Qualitative characterization of the protein fraction of exopolymeric substances (EPS) extracted with EDTA from sludge

2012 ◽  
Vol 104 ◽  
pp. 486-496 ◽  
Author(s):  
Isabelle Bourven ◽  
Guy Costa ◽  
Gilles Guibaud
2019 ◽  
Vol 28 (5) ◽  
pp. 1327-1335 ◽  
Author(s):  
Silvina Patricia Meriles ◽  
Maria Eugenia Steffolani ◽  
Alberto Edel León ◽  
Maria Cecilia Penci ◽  
Pablo Daniel Ribotta

2009 ◽  
Vol 72 (9) ◽  
pp. 1841-1847 ◽  
Author(s):  
SHIN-HEE KIM ◽  
CHENG-I WEI

The molecular mechanism of biofilm formation by Salmonella Typhimuriun DT104 was characterized for a better understanding of its attachment and colonization in food processing environments. A library of random mutagenized clones was screened for phenotypic analyses of their ability to form biofilm, pellicle, curli, and cellulose. The genes identified were involved in lipopolysaccharide synthesis, assembly of flagella, regulation of rRNA biosynthesis, and outer membrane transportation and signaling. The insertion of transposon in flgK, rfbA, nusB, and pnp genes resulted in decreased biofilm formation. Alterations of flagellar and lipopolysaccharide production were confirmed in the flgK mutant and rfbA mutant, respectively. Biofilm formation by these four mutants in meat and poultry broths and their attachment on surfaces of stainless steel and glass were significantly reduced compared with those of the wild-type strain (P < 0.05). On the contrary, the mutation of STM4263 and yjcC genes in Salmonella Typhimuriun DT104 resulted in increased biofilm formation and attachment of the species in tested broths and on contact surfaces. Our findings suggest that many factors, such as production of exopolymeric substances and their efficient transportation through outer membrane, expression of flagella, and regulation of exoribonucleases and RNA-binding protein, could be involved in biofilm formation and attachment of Salmonella Typhimurium DT104 on contact surfaces.


1998 ◽  
Vol 46 (6) ◽  
pp. 2130-2135 ◽  
Author(s):  
Sheikh M. Basha ◽  
M. Ying ◽  
M. R. Vives ◽  
C. T. Young ◽  
L. C. Boyd
Keyword(s):  

1977 ◽  
Vol 164 (1) ◽  
pp. 53-66 ◽  
Author(s):  
S Fujita ◽  
F Ogata ◽  
J Nakamura ◽  
S Omata ◽  
H Sugano

A protein fraction which has a high affinity for polyribosomes was isolated from rough microsomal membranes of rat liver. The mode of polyribosome binding to this fraction (R-fraction) was studied by using CsCl equilibrium centrifugation and compared with that for stripped rough microsomal membranes. The following were found. (1) The polyribosome-binding cpacity of the R-fraction was heat-labile and sensitive to trypsin, and was suppressed by increasing KCl concentration and addition of 0.1 mM-aurintricarboxylic acid. (2) Of the four subfractions obtained by gel filtration of the R-fraction on a Sephadex G-200, only the R1-fraction, eluted at the void volume, showed a high affinity for polyribosomes. The polyribosome-binding capacity of the R1-fraction decreased with time on storage at 4 degrees C. (3) The R1-fraction contained three major proteins with mol. wts. 108,000, 99,000 and 65,000.


Biofouling ◽  
2014 ◽  
Vol 30 (4) ◽  
pp. 501-511 ◽  
Author(s):  
Laura Castro ◽  
Ruiyong Zhang ◽  
Jesús A. Muñoz ◽  
Felisa González ◽  
M. Luisa Blázquez ◽  
...  

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