Enhanced biodegradation of hydrocarbons by Pseudomonas aeruginosa-encapsulated alginate/gellan gum microbeads

2021 ◽  
Vol 406 ◽  
pp. 124752
Author(s):  
Hyejoo Park ◽  
Hyojeon Kim ◽  
Ga-Yeong Kim ◽  
Mi-Young Lee ◽  
Young Kim ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Gellan Gum ◽  
Enhanced Biodegradation

scholarly journals Use of Alternative Gelling Agents Reveals the Role of Rhamnolipids in Pseudomonas aeruginosa Surface Motility

Biomolecules ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1468
Author(s):  
Charles D. Morin ◽  
Eric Déziel
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Strong Dependence ◽  
Gellan Gum ◽  
Gelling Agent ◽  
Gelling Agents ◽  
Bacterial Surface ◽  
Solid Media ◽  
Surface Motility ◽  
Wetting Agents ◽  
The Impact

Pseudomonas aeruginosa is a motile bacterium able to exhibit a social surface behaviour known as swarming motility. Swarming requires the polar flagellum of P. aeruginosa as well as the secretion of wetting agents to ease the spread across the surface. However, our knowledge on swarming is limited to observed phenotypes on agar-solidified media. To study the surface behaviour and the impact of wetting agents of P. aeruginosa on other surfaces, we assessed surface motility capabilities of the prototypical strain PA14 on semi-solid media solidified with alternative gelling agents, gellan gum and carrageenan. We found that, on these alternative surfaces, the characteristic dendritic spreading pattern of P. aeruginosa is drastically altered. One striking feature is the loss of dependence on rhamnolipids to spread effectively on plates solidified with these alternative gelling agents. Indeed, a rhlA-null mutant unable to produce its wetting agents still spreads effectively, albeit in a circular shape on both the gellan gum- and carrageenan-based media. Our data indicate that rhamnolipids do not have such a crucial role in achieving surface colonization of non-agar plates, suggesting a strong dependence on the physical properties of the tested surface. The use of alternative gelling agent provides new means to reveal unknown features of bacterial surface behaviour.

Molecularly imprinted nanofiber membranes enhanced biodegradation of trace bisphenol A by Pseudomonas aeruginosa

2015 ◽  
Vol 262 ◽  
pp. 989-998 ◽  
Author(s):  
Fei Liu ◽  
Qian Liu ◽  
Yanhong Zhang ◽  
Yanjie Liu ◽  
Yingchun Wan ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bisphenol A ◽  
Molecularly Imprinted ◽  
Enhanced Biodegradation ◽  
Nanofiber Membranes

scholarly journals Identification of the pgmG Gene, Encoding a Bifunctional Protein with Phosphoglucomutase and Phosphomannomutase Activities, in the Gellan Gum-Producing Strain Sphingomonas paucimobilis ATCC 31461

2000 ◽  
Vol 66 (5) ◽  
pp. 2252-2258 ◽  
Author(s):  
Paula A. Videira ◽  
Luísa L. Cortes ◽  
Arsénio M. Fialho ◽  
Isabel Sá-Correia
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Catalytic Efficiency ◽  
Gellan Gum ◽  
Sphingomonas Paucimobilis ◽  
Gene Encoding ◽  
Bifunctional Protein ◽  
Gram Negative ◽  
Marked Preference ◽  
Bifunctional Proteins ◽  
Alginate Biosynthesis

ABSTRACT The pgmG gene of Sphingomonas paucimobilisATCC 31461, the industrial gellan gum-producing strain, was cloned and sequenced. It encodes a 50,059-Da polypeptide that has phosphoglucomutase (PGM) and phosphomannomutase (PMM) activities and is 37 to 59% identical to other bifunctional proteins with PGM and PMM activities from gram-negative species, includingPseudomonas aeruginosa AlgC. Purified PgmG protein showed a marked preference for glucose-1-phosphate (G1P); the catalytic efficiency was about 50-fold higher for G1P than it was for mannose-1-phosphate (M1P). The estimated apparentKm values for G1P and M1P were high, 0.33 and 1.27 mM, respectively. The pgmG gene allowed the recovery of alginate biosynthetic ability in a P. aeruginosa mutant with a defective algC gene. This result indicates that PgmG protein can convert mannose-6-phosphate into M1P in the initial steps of alginate biosynthesis and, together with other results, suggests that PgmG may convert glucose-6-phosphate into G1P in the gellan pathway.

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