An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity

Haase-Aschoff, Paul; Linke, Diana; Nimtz, Manfred; Popper, Lutz; Berger, Ralf G.

doi:10.1016/j.procbio.2013.09.016

Cited by 9 publications

(7 citation statements)

References 35 publications

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“…Only three basidomycete FAEs have been biochemically characterized (173)(174)(175). The molecular masses of FAEs of the white rot fungi P. eryngii and P. sapidus are 67 kDa and 55 kDa, respectively, which are higher than those of the FAEs of A. awamori (35 kDa) (176) and A. niger FaeA (36 kDa) (177,178) but lower than that of A. niger FaeB (74 kDa) (178).…”

Section: Hemicellulose-and Pectin-debranching Enzymesmentioning

confidence: 99%

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Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

340

287

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SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

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Section: Hemicellulose-and Pectin-debranching Enzymesmentioning

confidence: 99%

“…Both PeFaeA and P. sapidus Est1 prefer F-AX over F-A and F-AXG of the natural substrates, whereas A. niger FaeA prefers F-A over F-AX (173,179). Recently, a novel type of FAE (EstBC), which hydrolyzes both benzoates and cinnamates, has been described for the jelly fungus A. auricula-judae (175).…”

Section: Hemicellulose-and Pectin-debranching Enzymesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

340

287

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“…(e.g., Jaapia argillacea , Penicillium rubens , and Armillaria mellea ). Subfamily SF8 contains FAEs from Auricularia auricular - judae (EstBC [104]), Anaeromyces mucronatus (Fae1A [48]), and Orpinomyces sp. (OrpFaeA [105]), while SF12 contains Pleurotus sapidus (Est1 [106]) and Pleurotus eryngii (PeFaeA [57]) FAEs, for which there were no homologs found in the previous study [51].…”

Section: Update On the Classification Of Fungal Faesmentioning

confidence: 99%

Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications

Dilokpimol

Mäkelä

Pontes

et al. 2016

Biotechnol Biofuels

133

166

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Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass conversion. Their ability to release ferulic acid and other hydroxycinnamic acids from plant biomass makes FAEs potential biocatalysts in a wide variety of applications such as in biofuel, food and feed, pulp and paper, cosmetics, and pharmaceutical industries. This review provides an updated overview of the knowledge on fungal FAEs, in particular describing their role in plant biomass degradation, diversity of their biochemical properties and substrate specificities, their regulation and conditions needed for their induction. Furthermore, the discovery of new FAEs using genome mining and phylogenetic analysis of current publicly accessible fungal genomes will also be presented. This has led to a new subfamily classification of fungal FAEs that takes into account both phylogeny and substrate specificity.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-016-0651-6) contains supplementary material, which is available to authorized users.

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“…DSWB was produced as described elsewhere [16]. PCR primers were synthesized by Eurofins MWG Operon (Ebersberg, Germany).…”

Section: Chemicals and Primersmentioning

confidence: 99%

“…substrate specificity and sequence data may be insufficient [16]. The Crepin classification was extended on the basis of phylogenetic data by Benoit et al [38] and descriptor-based analysis by Udatha et al [39].…”

Section: Substrate Specificity and Kinetic Parametersmentioning

confidence: 99%

Heterologous production of a feruloyl esterase from Pleurotus sapidus synthesizing feruloyl‐saccharide esters

Kelle

Nieter

Krings

et al. 2015

Biotech and App Biochem

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The feruloyl esterase (FAE) gene EST1 from the basidiomycete Pleurotus sapidus was heterologously expressed in Escherichia coli and Pichia pastoris. Catalytically active recombinant Est1 was secreted using P. pastoris as a host. For expression in P. pastoris, the expression vector pPIC9K was applied. The EST1 gene was cloned with an N-terminal α-mating factor pre-pro sequence and expressed under the control of a methanol inducible alcohol oxidase 1 promotor. Est1 was purified to homogeneity using ion exchange and hydrophobic interaction chromatography. The recombinant Est1 showed optima at pH 5.0 and 50 °C, and released ferulic acid from saccharide esters and from the natural substrate destarched wheat bran. Substrate specificity profile and descriptor-based analysis demonstrated unique properties, showing that Est1 did not fit into the current FAE classification model. Transferuloylation synthesis of feruloyl-saccharide esters was proven for mono- and disaccharides.

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An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity

Cited by 9 publications

References 35 publications

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications

Heterologous production of a feruloyl esterase from Pleurotus sapidus synthesizing feruloyl‐saccharide esters

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