Gene family expansions and contractions are associated with host range in plant pathogens of the genus Colletotrichum

Background: Many species belonging to the genus Colletotrichum cause anthracnose disease on a wide range of plant species. In addition to their economic impact, the genus Colletotrichum is a useful model for the study of the evolution of host specificity, speciation and reproductive behaviors. Genome projects of Colletotrichum species have already opened a new era for studying the evolution of pathogenesis in fungi. Results: We sequenced and annotated the genomes of four strains in the Colletotrichum acutatum species complex (CAsc), a clade of broad host range pathogens within the genus. The four CAsc proteomes and secretomes along with those representing an additional 13 species (six Colletotrichum spp. and seven other Sordariomycetes) were classified into protein families using a variety of tools. Hierarchical clustering of gene family and functional domain assignments, and phylogenetic analyses revealed lineage specific losses of carbohydrate-active enzymes (CAZymes) and proteases encoding genes in Colletotrichum species that have narrow host range as well as duplications of these families in the CAsc. We also found a lineage specific expansion of necrosis and ethylene-inducing peptide 1 (Nep1)-like protein (NLPs) families within the CAsc. Conclusions: This study illustrates the plasticity of Colletotrichum genomes, and shows that major changes in host range are associated with relatively recent changes in gene content

Influence of step duration in fractionated Py-GC/MS of lignocellulosic biomass

International audienceFractionated pyrolysis coupled to gas chromatography and mass spectrometry (Py-GC/MS) appears as an interesting analytical tool for elucidating lignocellulosic biomass structure, as it allows the progressive release of chemical fragments representative of biomass macromolecular composition. In this paper the effect of fractionated pyrolysis time (from 5 s to 300 s) on the degradation of lignin and carbohydrates from beech wood was studied at temperatures between 250 °C and 500 °C. Fractionated Py-GC/MS showed that the release temperature of the volatile degradation products varied between the volatile species detected. In addition, the step duration time changed the thermal degradation behavior of lignocellulosic components. Shortening the constant step duration time from 300 s to 5 s shifted the maximum weight loss to the higher temperatures. The result was opposite at long step duration times. Time optimization at each pyrolysis temperature (250 °C, 40 s; 300 °C, 30 s; 350 °C, 25 s; 370 °C, 20 s; 400 °C, 15 s; 450 °C, 10 s; 500 °C, 5 s) enhanced the yield of both lignin and carbohydrate volatile pyrolysis degradation products. In addition, two multiple temperature maxima were shown for some lignin and carbohydrate derivatives. This behavior may be due to the two different pathways of formation and macromolecular origins of compounds in beech wood. At optimized conditions lignin derivatives having a 3-carbon side chain substituent had a maximum at lower temperature than that of lignin derivatives with a 1-carbon side chain substituent. That phenomenon follows the order of primary and secondary pyrolysis reactions. Similar behaviors were observed among the degradation products of hemicelluloses and cellulose. Degradation products of hemicelluloses were mainly released at lower temperatures than those of cellulose derivatives, which illustrates the lower thermal stability of hemicelluloses compared to cellulose

Polymerization of coniferyl alcohol by Mn3+-mediated (enzymatic) oxidation : Effects of H2O2 concentration, aqueous organic solvents, and pH

The objective of this study was to evaluate the ability of one versatile peroxidase and the biocatalytically generated complex Mn(III)-malonate to polymerize coniferyl alcohol (CA) to obtain dehydrogenation polymers (DHPs) and to characterize how closely the structures of the formed DHPs resemble native lignin. Hydrogen peroxide was used as oxidant and Mn2+ as mediator. Based on the yields of the polymerized product, it was concluded that the enzymatic reaction should be performed in aqueous solution without organic solvents at 4.5pH6.0 and with 0.75H(2)O(2):CA ratio1. The results obtained from the Mn3+-malonate-mediated polymerization showed that the yield was almost 100%. Reaction conditions had, however, effect on the structures of the formed DHPs, as detected by size exclusion chromatography and pyrolysis-GC/MS. It can be concluded that from the structural point of view, the optimal pH for DHP formation using the presently studied system was 3 or 4.5. Low H2O2/CA ratio was beneficial to avoid oxidative side reactions. However, the high frequency of - linkages in all cases points to dimer formation between monomeric CA rather than endwise polymerization. (c) 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:81-90, 2018Peer reviewe