scholarly journals Disruption of the cell wall lytic enzyme CwlO affects the amount and molecular size of poly-γ-glutamic acid produced by Bacillus subtilis (natto)

2011 ◽  
Vol 57 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Nobuo Mitsui ◽  
Hisashi Murasawa ◽  
Junichi Sekiguchi
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Molecular Size ◽  
Lytic Enzyme ◽  
Bacillus Subtilis Natto

scholarly journals Bacillus subtilis natto: a non-toxic source of poly-γ-glutamic acid that could be used as a cryoprotectant for probiotic bacteria

AMB Express ◽  
2013 ◽  
Vol 3 (1) ◽  
pp. 36 ◽  
Author(s):  
Aditya R Bhat ◽  
Victor U Irorere ◽  
Terry Bartlett ◽  
David Hill ◽  
Gopal Kedia ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Probiotic Bacteria ◽  
Bacillus Subtilis Natto

Inhibition of nattokinase against the production of poly (γ-glutamic Acid) in Bacillus subtilis natto

2020 ◽  
Vol 42 (11) ◽  
pp. 2285-2291
Author(s):  
Li Wang ◽  
Ning Liu ◽  
Chenrui Yu ◽  
Junliu Chen ◽  
Kangjin Hong ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Bacillus Subtilis Natto

scholarly journals Localization of the GerD spore germination protein in the Bacillus subtilis spore

Microbiology ◽  
2009 ◽  
Vol 155 (4) ◽  
pp. 1146-1151 ◽  
Author(s):  
Wiyada Mongkolthanaruk ◽  
Carl Robinson ◽  
Anne Moir
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Germ Cell ◽  
Spore Germination ◽  
Signal Sequence ◽  
Lytic Enzyme ◽  
Western Blots ◽  
Inner Membrane ◽  
Bacillus Subtilis Spore ◽  
High Level

The GerD protein of Bacillus subtilis is required for efficient spore germination in l-alanine, and for germination in the alternative germinant combination of amino acids plus sugars. Only germination via nutrient receptors is affected in the mutant. The GerD protein is predicted to be a lipoprotein that is produced in the forespore compartment of the sporulating cell. Using antibody raised against the GerD protein, Western blots of proteins from spore fractions revealed that, as might be expected, the protein was detected in the inner membrane of spores, but it was also present at a high level in spore integuments (comprising coat, cortex and germ cell wall layers), and to some extent in the soluble fraction. It is likely that the GerD protein in the outer layers of dormant spores is located in the germ cell wall, as it was detected in coat-defective spores, and in the cell wall fraction of cells that were outgrowing from spores. Which of the multiple locations of GerD is important for its function is not known, but the inner membrane association would be appropriate for any interaction with germinant receptor proteins or SleB cortex lytic enzyme. Substitution of alanine for cysteine in the conserved cleavage site of the predicted prelipoprotein signal sequence of GerD resulted in mutant spores that lacked the GerD protein entirely.

Poly-γ-glutamic acid production of Bacillus subtilis (natto) in the absence of DegQ: A gain-of-function mutation in yabJ gene

2019 ◽  
Vol 128 (6) ◽  
pp. 690-696 ◽  
Author(s):  
Le Thi Thu Hong ◽  
Tsuyoshi Hachiya ◽  
Sumitaka Hase ◽  
Yuh Shiwa ◽  
Hirofumi Yoshikawa ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Acid Production ◽  
Gain Of Function ◽  
Bacillus Subtilis Natto ◽  
Glutamic Acid Production

Feasible protein aggregation of phosphorylated poly-γ-glutamic acid derivative from Bacillus subtilis ( natto )

2017 ◽  
Vol 103 ◽  
pp. 484-492 ◽  
Author(s):  
Osamu Kurita ◽  
Toru Sago ◽  
Kaori Umetani ◽  
Yasushi Kokean ◽  
Chizuru Yamaoka ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Protein Aggregation ◽  
Glutamic Acid ◽  
Acid Derivative ◽  
Bacillus Subtilis Natto

scholarly journals Exploring the Potential for Fungal Antagonism and Cell Wall Attack by Bacillus subtilis natto

2020 ◽  
Vol 11 ◽  
Author(s):  
Anna Schönbichler ◽  
Sara M. Díaz-Moreno ◽  
Vaibhav Srivastava ◽  
Lauren Sara McKee
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Bacillus Subtilis Natto ◽  
Fungal Antagonism

Specificity of cell wall labeling with tritiated diaminopimelic acid in Bacillus subtilis

1973 ◽  
Vol 19 (8) ◽  
pp. 1049-1051
Author(s):  
Siegfried Maier
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Diaminopimelic Acid ◽  
Chromatographic Purification ◽  
Membrane Chromatography

The suitability of tritiated 2,6-diaminopimelic acid (3H-DAP) as a label specific for cell walls was explored in Bacillus subtilis BC 102 grown in a medium enriched with 3H-DAP and an excess of L-lysine. Fractionation of labeled cells showed 57% of the activity in the cell wall and 28% in the membrane. Chromatography of labeled wall hydrolysates revealed two activity peaks: 62% in DAP and 29% in glutamic acid – alanine. Labeled membrane was devoid of activity in the DAP position. Chromatographic purification of the 3H-DAP improved specificity, giving 7% of the activity in the membrane and 85% in the wall. In such walls DAP accounted for 82% of the total wall activity. Therefore, only 69% of the total fixed purified 3H label remained with DAP in the wall.

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