Enhanced biodegradation of n-Hexadecane in solid-phase of soil by employing immobilized Pseudomonas Aeruginosa on size-optimized coconut fibers

2020 ◽  
Vol 389 ◽  
pp. 122134
Author(s):  
Mahdiyeh Hajieghrari ◽  
Parisa Hejazi
1998 ◽  
Vol 44 (3) ◽  
pp. 307-311 ◽  
Author(s):  
Frank Schweizer ◽  
Hailong Jiao ◽  
Ole Hindsgaul ◽  
Wah Y Wong ◽  
Randall T Irvin

Pseudomonas aeruginosa employs pili to mediate adherence to epithelial cell surface receptors. Previously, it has been shown that the pilus adhesin of P. aeruginosa PAK binds to the ganglioside asialo-GM1. In particular, it was found that the carbohydrate sequence β-D-GalNAc(1->4) β-D-Gal is the minimal carbohydrate receptor sequence of asialo-GM1. To study the binding specificity of P. aeruginosa, O-modified and N-modified sugar analogs, where each hydroxyl group was substituted either by O-methyl or O-propyl and the acetamido group was changed to a propionamido group, were synthesized. The sugar analogs were evaluated as inhibitors in a competitive solid phase binding assay. The results demonstrate that the pili of P. aeruginosa PAK accepts a variety of sugar analogs possessing the sequence β-D-GalNAc(1->4) β-D-Gal. Most sugar analogs bind with a similar order of magnitude (50% inhibitory concentration (IC50) = 60-130 μM) except for the 2-O-propyl derivative 7 (IC50 = 8 ± 4 μM) compared with an IC50 of 79 ± 18 μM for the native compound. The significant increase in binding affinity of 2-O-propyl derivative 7 suggests that improved inhibitors of adhesion may be prepared by introducing a hydrophobic side chain at the 2-position of galactose.Key words: Pseudomonas aeruginosa, pili, adhesion, carbohydrate.


2015 ◽  
Vol 262 ◽  
pp. 989-998 ◽  
Author(s):  
Fei Liu ◽  
Qian Liu ◽  
Yanhong Zhang ◽  
Yanjie Liu ◽  
Yingchun Wan ◽  
...  

Cosmetics ◽  
2020 ◽  
Vol 7 (2) ◽  
pp. 38
Author(s):  
Maria Celeiro ◽  
Esther Varela ◽  
Rocio Rodriguez ◽  
Manuel Penedo ◽  
Marta Lores

The main goal of this work was the use of the powerful solid-phase microextraction-gas chromatography-mass spectrometry (SPME-GC-MS) technique to unequivocally identify microbial volatile organic compounds (MVOCs) derived from the enzymatic activity produced during metabolic processes using analytical profile index (API) biochemical tests. Three bacteria were selected for this study: Escherichia coli, Proteus mirabilis, and Pseudomonas aeruginosa. They were inoculated and incubated to both API components and real cosmetics, as well as to a mixture of them. Specific MVOCs were successfully identified as biomarkers for each one of the studied microorganisms: Indole and 2-nitrophenol as Escherichia coli markers, 2-undecanone and phenylethyl alcohol as Proteus mirabilis-specific markers, and 1-undecene and 2′-aminoacetophenone as Pseudomonas aeruginosa ones. In addition, a high number of MVOCs were identified as general markers of bacterial presence. The results revealed that the MVOCs’ formation is highly subtract dependent. Therefore, the ultimate and most challenging objective is to establish a relationship between the identified MVOCs and the original compound present in the substrate. This work establishes the design and development of this original approach, and its practical application to the control of microbial contamination in real cosmetic samples.


Antibiotics ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 566 ◽  
Author(s):  
Malgorzata Anna Paduszynska ◽  
Katarzyna Ewa Greber ◽  
Wojciech Paduszynski ◽  
Wieslaw Sawicki ◽  
Wojciech Kamysz

The formation of biofilms on biomaterials causes biofilm-associated infections. Available treatments often fail to fight the microorganisms in the biofilm, creating serious risks for patient well-being and life. Due to their significant antibiofilm activities, antimicrobial peptides are being intensively investigated in this regard. A promising approach is a combination therapy that aims to increase the efficacy and broaden the spectrum of antibiotics. The main goal of this study was to evaluate the antimicrobial efficacy of temporin A and the short lipopeptides (C10)2-KKKK-NH2 and (C12)2-KKKK-NH2 in combination with gentamicin against biofilm formed by Staphylococcus aureus (SA) and Pseudomonas aeruginosa (PA). Peptides were synthesized with solid-phase temperature-assisted synthesis methodology. The minimum inhibitory concentrations (MICs), fractional inhibitory concentrations (FICs), minimum biofilm eradication concentrations (MBECs), and the influence of combinations of compounds with gentamicin on bacterial biofilm were determined for reference strains of SA (ATCC 25923) and PA (ATCC 9027). The peptides exhibited significant potential to enhance the antibacterial activity of gentamicin against SA biofilm, but there was no synergy in activity against planktonic cells. The antibiotic applied alone demonstrated strong activity against planktonic cells and poor effectiveness against SA biofilm. Biofilm formed by PA was much more sensitive to gentamicin, but some positive influences of supplementation with peptides were noticed. The results of the performed experiments suggest that the potential application of peptides as adjuvant agents in the treatment of biofilm-associated infections should be studied further.


