Classification of fungal and bacterial lytic polysaccharide monooxygenases

Busk, Peter Kamp; Lange, Lene

doi:10.1186/s12864-015-1601-6

Cited by 85 publications

(76 citation statements)

References 62 publications

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“…hancockii genome by PPR/HotPep analysis: AA9 (14 genes in 7 subgroups) and AA11 (5 genes in 3 subgroups) in the genome (see Table 2). The peptide patterns used for the LPMO analysis were expanded beyond the Cazy database and validated in a recent study [18]. LPMO enzymes are primarily described to be active on crystalline cellulose, acting in synergy with endoglucanases (EC 3.2.1.4).…”

Section: Resultsmentioning

confidence: 99%

“…LPMO enzymes were first associated with acting synergistically with GH cellulases in degrading cellulose. Recently it has been documented that LPMO enzymes can also play a role in breaking down hemicellulosic structures, and a subdivision of the LPMO enzymes based on peptide pattern recognition has been suggested recently [18]. Further studies are needed to characterise the distribution at subfamily level of the LPMO enzymes found in Aspergillus species and to characterise and document the diversity and variation among the many LPMO genes found in the genome of this type of fungus.…”

Section: Resultsmentioning

confidence: 99%

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Aspergillus hancockii sp. nov., a biosynthetically talented fungus endemic to southeastern Australian soils

Pitt

Lange

Lacey³

et al. 2017

PLoS ONE

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Aspergillus hancockii sp. nov., classified in Aspergillus subgenus Circumdati section Flavi, was originally isolated from soil in peanut fields near Kumbia, in the South Burnett region of southeast Queensland, Australia, and has since been found occasionally from other substrates and locations in southeast Australia. It is phylogenetically and phenotypically related most closely to A. leporis States and M. Chr., but differs in conidial colour, other minor features and particularly in metabolite profile. When cultivated on rice as an optimal substrate, A. hancockii produced an extensive array of 69 secondary metabolites. Eleven of the 15 most abundant secondary metabolites, constituting 90% of the total area under the curve of the HPLC trace of the crude extract, were novel. The genome of A. hancockii, approximately 40 Mbp, was sequenced and mined for genes encoding carbohydrate degrading enzymes identified the presence of more than 370 genes in 114 gene clusters, demonstrating that A. hancockii has the capacity to degrade cellulose, hemicellulose, lignin, pectin, starch, chitin, cutin and fructan as nutrient sources. Like most Aspergillus species, A. hancockii exhibited a diverse secondary metabolite gene profile, encoding 26 polyketide synthase, 16 nonribosomal peptide synthase and 15 nonribosomal peptide synthase-like enzymes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Aspergillus hancockii sp. nov., a biosynthetically talented fungus endemic to southeastern Australian soils

Pitt

Lange

Lacey³

et al. 2017

PLoS ONE

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“…These include lignin-degrading enzymes as well as lytic polysaccharide monooxygenases (LPMO) (84). In U. maydis, only one putative LPMO member of AA10, the copper-dependent LPMO, has been identified (85), suggesting that the insertion of additional foreign enzymes may be beneficial. Interestingly, putative oxidoreductases that are yet uncharacterized seem to be overrepresented in the U. maydis genome.…”

Section: Discussionmentioning

confidence: 99%

Activating Intrinsic Carbohydrate-Active Enzymes of the Smut Fungus Ustilago maydis for the Degradation of Plant Cell Wall Components

