 1-8 ◽  
Author(s):  
N. Zeytuni ◽  
K.A. Flanagan ◽  
L.J. Worrall ◽  
S.C. Massoni ◽  
A.H. Camp ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization

Isolation and characterization of lactic acid bacteria from pobuzihi (fermented cummingcordia), a traditional fermented food in Taiwan

2012 ◽  
Vol 58 (2) ◽  
pp. 103-109 ◽  
Author(s):  
Yi-sheng Chen ◽  
Hui-chung Wu ◽  
Chiung-mei Wang ◽  
Chia-chun Lin ◽  
Yi-ting Chen ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Fermented Food ◽  
Isolation And Characterization ◽  
Traditional Fermented Food

scholarly journals Biochemical Characterization of the C4-Dicarboxylate Transporter DctA from Bacillus subtilis

2010 ◽  
Vol 192 (11) ◽  
pp. 2900-2907 ◽  
Author(s):  
Maarten Groeneveld ◽  
Ruud G. J. Detert Oude Weme ◽  
Ria H. Duurkens ◽  
Dirk Jan Slotboom
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Krebs Cycle ◽  
Membrane Vesicles ◽  
Positive Bacterium ◽  
Proton Symport ◽  
Negative Membrane Potential ◽  
Isolated Membrane Vesicles

ABSTRACT Bacterial secondary transporters of the DctA family mediate ion-coupled uptake of C4-dicarboxylates. Here, we have expressed the DctA homologue from Bacillus subtilis in the Gram-positive bacterium Lactococcus lactis. Transport of dicarboxylates in vitro in isolated membrane vesicles was assayed. We determined the substrate specificity, the type of cotransported ions, the electrogenic nature of transport, and the pH and temperature dependence patterns. DctA was found to catalyze proton-coupled symport of the four C4-dicarboxylates from the Krebs cycle (succinate, fumurate, malate, and oxaloacetate) but not of other mono- and dicarboxylates. Because (i) succinate-proton symport was electrogenic (stimulated by an internal negative membrane potential) and (ii) the divalent anionic form of succinate was recognized by DctA, at least three protons must be cotransported with succinate. The results were interpreted in the light of the crystal structure of the homologous aspartate transporter GltPh from Pyrococcus horikoshii.

Biochemical characterization of unusual meso-2,3-butanediol dehydrogenase from a strain of Bacillus subtilis

2014 ◽  
Vol 109 ◽  
pp. 184-190 ◽  
Author(s):  
Wenbo Hao ◽  
Fangling Ji ◽  
Jingyun Wang ◽  
Yue Zhang ◽  
Tianqi Wang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Butanediol Dehydrogenase
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