Using bacterial culture supernatant for extraction of manganese and zinc from waste alkaline button-cell batteries

2019 ◽  
Vol 188 ◽  
pp. 81-91 ◽  
Author(s):  
Mohammad Sadeghi Sadeghabad ◽  
Nazanin Bahaloo-Horeh ◽  
Seyyed Mohammad Mousavi
2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Rafael Nascimento ◽  
Hossein Gouran ◽  
Sandeep Chakraborty ◽  
Hyrum W. Gillespie ◽  
Hebréia O. Almeida-Souza ◽  
...  

Abstract Pierce’s disease (PD) of grapevines is caused by Xylella fastidiosa (Xf), a xylem-limited gamma-proteobacterium that is responsible for several economically important crop diseases. The occlusion of xylem elements and interference with water transport by Xf and its associated biofilm have been posited as the main cause of PD symptom development; however, Xf virulence mechanisms have not been described. Analysis of the Xf secretome revealed a putative lipase/esterase (LesA) that was abundantly secreted in bacterial culture supernatant and was characterized as a protein ortholog of the cell wall-degrading enzyme LipA of Xanthomonas strains. LesA was secreted by Xf and associated with a biofilm filamentous network. Additional proteomic analysis revealed its abundant presence in outer membrane vesicles (OMVs). Accumulation of LesA in leaf regions associated positively with PD symptoms and inversely with bacterial titer. The lipase/esterase also elicited a hypersensitive response in grapevine. Xf lesA mutants were significantly deficient for virulence when mechanically inoculated into grapevines. We propose that Xf pathogenesis is caused by LesA secretion mediated by OMV cargos and that its release and accumulation in leaf margins leads to early stages of observed PD symptoms.


1989 ◽  
Vol 43 (6) ◽  
pp. 1062-1067 ◽  
Author(s):  
John G. Jolley ◽  
Gill G. Geesey ◽  
Michael R. Hankins ◽  
Randy B. Wright ◽  
Paul L. Wichlacz

Thin films (2.0 nm) of copper on germanium internal reflection elements (IREs) were exposed to 10% gum arabic (aqueous solution), 2% alginic acid (aqueous solution), 1% bacterial culture supernatant (BCS, simulated seawater solution), and 0.5% Pseudomonas atlantica exopolymer (simulated seawater solution) and monitored in situ, real time, with the use of Fourier transform infrared/cylindrical internal reflection/attenuated total reflection spectroscopy as a function of time at ambient conditions. Ancillary graphite furnace atomic absorption spectroscopy was used to monitor the removal process of the copper thin film from the germanium IREs. Results indicate that some of the copper was removed from the Cu/Ge interface by all four polymers and incorporated into the polymer matrix. Thus, biocorrosion of copper was exhibited by the four polymers in the order of alginic acid < gum arabic < BCS > Pseudomonas atlantica exopolymer. The FT-IR/CIR/ATR technique can be successfully used to monitor biocorrosion systems in in situ, real-time settings.


2004 ◽  
Vol 70 (1) ◽  
pp. 610-612 ◽  
Author(s):  
Randolph B. Caldwell ◽  
Claus T. Lattemann

ABSTRACT A simple and reliable method for precipitating protein from bacterial culture supernatants based on a pyrogallol red-molybdate-methanol (PRMM) protocol has been developed and applied for the analysis of proteins secreted by a bacterial type III secretion system. PRMM-based precipitation has been shown to be more efficient and robust than are conventional protocols.


Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


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