Geiser

Reindl

Blank

et al. 2016

Appl Environ Microbiol

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The microbial conversion of plant biomass to valuable products in a consolidated bioprocess could greatly increase the ecologic and economic impact of a biorefinery. Current strategies for hydrolyzing plant material mostly rely on the external application of carbohydrate-active enzymes (CAZymes). Alternatively, production organisms can be engineered to secrete CAZymes to reduce the reliance on externally added enzymes. Plant-pathogenic fungi have a vast repertoire of hydrolytic enzymes to sustain their lifestyle, but expression of the corresponding genes is usually highly regulated and restricted to the pathogenic phase. Here, we present a new strategy in using the biotrophic smut fungus Ustilago maydis for the degradation of plant cell wall components by activating its intrinsic enzyme potential during axenic growth. This fungal model organism is fully equipped with hydrolytic enzymes, and moreover, it naturally produces value-added substances, such as organic acids and biosurfactants. To achieve the deregulated expression of hydrolytic enzymes during the industrially relevant yeast-like growth in axenic culture, the native promoters of the respective genes were replaced by constitutively active synthetic promoters. This led to an enhanced conversion of xylan, cellobiose, and carboxymethyl cellulose to fermentable sugars. Moreover, a combination of strains with activated endoglucanase and ␤-glucanase increased the release of glucose from carboxymethyl cellulose and regenerated amorphous cellulose, suggesting that mixed cultivations could be a means for degrading more complex substrates in the future. In summary, this proof of principle demonstrates the potential applicability of activating the expression of native CAZymes from phytopathogens in a biocatalytic process. IMPORTANCEThis study describes basic experiments that aim at the degradation of plant cell wall components by the smut fungus Ustilago maydis. As a plant pathogen, this fungus contains a set of lignocellulose-degrading enzymes that may be suited for biomass degradation. However, its hydrolytic enzymes are specifically expressed only during plant infection. Here, we provide the proof of principle that these intrinsic enzymes can be synthetically activated during the industrially relevant yeast-like growth. The fungus is known to naturally synthesize valuable compounds, such as itaconate or glycolipids. Therefore, it could be suited for use in a consolidated bioprocess in which more complex and natural substrates are simultaneously converted to fermentable sugars and to value-added compounds in the future. O ne central aim of a sustainable bioeconomy is the switch from fossil-to bio-based production of platform chemicals and other valuable substances. To date, the most promising feedstock for biorefineries is lignocellulosic nonfood plant biomass (1). Lignocellulose is a complex composite mainly consisting of cellulose, hemicelluloses, pectin, and lignin (2). The selective conversion of lignocellulosic biomass comprises different steps: pret...

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“…The capability of virolysins in lysing S. typhi can be induced in the absence of bacteriophage due to expression of functions from cell wall degraded by the enzyme (Clement et al, 1990;Sanz-Gaitero et al, 2013). Better results were obtained when phages and virolysins were mixed with bacterial cells in the solution because they adsorbed cell surfaces and cleaved to bonds, eventually causing lysis (Nelson et al, 2001;Busk and Lange, 2015).…”

Section: Discussionmentioning

confidence: 91%

Potentiality of lytic bacteriophages and their virolysins in lysing multi-drug resistant Salmonella typhi

Elshayeb¹,

Ahmed²,

Siddig³

et al. 2017

Afr. J. Biotechnol.

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Bacteriophage virolysins or lytic enzymes are bacterial peptidoglycan hydrolases responsible for lysing bacterial cells. Consequently, they are used as enzybiotics alongside with bacteriophage therapy to remedy multi-drug resistant Salmonella typhi. The objective of this study was to evaluate the potentiality of lytic bacteriophages and their virolysins in curing multi-drug resistant S. typhi. S. typhi was isolated and identified according to WHO and ISO guidelines. Antibiotics susceptibilities were tested using CLSI recommendations. Correspondingly, bacteriophage-lysing efficiency was assayed by plaques formation using the double-layer agar technique. Virolysins were extracted using ultracentrifugation and purified by dialysis after buffering in ammonium sulfate. Virolysins activity was determined by measuring the reaction mixtures spectrophotometrically (bacteria incubated as substrate in 37°C for 4 h). The phages and virolysins kinetics exponential rates were calculated using specific differential equations. Susceptibility data plotted based on antibiogram criteria confirmed that 33% of S. typhi isolates were multi-drug resistant. For bacteriophage replication and multiplicity of infection, phages were amplified to produce the maximum particles of titers. The phage titration data fit on sonogram revealed exponential decay of S. typhi incubated for 12 h. Meanwhile, the enzyme kinetics exponential decay on double reciprocal plot showed irretrievable relationship of host decay in 4 h. Since phages depend on their lytic cycle in lysing bacterial host, their enzymes have more capability in decaying the host; besides they are safe and time-saving when used in the treatment of antibiotics resistant S. typhi.

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Classification of fungal and bacterial lytic polysaccharide monooxygenases

Cited by 85 publications

References 62 publications

Aspergillus hancockii sp. nov., a biosynthetically talented fungus endemic to southeastern Australian soils

Aspergillus hancockii sp. nov., a biosynthetically talented fungus endemic to southeastern Australian soils

Activating Intrinsic Carbohydrate-Active Enzymes of the Smut Fungus Ustilago maydis for the Degradation of Plant Cell Wall Components

Potentiality of lytic bacteriophages and their virolysins in lysing multi-drug resistant Salmonella typhi

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