scholarly journals Potential application of cyclic lipopeptide biosurfactants produced by Bacillus subtilis strains in laundry detergent formulations

2007 ◽  
Vol 45 (3) ◽  
pp. 330-335 ◽  
Author(s):  
A.K. Mukherjee
2015 ◽  
Vol 10 (12) ◽  
pp. 1934578X1501001 ◽  
Author(s):  
Da-Le Guo ◽  
Bo Wan ◽  
Shi-Ji Xiao ◽  
Sarah Allen ◽  
Yu-Cheng Gu ◽  
...  

Seven cyclic lipopeptide biosurfactants (1–7) were isolated for the first time from the fermentation broth of endophytic Bacillus clausii DTM1 and were identified as anteisoC13[Val7] surfactin-(L-Glu)-O-methyl-ester (1), anteisoC12[Val7] surfactin (2), anteisoC15[Val7] surfactin (3), isoC14[Leu7] surfactin (4), anteisoC12[Leu7] surfactin (5), nC13[Leu7] surfactin (6), and anteisoC14[Leu7] surfactin-(L-Glu)-O-methyl-ester (7); 1 has not been isolated before as a natural product from any source. Plate-based herbicide and insecticide bioassays showed that all compounds exhibited interesting insecticidal and herbicidal activities.


2009 ◽  
Vol 53 (4) ◽  
pp. 1598-1609 ◽  
Author(s):  
Anna-Barbara Hachmann ◽  
Esther R. Angert ◽  
John D. Helmann

ABSTRACT Daptomycin is the first of a new class of cyclic lipopeptide antibiotics used against multidrug-resistant, gram-positive pathogens. The proposed mechanism of action involves disruption of the functional integrity of the bacterial membrane in a Ca2+-dependent manner. We have used transcriptional profiling to demonstrate that treatment of Bacillus subtilis with daptomycin strongly induces the lia operon including the autoregulatory LiaRS two-component system (homologous to Staphylococcus aureus VraSR). The lia operon protects against daptomycin, and deletion of liaH, encoding a phage-shock protein A (PspA)-like protein, leads to threefold increased susceptibility. Since daptomycin interacts with the membrane, we tested mutants with altered membrane composition for effects on susceptibility. Deletion mutations of mprF (lacking lysyl-phosphatidylglycerol) or des (lipid desaturase) increased daptomycin susceptibility, whereas overexpression of MprF decreased susceptibility. Conversely, depletion of the cell for the anionic lipid phosphatidylglycerol led to increased resistance. Fluorescently labeled daptomycin localized to the septa and in a helical pattern around the cell envelope and was delocalized upon the depletion of phosphatidylglycerol. Together, these results indicate that the daptomycin-Ca2+ complex interacts preferentially with regions enriched in anionic phospholipids and leads to membrane stresses that can be ameliorated by PspA family proteins.


2011 ◽  
Vol 49 (4) ◽  
pp. 603-609 ◽  
Author(s):  
Christopher A. Dunlap ◽  
David A. Schisler ◽  
Neil P. Price ◽  
Steven F. Vaughn

2017 ◽  
Vol 184 (3) ◽  
pp. 838-851 ◽  
Author(s):  
Gabrielly Terassi Bersaneti ◽  
Nicole Caldas Pan ◽  
Cristiani Baldo ◽  
Maria Antonia Pedrine Colabone Celligoi

2012 ◽  
Vol 38 (8) ◽  
pp. 966-974 ◽  
Author(s):  
Lei Li ◽  
MingChuan Ma ◽  
Rong Huang ◽  
Qing Qu ◽  
GuoHong Li ◽  
...  

2019 ◽  
Vol 17 ◽  
pp. 638-646 ◽  
Author(s):  
Tanchanok Poonsin ◽  
Benjamin K. Simpson ◽  
Soottawat Benjakul ◽  
Wonnop Visessanguan ◽  
Asami Yoshida ◽  
...  

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