The polyester polyurethanase gene (<i>pueA</i>) from<i>Pseudomonas chlororaphis</i>encodes a lipase

Stern, Robert V.; Howard, Gary T.

doi:10.1111/j.1574-6968.2000.tb09056.x

Cited by 82 publications

(31 citation statements)

References 13 publications

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“…Many secreted enzymes from fungal and bacterial organisms also possess the ability to degrade PUs of various formulations (4,6,7,(35)(36)(37)(38). Genes that encode enzymes capable of degrading PU ex vivo from some of these organisms have also been identified and cloned (5,9,11). Comparison of these gene sequences revealed that the gene products from these diverse organisms all contain a lipase domain and are predicted to be secreted.…”

Section: Discussionmentioning

confidence: 99%

“…Several Pseudomonas species including Pseudomonas chlororaphis, Pseudomonas aeruginosa, and Pseudomonas fluorescens have been shown to degrade a model polyester PU, Impranil DLN (Impranil) (4)(5)(6). Three PU-degrading enzymes have been purified and characterized from some of these strains, including polyurethane esterases A (PueA) and B (PueB) from Pseudomonas chlororaphis (5,9) and polyurethane lipase (PulA) from P. fluorescens (5,(9)(10)(11). Although they are often referred to as "polyurethanases," these enzymes are more accurately classified as extracellular lipases and esterases.…”

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confidence: 99%

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Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

Hung

Zingarelli

Nadeau

et al. 2016

Appl Environ Microbiol

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Polyester polyurethane (PU) coatings are widely used to help protect underlying structural surfaces but are susceptible to biological degradation. PUs are susceptible to degradation by Pseudomonas species, due in part to the degradative activity of secreted hydrolytic enzymes. Microorganisms often respond to environmental cues by secreting enzymes or secondary metabolites to benefit their survival. This study investigated the impact of exposing several Pseudomonas strains to select carbon sources on the degradation of the colloidal polyester polyurethane Impranil DLN (Impranil). The prototypic Pseudomonas protegens strain Pf-5 exhibited Impranil-degrading activities when grown in sodium citrate but not in glucose-containing medium. Glucose also inhibited the induction of Impranil-degrading activity by citrate-fed Pf-5 in a dose-dependent manner. Biochemical and mutational analyses identified two extracellular lipases present in the Pf-5 culture supernatant (PueA and PueB) that were involved in degradation of Impranil. Deletion of the pueA gene reduced Impranil-clearing activities, while pueB deletion exhibited little effect. Removal of both genes was necessary to stop degradation of the polyurethane. Bioinformatic analysis showed that putative Cbr/Hfq/Crc-mediated regulatory elements were present in the intergenic sequences upstream of both pueA and pueB genes. Our results confirmed that both PueA and PueB extracellular enzymes act in concert to degrade Impranil. Furthermore, our data showed that carbon sources in the growth medium directly affected the levels of Impranil-degrading activity but that carbon source effects varied among Pseudomonas strains. This study uncovered an intricate and complicated regulation of P. protegens PU degradation activity controlled by carbon catabolite repression. IMPORTANCEPolyurethane (PU) coatings are commonly used to protect metals from corrosion. Microbiologically induced PU degradation might pose a substantial problem for the integrity of these coatings. Microorganisms from diverse genera, including pseudomonads, possess the ability to degrade PUs via various means. This work identified two extracellular lipases, PueA and PueB, secreted by P. protegens strain Pf-5, to be responsible for the degradation of a colloidal polyester PU, Impranil. This study also revealed that the expression of the degradative activity by strain Pf-5 is controlled by glucose carbon catabolite repression. Furthermore, this study showed that the Impranil-degrading activity of many other Pseudomonas strains could be influenced by different carbon sources. This work shed light on the carbon source regulation of PU degradation activity among pseudomonads and identified the polyurethane lipases in P. protegens.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

Hung

Zingarelli

Nadeau

et al. 2016

Appl Environ Microbiol

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“…All the purified serine hydrolases above have the same hydrolytic capacity to emulsify polyester PUR. In addition, they also cloned a gene named pulA from Pseudomonas fluorescens and two genes, pueA and pueB, from Pseudomonas chlororaphis (Stern and Howard, 2000;Howard et al, 2001b). These genes encoded three different esterases involved in the microbial degradation of emulsified polyester PUR by Pseudomonas fluorescens and Pseudomonas chlororaphis.…”

Section: Purmentioning

confidence: 99%

Microbial Degradation and Valorization of Plastic Wastes

2020

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“…strains MIS38 and KB700A (Amada et al , 2000; Rashid et al , 2001;). The polyester polyurethanases PueA and PueB of Pseudomonas chlororaphis are also classified as lipases (Stern & Howard, 2000). …”

Section: Classes Of Rtx Proteinsmentioning

confidence: 99%

RTX proteins: a highly diverse family secreted by a common mechanism

et al. 2010

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Repeats-in-toxin (RTX) exoproteins of Gram-negative bacteria form a steadily growing family of proteins with diverse biological functions. Their common feature is the unique mode of export across the bacterial envelope via the type I secretion system and the characteristic, typically nonapeptide, glycine- and aspartate-rich repeats binding Ca2+ ions. In this review, we summarize the current state of knowledge on the organization of rtx loci and on the biological and biochemical activities of therein encoded proteins. Applying several types of bioinformatic screens on the steadily growing set of sequenced bacterial genomes, over 1000 RTX family members were detected, with the biological functions of most of them remaining to be characterized. Activities of the so far characterized RTX family members are then discussed and classified according to functional categories, ranging from the historically first characterized pore-forming RTX leukotoxins, through the large multifunctional enzymatic toxins, bacteriocins, nodulation proteins, surface layer proteins, up to secreted hydrolytic enzymes exhibiting metalloprotease or lipase activities of industrial interest.

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The polyester polyurethanase gene (pueA) fromPseudomonas chlororaphisencodes a lipase

Cited by 82 publications

References 13 publications

Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

Microbial Degradation and Valorization of Plastic Wastes

RTX proteins: a highly diverse family secreted by a common mechanism

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