scholarly journals The foliar endophytePhialocephala scopiformisDAOMC 229536 secretes enzymes supporting growth on wood as sole carbon source

2018 ◽  
Author(s):  
Jennifer M. Bhatnagar ◽  
Grzegorz Sabat ◽  
Daniel Cullen
Keyword(s):  
Carbon Source ◽  
Aromatic Compounds ◽  
Glycoside Hydrolase ◽  
Pinus Contorta ◽  
Sole Carbon Source ◽  
Oxidative Degradation ◽  
Cellobiose Dehydrogenase ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Conifer Needle

AbstractThe conifer needle endophyte,Phialocephala scopiformis, was cultivated in media containing groundPinus contortawood as sole carbon source. After five and seven days growth, concentrated extracellular fluids were subjected to LC-MS/MS analyses. A total of 590 proteins were identified of which 99 were assigned to glycoside hydrolase families within the Carbohydrate Active Enzyme (CAzyme) system. Multiple isozymes of exo-and endo-acting cellulases were among the most abundant proteins, and oxidative degradation of cellulose was supported by the presence of lytic polysaccharide monooxygenases, glucooligosaccharide oxidase and cellobiose dehydrogenase. Oxidoreductases were also plentiful and included GMC oxidoreductases, alcohol dehydrogenases, laccases, copper radical oxidases, tyrosinases and catalase. The expression and diversity of extracellular oxidoreductases indicates a capacity to metabolize alcohols and aromatic compounds.

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 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 Host engineering for improved valerolactam production in Pseudomonas putida

2019 ◽  
Author(s):  
Mitchell G. Thompson ◽  
Luis E. Valencia ◽  
Jacquelyn M. Blake-Hedges ◽  
Pablo Cruz-Morales ◽  
Alexandria E. Velasquez ◽  
...  
Keyword(s):  
Metabolic Engineering ◽  
Carbon Source ◽  
Pseudomonas Putida ◽  
Aromatic Compounds ◽  
Sole Carbon Source ◽  
Carbon Sources ◽  
Shotgun Proteomics ◽  
Rich Media ◽  
Amide Hydrolase

ABSTRACTPseudomonas putida is a promising bacterial chassis for metabolic engineering given its ability to metabolize a wide array of carbon sources, especially aromatic compounds derived from lignin. However, this omnivorous metabolism can also be a hindrance when it can naturally metabolize products produced from engineered pathways. Herein we show that P. putida is able to use valerolactam as a sole carbon source, as well as degrade caprolactam. Lactams represent important nylon precursors, and are produced in quantities exceeding one million tons per year[1]. To better understand this metabolism we use a combination of Random Barcode Transposon Sequencing (RB-TnSeq) and shotgun proteomics to identify the oplBA locus as the likely responsible amide hydrolase that initiates valerolactam catabolism. Deletion of the oplBA genes prevented P. putida from growing on valerolactam, prevented the degradation of valerolactam in rich media, and dramatically reduced caprolactam degradation under the same conditions. Deletion of oplBA, as well as pathways that compete for precursors L-lysine or 5-aminovalerate, increased the titer of valerolactam from undetectable after 48 hours of production to ~90 mg/L. This work may serve as a template to rapidly eliminate undesirable metabolism in non-model hosts in future metabolic engineering efforts.

scholarly journals Lytic Polysaccharide Monooxygenases as Chitin-Specific Virulence Factors in Crayfish Plague

Biomolecules ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1180
Author(s):  
Federico Sabbadin ◽  
Bernard Henrissat ◽  
Neil C. Bruce ◽  
Simon J. McQueen-Mason
Keyword(s):  
Endangered Species ◽  
Virulence Factors ◽  
Molecular Mechanisms ◽  
Oxidative Degradation ◽  
Aphanomyces Astaci ◽  
Lytic Polysaccharide Monooxygenases ◽  
Enzyme Family ◽  
Polysaccharide Monooxygenases ◽  
Oomycete Pathogen ◽  
Specific Virulence

The oomycete pathogen Aphanomyces astaci, also known as “crayfish plague”, is an obligate fungal-like parasite of freshwater crustaceans and is considered responsible for the ongoing decline of native European crayfish populations. A. astaci is thought to secrete a wide array of effectors and enzymes that facilitate infection, however their molecular mechanisms have been poorly characterized. Here, we report the identification of AA15 lytic polysaccharide monooxygenases (LPMOs) as a new group of secreted virulence factors in A. astaci. We show that this enzyme family has greatly expanded in A. astaci compared to all other oomycetes, and that it may facilitate infection through oxidative degradation of crystalline chitin, the most abundant polysaccharide found in the crustacean exoskeleton. These findings reveal new roles for LPMOs in animal–pathogen interactions, and could help inform future strategies for the protection of farmed and endangered species.

