scholarly journals Biodegradation of Polyester Polyurethane by Endophytic Fungi

2011 ◽  
Vol 77 (17) ◽  
pp. 6076-6084 ◽  
Author(s):  
Jonathan R. Russell ◽  
Jeffrey Huang ◽  
Pria Anand ◽  
Kaury Kucera ◽  
Amanda G. Sandoval ◽  
...  
Keyword(s):  
Carbon Source ◽  
Endophytic Fungi ◽  
Sole Carbon Source ◽  
Anaerobic Growth ◽  
Serine Hydrolase ◽  
Microbial World ◽  
Content Type ◽  
Metabolic Properties ◽  
Liquid Suspensions ◽  
Promising Source

ABSTRACTBioremediation is an important approach to waste reduction that relies on biological processes to break down a variety of pollutants. This is made possible by the vast metabolic diversity of the microbial world. To explore this diversity for the breakdown of plastic, we screened several dozen endophytic fungi for their ability to degrade the synthetic polymer polyester polyurethane (PUR). Several organisms demonstrated the ability to efficiently degrade PUR in both solid and liquid suspensions. Particularly robust activity was observed among several isolates in the genusPestalotiopsis, although it was not a universal feature of this genus. TwoPestalotiopsis microsporaisolates were uniquely able to grow on PUR as the sole carbon source under both aerobic and anaerobic conditions. Molecular characterization of this activity suggests that a serine hydrolase is responsible for degradation of PUR. The broad distribution of activity observed and the unprecedented case of anaerobic growth using PUR as the sole carbon source suggest that endophytes are a promising source of biodiversity from which to screen for metabolic properties useful for bioremediation.

scholarly journals Engineered Pentafunctional Minicellulosome for Simultaneous Saccharification and Ethanol Fermentation in Saccharomyces cerevisiae

2014 ◽  
Vol 80 (21) ◽  
pp. 6677-6684 ◽  
Author(s):  
Youyun Liang ◽  
Tong Si ◽  
Ee Lui Ang ◽  
Huimin Zhao
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Carbon Source ◽  
Phosphoric Acid ◽  
Sole Carbon Source ◽  
Consolidated Bioprocessing ◽  
Content Type ◽  
Yeast Strains ◽  
Recombinant Yeast Strain ◽  
Polysaccharide Monooxygenases ◽  
Simultaneous Saccharification

ABSTRACTSeveral yeast strains have been engineered to express different cellulases to achieve simultaneous saccharification and fermentation of lignocellulosic materials. However, successes in these endeavors were modest, as demonstrated by the relatively low ethanol titers and the limited ability of the engineered yeast strains to grow using cellulosic materials as the sole carbon source. Recently, substantial enhancements to the breakdown of cellulosic substrates have been observed when lytic polysaccharide monooxygenases (LPMOs) were added to traditional cellulase cocktails. LPMOs are reported to cleave cellulose oxidatively in the presence of enzymatic electron donors such as cellobiose dehydrogenases. In this study, we coexpressed LPMOs and cellobiose dehydrogenases with cellobiohydrolases, endoglucanases, and β-glucosidases inSaccharomyces cerevisiae. These enzymes were secreted and docked onto surface-displayed miniscaffoldins through cohesin-dockerin interaction to generate pentafunctional minicellulosomes. The enzymes on the miniscaffoldins acted synergistically to boost the degradation of phosphoric acid swollen cellulose and increased the ethanol titers from our previously achieved levels of 1.8 to 2.7 g/liter. In addition, the newly developed recombinant yeast strain was also able to grow using phosphoric acid swollen cellulose as the sole carbon source. The results demonstrate the promise of the pentafunctional minicellulosomes for consolidated bioprocessing by yeast.

scholarly journals Genome Sequence of Bacillus megaterium O1, a Saponin-Degrading Bacterium

2020 ◽  
Vol 9 (40) ◽  
Author(s):  
Cassandra E. Overney ◽  
Jean J. Huang
Keyword(s):  
Carbon Source ◽  
Genome Sequence ◽  
Bacillus Megaterium ◽  
Sole Carbon Source ◽  
Draft Genome ◽  
Draft Genome Sequence ◽  
Content Type ◽  
Degrading Bacterium ◽  
Sapindus Saponaria ◽  
Insight Into

