Mechanism of Bacillus subtilis spore inactivation induced by moderate electric fields

2020 ◽  
Vol 62 ◽  
pp. 102349 ◽  
Author(s):  
Lang-Hong Wang ◽  
Taras Pyatkovskyy ◽  
Ahmed Yousef ◽  
Xin-An Zeng ◽  
Sudhir K. Sastry
Keyword(s):  
Bacillus Subtilis ◽  
Electric Fields ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore

scholarly journals Laccase and Its Mutant Displayed on the Bacillus subtilis Spore Coat for Oxidation of Phenolic Compounds in Organic Solvents

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 606
Author(s):  
Silu Sheng ◽  
Edgardo T. Farinas
Keyword(s):  
Bacillus Subtilis ◽  
Organic Solvents ◽  
Environmental Changes ◽  
Sinapic Acid ◽  
Product Yield ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Cota Laccase ◽  
Inert Surface

Enzymes displayed on the Bacillus subtilis spore coat have several features that are useful for biocatalysis. The enzyme is preimmobilized on an inert surface of the spore coat, which is due to the natural sporulation process. As a result, protein stability can be increased, and they are resistant to environmental changes. Next, they would not lyse under extreme conditions, such as in organic solvents. Furthermore, they can be easily removed from the reaction solution and reused. The laboratory evolved CotA laccase variant T480A-CotA was used to oxidize the following phenolic substrates: (+)-catechin, (−)-epicatechin, and sinapic acid. The kinetic parameters were determined and T480A-CotA had a greater Vmax/Km than wt-CotA for all substrates. The Vmax/Km for T480A-CotA was 4.1, 5.6, and 1.4-fold greater than wt-CotA for (+)-catechin, (−)-epicatechin, and sinapic acid, respectively. The activity of wt-CotA and T480A-CotA was measured at different concentrations from 0–70% in organic solvents (dimethyl sulfoxide, ethanol, methanol, and acetonitrile). The Vmax for T480A-CotA was observed to be greater than the wt-CotA in all organic solvents. Finally, the T480A-CotA was recycled 7 times over a 23-h period and up to 60% activity for (+)-catechin remained. The product yield was up to 3.1-fold greater than the wild-type.

scholarly journals Bactericidal Effect of Peracetic Acid on Bacillus subtilis Spore

1984 ◽  
Vol 25 (2) ◽  
pp. 99-105_1 ◽  
Author(s):  
Michio HAMAMOTO ◽  
Shigetoshi YAMAGUCHI ◽  
Yoshiteru ASAI ◽  
Kousou SHIMODA
Keyword(s):  
Bacillus Subtilis ◽  
Peracetic Acid ◽  
Bactericidal Effect ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore

Display of Bombyx mori Nucleopolyhedrovirus GP64 on the Bacillus subtilis Spore Coat

2011 ◽  
Vol 62 (5) ◽  
pp. 1368-1373 ◽  
Author(s):  
Guohui Li ◽  
Qi Tang ◽  
Huiqing Chen ◽  
Qin Yao ◽  
Degang Ning ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Bombyx Mori ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bombyx Mori Nucleopolyhedrovirus ◽  
Bacillus Subtilis Spore

scholarly journals Assembly of Multiple CotC Forms into the Bacillus subtilis Spore Coat

2004 ◽  
Vol 186 (4) ◽  
pp. 1129-1135 ◽  
Author(s):  
Rachele Isticato ◽  
Giovanni Esposito ◽  
Rita Zilhão ◽  
Sofia Nolasco ◽  
Giuseppina Cangiano ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Posttranslational Modifications ◽  
Mother Cell ◽  
Spore Coat ◽  
Spore Surface ◽  
Subtilis Spore ◽  
Cell Compartment ◽  
Bacillus Subtilis Spore ◽  
Molecular Masses

ABSTRACT We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset of sporulation and were probably assembled on the forming spore immediately after their synthesis, since no accumulation of either of them was detected in the mother cell compartment, where their synthesis occurs. The other two components, 12.5 and 30 kDa, were generated 2 h later and were probably the products of posttranslational modifications of the two early forms occurring directly on the coat surface during spore maturation. None of the CotC forms was found either on the spore coat or in the mother cell compartment of a cotH mutant. This indicates that CotH serves a dual role of stabilizing the early forms of CotC and promoting the assembly of both early and late forms on the spore surface.

scholarly journals Temporal and spatial regulation of protein cross-linking by the pre-assembled substrates of a Bacillus subtilis spore coat transglutaminase

PLoS Genetics ◽  
2019 ◽  
Vol 15 (4) ◽  
pp. e1007912 ◽  
Author(s):  
Catarina G. Fernandes ◽  
Diogo Martins ◽  
Guillem Hernandez ◽  
Ana L. Sousa ◽  
Carolina Freitas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cross Linking ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Spatial Regulation ◽  
Bacillus Subtilis Spore ◽  
Temporal And Spatial ◽  
Protein Cross Linking
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