2020 ◽  
Vol 22 (4) ◽  
pp. 805-810
Author(s):  
A. V. Soldatenkova ◽  
A. M. Kudryashova ◽  
N. F. Gavrilova ◽  
I. V. Yakovleva ◽  
O. V. Borisova ◽  
...  

A hybrid recombinant protein containing the amino  acid sequences of the three  most significant Pseudomonas aeruginosa antigens  (membrane proteins OprF, OprI  and toxoid  aTox)  was incorporated into a vaccine against Pseudomonas infection. Quality control of a hybrid recombinant protein and appropriate vaccine includes  determination of authentity and completeness of adsorption upon aluminum hydroxide adjuvant. The aim of our study was to develop  techniques of quality  control for a vaccine  based on the hybrid  OprF-aToxOprI  recombinant protein specific  to  P. aeruginosa.  Hybridomas secreting  specific  monoclonal antibodies for OprF-aTox-OprI were derived  from the fusion of myeloma cells and murine spleen  cells immunized with recombinant proteins P. aeruginosa. To  produce sufficient  quantities of antibodies, the  hybrid  cells were in vivo cultured in BALB/c mice.  Supernates and ascite liquids were chromatographically purified  with immune sorbent. Conjugation of antibodies with  horseradish peroxidase was carried  out  according to  P.K.Nakane. The  hybrid  OprF-aTox-OprI recombinant protein was detected by the  solid-phase ELISA, using a panel  of monoclonal antibodies and  conjugates of monoclonal antibodies with  horseradish peroxidase. Monoclonal antibodies were specific for different  OprF-aTox-OprI epitopes. Titration assays containing OprF-aTox-OprI protein at 78 ng/ml to 5000 ng/ml were used as quantitative standards for calibration curves.To identify  the recombinant protein OprF-aTox-OprI, 55 variants  of of MAb pairs were tested.  Limits  of quantitative detection served  for selection of most  sensitive  and  specific  ELISA  variants.  The  quantitative detection limit was calculated for all 11 ELISA  variants.  Two ELISA  variants  with the highest  sensitivity were selected  for  quality  control of the  hybrid  recombinant protein. The  limits  of quantitative detection were, respectively, 2.9 and 13.6 ng/ml (0.0058  and 0.027% of the estimated antigen  content in the vaccine)  for the first and  second  ELISA  variants.  The  first variant  included a pair  of monoclonal antibodies specific  for the OprF  and OprI  epitopes, the second  variant  represented aTox and OprI  epitopes. Two variants  of ELISA  were developed to detect  the hybrid recombinant OprF-aTox-OprI protein. The first variant allows to determine the protein amount and to evaluate completeness of its adsorption on aluminum hydroxide. To confirm authenticity of the protein, both methods must be used, since they can detect all three antigens (OprF, aTox and OprI) which are present  in the fusion protein.


1979 ◽  
Vol 9 (2) ◽  
pp. 253-258
Author(s):  
R B Kohler ◽  
L J Wheat ◽  
A White

A solid-phase radioimmunoassay designed to detect serotype 6 Pseudomonas aeruginosa antigens was evaluated for its ability to rapidly diagnose urinary tract infections. Twelve P. aeruginosa serotypes were easily differentiated in the assay from eight other gram-negative bacterial species. During log-phase growth, the assay detected antigens in culture when approximately 10(6) or more serotype 6 P. aeruginosa organisms were present. Both cell-associated and solubilized antigens were detected. The assay detected antigens in 13 of 17 urine specimens which grew greater than 10(5) P. aeruginosa, 3 of 38 which grew other gram-negative rods, and none of 83 with no growth. Two of the three positive specimens from the other gram-negative rod group probably also contained P. aeruginosa. No preincubation of the urine specimens was required, and results were available within 2.5 h. The assay represents an improvement over other procedures for rapidly diagnosing urinary tract infections in that it allows diagnosis by species and should be adaptable to semiautomation.


2021 ◽  
Vol 406 ◽  
pp. 124752
Author(s):  
Hyejoo Park ◽  
Hyojeon Kim ◽  
Ga-Yeong Kim ◽  
Mi-Young Lee ◽  
Young Kim ◽  
...  

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