ABSTRACT Bacillus megaterium strain O1 was isolated from a soapnut (Sapindus saponaria) surface and degrades Quillaja saponin as a sole carbon source. We report the draft genome sequence of B. megaterium O1, which has an estimated size of 5.1 Mb. Study of this isolate will provide insight into mechanisms of saponin degradation.

scholarly journals Oxadiazoles Have Butyrate-Specific Conditional Activity against Mycobacterium tuberculosis

2016 ◽  
Vol 60 (6) ◽  
pp. 3608-3616 ◽  
Author(s):  
Julie V. Early ◽  
Allen Casey ◽  
Maria Angeles Martinez-Grau ◽  
Isabel C. Gonzalez Valcarcel ◽  
Michal Vieth ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Carbon Source ◽  
Mammalian Cells ◽  
Sole Carbon Source ◽  
Specific Activity ◽  
Antitubercular Activity ◽  
Content Type ◽  
Phenotypic Screen

Mycobacterium tuberculosisis a global pathogen of huge importance which can adapt to several host niche environments in which carbon source availability is likely to vary. We developed and ran a phenotypic screen using butyrate as the sole carbon source to be more reflective of the host lung environment. We screened a library of ∼87,000 small compounds and identified compounds which demonstrated good antitubercular activity againstM. tuberculosisgrown with butyrate but not with glucose as the carbon source. Among the hits, we identified an oxadiazole series (six compounds) which had specific activity againstM. tuberculosisbut which lacked cytotoxicity against mammalian cells.

scholarly journals Genetically Modified Strains of Ralstonia eutropha H16 with β-Ketothiolase Gene Deletions for Production of Copolyesters with Defined 3-Hydroxyvaleric Acid Contents

2012 ◽  
Vol 78 (15) ◽  
pp. 5375-5383 ◽  
Author(s):  
Nicole Lindenkamp ◽  
Elena Volodina ◽  
Alexander Steinbüchel
Keyword(s):  
Fatty Acids ◽  
Carbon Source ◽  
Sole Carbon Source ◽  
Ralstonia Eutropha ◽  
Carbon Sources ◽  
Production Capacity ◽  
Wild Type ◽  
Content Type ◽  
Storage Behavior ◽  
Copolymer Poly

ABSTRACTβ-Ketothiolases catalyze the first step of poly(3-hydroxybutyrate) [poly(3HB)] biosynthesis in bacteria by condensation of two acetyl coenzyme A (acetyl-CoA) molecules to acetoacetyl-CoA and also take part in the degradation of fatty acids. During growth on propionate or valerate,Ralstonia eutrophaH16 produces the copolymer poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [poly(3HB-co-3HV)]. InR. eutropha, 15 β-ketothiolase homologues exist. The synthesis of 3-hydroxybutyryl-CoA (3HB-CoA) could be significantly reduced in an 8-fold mutant (Lindenkamp et al., Appl. Environ. Microbiol. 76:5373–5382, 2010). In this study, a 9-fold mutant deficient in nine β-ketothiolase gene homologues (phaA,bktB, H16_A1713, H16_B1771, H16_A1528, H16_B0381, H16_B1369, H16_A0170, andpcaF) was generated. In order to examine the polyhydroxyalkanoate production capacity when short- or long-chain and even- or odd-chain-length fatty acids were provided as carbon sources, the growth and storage behavior of several mutants from the previous study and the newly generated 9-fold mutant were analyzed. Propionate, valerate, octanoate, undecanoic acid, or oleate was chosen as the sole carbon source. On octanoate, no significant differences in growth or storage behavior were observed between wild-typeR. eutrophaand the mutants. In contrast, during the growth on oleate of a multiple mutant lackingphaA,bktB, and H16_A0170, diminished poly(3HB) accumulation occurred. Surprisingly, the amount of accumulated poly(3HB) in the multiple mutants grown on gluconate differed; it was much lower than that on oleate. The β-ketothiolase activity toward acetoacetyl-CoA in H16ΔphaAand all the multiple mutants remained 10-fold lower than the activity of the wild type, regardless of which carbon source, oleate or gluconate, was employed. During growth on valerate as a sole carbon source, the 9-fold mutant accumulated almost a poly(3-hydroxyvalerate) [poly(3HV)] homopolyester with 99 mol% 3HV constituents.

scholarly journals Biodegradation of the Organic Disulfide 4,4′-Dithiodibutyric Acid by Rhodococcus spp.