scholarly journals Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Sona Garajova ◽  
Yann Mathieu ◽  
Maria Rosa Beccia ◽  
Chloé Bennati-Granier ◽  
Frédéric Biaso ◽  
...  
Keyword(s):  
Oxidative Degradation ◽  
Single Domain ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases

Cometabolic oxidation of phenanthrene to phenanthrenetrans-9,10-dihydrodiol byMycobacteriumstrain S1 growing on anthracene in the presence of phenanthrene

1999 ◽  
Vol 45 (5) ◽  
pp. 369-376 ◽  
Author(s):  
Saowanit Tongpim ◽  
Michael A Pickard
Keyword(s):  
Carbon Source ◽  
Growth Medium ◽  
Aromatic Compounds ◽  
Sole Carbon Source ◽  
Polycyclic Aromatic Compounds ◽  
P450 Monooxygenase ◽  
Original Source ◽  
Dead End ◽  
Polycyclic Aromatic ◽  
Rhodococcus Strain

Mycobacterium strain S1, originally described as Rhodococcus strain S1 by chemotaxonomic criteria, was isolated by growth on anthracene, and is unable to use any of nine other polycyclic aromatic compounds as carbon source. Metabolism of phenanthrene during growth on anthracene as sole carbon source results in the accumulation of traces of a dihydrodiol metabolite in the growth medium, which, by comparison with authentic standards, has been tentatively identified as phenanthrene trans-9,10-dihydrodiol. Anthracene metabolites were ruled out on the basis of comparisons with authentic anthracene dihydrodiols from Pseudomonas fluorescens D1 and chemically synthesized anthrols. The original source of phenanthrene for dihydrodiol production was phenanthrene present as a <1% contaminant in the anthracene used as carbon source. However, addition of further phenanthrene to the anthracene growth medium increased the level of phenanthrene trans-9,10-dihydrodiol formed. Mycobacterium strain S1 also produced phenanthrene trans-9,10-dihydrodiol when grown in a glucose-salts medium in the presence of phenanthrene. This dihydrodiol is a dead-end metabolite, and neither it nor its parent hydrocarbon are able to support the growth of Mycobacterium strain S1. Studies with metyrapone and ancimidol, which did not inhibit growth on anthracene but did inhibit formation of phenanthrene trans-9,10-dihydrodiol, suggest it is likely the product of a cytochrome P450 monooxygenase-like activity.Key words: phenanthrene trans-9,10-dihydrodiol, Mycobacterium.

scholarly journals Activation of bacterial lytic polysaccharide monooxygenases with cellobiose dehydrogenase

2016 ◽  
Vol 25 (12) ◽  
pp. 2175-2186 ◽  
Author(s):  
Jennifer S. M. Loose ◽  
Zarah Forsberg ◽  
Daniel Kracher ◽  
Stefan Scheiblbrandner ◽  
Roland Ludwig ◽  
...  
Keyword(s):  
Cellobiose Dehydrogenase ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases

scholarly journals Cinnamic Acid, an Autoinducer of Its Own Biosynthesis, Is Processed via Hca Enzymes in Photorhabdus luminescens

2008 ◽  
Vol 74 (6) ◽  
pp. 1717-1725 ◽  
Author(s):  
Sabina Chalabaev ◽  
Evelyne Turlin ◽  
Sylvie Bay ◽  
Christelle Ganneau ◽  
Emma Brito-Fravallo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Cinnamic Acid ◽  
Aromatic Compounds ◽  
Sole Carbon Source ◽  
Biosynthetic Pathway ◽  
Phenylalanine Ammonia Lyase ◽  
Carbon Sources ◽  
Degradation Pathway ◽  
Photorhabdus Luminescens

ABSTRACT Photorhabdus luminescens, an entomopathogenic bacterium and nematode symbiont, has homologues of the Hca and Mhp enzymes. In Escherichia coli, these enzymes catalyze the degradation of the aromatic compounds 3-phenylpropionate (3PP) and cinnamic acid (CA) and allow the use of 3PP as sole carbon source. P. luminescens is not able to use 3PP and CA as sole carbon sources but can degrade them. Hca dioxygenase is involved in this degradation pathway. P. luminescens synthesizes CA from phenylalanine via a phenylalanine ammonia-lyase (PAL) and degrades it via the not-yet-characterized biosynthetic pathway of 3,5-dihydroxy-4-isopropylstilbene (ST) antibiotic. CA induces its own synthesis by enhancing the expression of the stlA gene that codes for PAL. P. luminescens bacteria release endogenous CA into the medium at the end of exponential growth and then consume it. Hca dioxygenase is involved in the consumption of endogenous CA but is not required for ST production. This suggests that CA is consumed via at least two separate pathways in P. luminescens: the biosynthesis of ST and a pathway involving the Hca and Mhp enzymes.

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