Comparative analyses of Podospora anserina secretomes reveal a large array of lignocellulose-active enzymes

Poidevin, Laetitia; Berrin, Jean‐Guy; Bennati-Granier, Chloé; Levasseur, Anthony; Herpoël-Gimbert, Isabelle; Chevret, Didier; Coutinho, Pedro M.; Henrissat, Bernard; Heiss-Blanquet, Senta; Record, Éric

doi:10.1007/s00253-014-5698-3

Cited by 39 publications

(29 citation statements)

References 34 publications

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“…A respective 3.7-and 7.7-fold increase in two putative AA3 GMC oxidoreductases (#401428 and #420563; no signal P) further contributed to the overall increase in H 2 O 2 -producing enzymes (Additional file 2: Figure S3N). P. anserina has previously been shown to respond differently on various biomass sources regarding the induction of H 2 O 2 -producing enzymes [10,16]. Our observations clearly show that lignin is amongst the inducing agents for these enzymes and this report constitutes the first experimental evidence of induction of AA7 oxidoreductases of P. anserina.…”

Section: Structural Changes In Light Of the Fungal Secretomesupporting

confidence: 64%

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Evidence for ligninolytic activity of the ascomycete fungus Podospora anserina

Erven

Kleijn

Patyshakuliyeva

et al. 2020

Biotechnol Biofuels

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Background: The ascomycete fungus Podospora anserina has been appreciated for its targeted carbohydrate-active enzymatic arsenal. As a late colonizer of herbivorous dung, the fungus acts specifically on the more recalcitrant fraction of lignocellulose and this lignin-rich biotope might have resulted in the evolution of ligninolytic activities. However, the lignin-degrading abilities of the fungus have not been demonstrated by chemical analyses at the molecular level and are, thus far, solely based on genome and secretome predictions. To evaluate whether P. anserina might provide a novel source of lignin-active enzymes to tap into for potential biotechnological applications, we comprehensively mapped wheat straw lignin during fungal growth and characterized the fungal secretome.Results: Quantitative 13 C lignin internal standard py-GC-MS analysis showed substantial lignin removal during the 7 days of fungal growth (24% w/w), though carbohydrates were preferably targeted (58% w/w removal). Structural characterization of residual lignin by using py-GC-MS and HSQC NMR analyses demonstrated that C α -oxidized substructures significantly increased through fungal action, while intact β-O-4′ aryl ether linkages, p-coumarate and ferulate moieties decreased, albeit to lesser extents than observed for the action of basidiomycetes. Proteomic analysis indicated that the presence of lignin induced considerable changes in the secretome of P. anserina. This was particularly reflected in a strong reduction of cellulases and galactomannanases, while H 2 O 2 -producing enzymes clearly increased. The latter enzymes, together with laccases, were likely involved in the observed ligninolysis. Conclusions:For the first time, we provide unambiguous evidence for the ligninolytic activity of the ascomycete fungus P. anserina and expand the view on its enzymatic repertoire beyond carbohydrate degradation. Our results can be of significance for the development of biological lignin conversion technologies by contributing to the quest for novel lignin-active enzymes and organisms.

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Section: Structural Changes In Light Of the Fungal Secretomesupporting

confidence: 64%

“…cazy.org) [15]. Secretome analyses revealed that some of these enzymes were produced and secreted during growth on lignocellulose [10,16]. Furthermore, deletion of some of the laccase-encoding genes reduced the ability of the fungus to grow on wood shavings, suggesting that they are indeed involved in wood degradation [17].…”

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confidence: 99%

Evidence for ligninolytic activity of the ascomycete fungus Podospora anserina

Erven

Kleijn

Patyshakuliyeva

et al. 2020

Biotechnol Biofuels

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“…LPMO activity has been demonstrated in vitro using ascorbate, gallate, gluthatione10, cysteine11, 3-hydroxyanthranilic acid, quinones and mixtures of low and high molecular weight fractions of lignin12 but the concentration of reductants used in vitro is generally very high. Fungal AA9 LPMOs are secreted under lignocellulolytic conditions together with cellobiose dehydrogenases (CDHs) in many fungal saprotrophs such as Laetisaria arvalis 13, Pycnoporus cinnabarinus 14, Pycnoporus coccineus 15, Podospora anserina 16 and Neurospora crassa 17. CDHs are extracellular fungal flavoenzymes that harbor a flavin-binding dehydrogenase (FAD-DH) domain from the AA3_1 family and a cytochrome-domain from the AA8 family.…”

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confidence: 99%

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

Garajová

Mathieu

Beccia

et al. 2016

Sci Rep

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113

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The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMOs) that carry out oxidative cleavage of polysaccharides. These very powerful enzymes are abundant in fungal saprotrophs. LPMOs require activation by electrons that can be provided by cellobiose dehydrogenases (CDHs), but as some fungi lack CDH-encoding genes, other recycling enzymes must exist. We investigated the ability of AA3_2 flavoenzymes secreted under lignocellulolytic conditions to trigger oxidative cellulose degradation by AA9 LPMOs. Among the flavoenzymes tested, we show that glucose dehydrogenase and aryl-alcohol quinone oxidoreductases are catalytically efficient electron donors for LPMOs. These single-domain flavoenzymes display redox potentials compatible with electron transfer between partners. Our findings extend the array of enzymes which regulate the oxidative degradation of cellulose by lignocellulolytic fungi.

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“…For instance, the enzymatic diversity of P. anserina secretomes induced by a range of carbon sources (i.e. dextrin, glucose, xylose, arabinose, lactose, cellobiose, saccharose, Avicel, Solka-floc, birchwood xylan, wheat straw, maize bran, and sugar beet pulp) was investigated (Poidevin et al, 2014). Compared with the T. reesei enzymatic cocktail, P. anserina secretomes displayed similar cellulase, xylanase, and pectinase activities and greater arabinofuranosidase, arabinanase, and galactanase activities.…”

Section: P Anserina Enzymes In Saccharification Assaysmentioning

confidence: 99%