2015 ◽  
Vol 81 (24) ◽  
pp. 8294-8306 ◽  
Author(s):  
Heba Khairy ◽  
Jan Hendrik Wübbeler ◽  
Alexander Steinbüchel
Keyword(s):  
Carbon Source ◽  
Sole Carbon Source ◽  
Rhodococcus Erythropolis ◽  
Model Organism ◽  
Hypothetical Protein ◽  
Gene Encoding ◽  
Content Type ◽  
Gene Coding ◽  
Initial Cleavage ◽  
Genes Encoding

ABSTRACTFourRhodococcusspp. exhibited the ability to use 4,4′-dithiodibutyric acid (DTDB) as a sole carbon source for growth. The most important step for the production of a novel polythioester (PTE) using DTDB as a precursor substrate is the initial cleavage of DTDB. Thus, identification of the enzyme responsible for this step was mandatory. BecauseRhodococcus erythropolisstrain MI2 serves as a model organism for elucidation of the biodegradation of DTDB, it was used to identify the genes encoding the enzymes involved in DTDB utilization. To identify these genes, transposon mutagenesis ofR. erythropolisMI2 was carried out using transposon pTNR-TA. Among 3,261 mutants screened, 8 showed no growth with DTDB as the sole carbon source. In five mutants, the insertion locus was mapped either within a gene coding for a polysaccharide deacetyltransferase, a putative ATPase, or an acetyl coenzyme A transferase, 1 bp upstream of a gene coding for a putative methylase, or 176 bp downstream of a gene coding for a putative kinase. In another mutant, the insertion was localized between genes encoding a putative transcriptional regulator of the TetR family (noxR) and an NADH:flavin oxidoreductase (nox). Moreover, in two other mutants, the insertion loci were mapped within a gene encoding a hypothetical protein in the vicinity ofnoxRandnox. The interruption mutant generated,R. erythropolisMI2noxΩtsr, was unable to grow with DTDB as the sole carbon source. Subsequently,noxwas overexpressed and purified, and its activity with DTDB was measured. The specific enzyme activity of Nox amounted to 1.2 ± 0.15 U/mg. Therefore, we propose that Nox is responsible for the initial cleavage of DTDB into 2 molecules of 4-mercaptobutyric acid (4MB).

scholarly journals Alginate Lyases from Alginate-Degrading Vibrio splendidus 12B01 Are Endolytic

2015 ◽  
Vol 81 (5) ◽  
pp. 1865-1873 ◽  
Author(s):  
Ahmet H. Badur ◽  
Sujit Sadashiv Jagtap ◽  
Geethika Yalamanchili ◽  
Jung-Kul Lee ◽  
Huimin Zhao ◽  
...  
Keyword(s):  
Carbon Source ◽  
Marine Environment ◽  
Sole Carbon Source ◽  
Vibrio Splendidus ◽  
Turnover Number ◽  
Content Type ◽  
Marine Bacterioplankton ◽  
Polysaccharide Lyase ◽  
Optimal Activity ◽  
Alginate Lyases

ABSTRACTAlginate lyases are enzymes that degrade alginate through β-elimination of the glycosidic bond into smaller oligomers. We investigated the alginate lyases fromVibrio splendidus12B01, a marine bacterioplankton species that can grow on alginate as its sole carbon source. We identified, purified, and characterized four polysaccharide lyase family 7 alginates lyases, AlyA, AlyB, AlyD, and AlyE, fromV. splendidus12B01. The four lyases were found to have optimal activity between pH 7.5 and 8.5 and at 20 to 25°C, consistent with their use in a marine environment. AlyA, AlyB, AlyD, and AlyE were found to exhibit a turnover number (kcat) for alginate of 0.60 ± 0.02 s−1, 3.7 ± 0.3 s−1, 4.5 ± 0.5 s−1, and 7.1 ± 0.2 s−1, respectively. TheKmvalues of AlyA, AlyB, AlyD, and AlyE toward alginate were 36 ± 7 μM, 22 ± 5 μM, 60 ± 2 μM, and 123 ± 6 μM, respectively. AlyA and AlyB were found principally to cleave the β-1,4 bonds between β-d-mannuronate and α-l-guluronate and subunits; AlyD and AlyE were found to principally cleave the α-1,4 bonds involving α-l-guluronate subunits. The four alginate lyases degrade alginate into longer chains of oligomers.

scholarly journals The Foliar Endophyte Phialocephala scopiformis DAOMC 229536 Proteome When Grown on Wood Used as the Sole Carbon Source

2019 ◽  
Vol 8 (6) ◽  
Author(s):  
Jennifer M. Bhatnagar ◽  
Grzegorz Sabat ◽  
Daniel Cullen
Keyword(s):  
Mass Spectrometry ◽  
Carbon Source ◽  
Pinus Contorta ◽  
Sole Carbon Source ◽  
Content Type ◽  
Source Mass ◽  
Conifer Needle

The conifer needle endophyte Phialocephala scopiformis DAOMC 229536 was cultivated in medium containing ground Pinus contorta wood as the sole carbon source. Mass spectrometry analyses identified 590 proteins.

scholarly journals Complete Genome Sequence of Acinetobacter calcoaceticus CA16, a Bacterium Capable of Degrading Diesel and Lignin

2017 ◽  
Vol 5 (24) ◽  
Author(s):  
Margaret T. Ho ◽  
Brian Weselowski ◽  
Ze-Chun Yuan
Keyword(s):  
Carbon Source ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Metabolic Pathways ◽  
Complete Genome ◽  
Sole Carbon Source ◽  
Acinetobacter Calcoaceticus ◽  
Hydrocarbon Degradation ◽  
Content Type ◽  
Degradation Ability

ABSTRACT We report here the complete assembled genome sequence of Acinetobacter calcoaceticus CA16, which is capable of utilizing diesel and lignin as a sole carbon source. CA16 contains a 4,110,074-bp chromosome and a 5,920-bp plasmid. The assembled sequences will help elucidate potential metabolic pathways and mechanisms responsible for CA16’s hydrocarbon degradation ability.

scholarly journals LacR Is a Repressor oflacABCDand LacT Is an Activator oflacTFEG, Constituting thelacGene Cluster in Streptococcus pneumoniae

2014 ◽  
Vol 80 (17) ◽  
pp. 5349-5358 ◽  
Author(s):  
Muhammad Afzal ◽  
Sulman Shafeeq ◽  
Oscar P. Kuipers
Keyword(s):  
Streptococcus Pneumoniae ◽  
Carbon Source ◽  
Gene Cluster ◽  
Sole Carbon Source ◽  
Transcriptional Repressor ◽  
Transcriptional Regulator ◽  
Transcriptional Activator ◽  
Content Type ◽  
Elevated Expression

ABSTRACTComparison of the transcriptome ofStreptococcus pneumoniaestrain D39 grown in the presence of either lactose or galactose with that of the strain grown in the presence of glucose revealed the elevated expression of various genes and operons, including thelacgene cluster, which is organized into two operons, i.e.,lacoperon I (lacABCD) andlacoperon II (lacTFEG). Deletion of the DeoR family transcriptional regulatorlacRthat is present downstream of thelacgene cluster revealed elevated expression oflacoperon I even in the absence of lactose. This suggests a function of LacR as a transcriptional repressor oflacoperon I, which encodes enzymes involved in the phosphorylated tagatose pathway in the absence of lactose or galactose. Deletion oflacRdid not affect the expression oflacoperon II, which encodes a lactose-specific phosphotransferase. This finding was further confirmed by β-galactosidase assays with PlacA-lacZand PlacT-lacZin the presence of either lactose or glucose as the sole carbon source in the medium. This suggests the involvement of another transcriptional regulator in the regulation oflacoperon II, which is the BglG-family transcriptional antiterminator LacT. We demonstrate the role of LacT as a transcriptional activator oflacoperon II in the presence of lactose and CcpA-independent regulation of thelacgene cluster inS. pneumoniae.

scholarly journals Draft Genome Sequences of Bacterial Strains Capable of Degrading Ulvan from the Green Alga Ulva ohnoi

2020 ◽  
Vol 9 (3) ◽  
Author(s):  
Ratna Mondal ◽  
Miho Satoh ◽  
Kouhei Ohnishi
Keyword(s):  
Carbon Source ◽  
Green Alga ◽  
Sole Carbon Source ◽  
Draft Genome ◽  
Bacterial Strains ◽  
Genome Sequences ◽  
Content Type ◽  
Complete Degradation ◽  
Ulva Ohnoi

We present here the draft genome sequences of four marine bacterial strains which can use ulvan as their sole carbon source. We used ulvan extracted from the green alga Ulva ohnoi. Each bacterium contains a polysaccharide-utilizing locus, which is necessary for the complete degradation of ulvan.

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