An esterase from the basidiomycete Pleurotus sapidus hydrolyzes feruloylated saccharides

Linke, Diana; Matthes, René; Nimtz, Manfred; Zorn, Holger; Bunzel, Mirko; Berger, Ralf G.

doi:10.1007/s00253-012-4598-7

Cited by 39 publications

(39 citation statements)

References 36 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%

“…However, they do not show significant homology to A. niger FaeA or FaeB, which is also reflected in their biochemical differences. P. sapidus Est1 hydrolyzes arabinosyl esters of ferulic acid more efficiently than methyl ferulate, which is the commonly used substrate for feruloyl esterases (174). PeFaeA had higher activity toward natural substrates, such as feruloylated mono-, di-, and trisaccharides (F-A, F-AX, and F-AXG, respectively), than toward the typical synthetic feruloyl ester substrates methyl ferulate, methyl coumarate, and methyl sinapate (173).…”

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

348

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%

Section: Hemicellulose-and Pectin-debranching Enzymesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

348

287

View full text Add to dashboard Cite

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“…Screening for Laccase Activity: Laccase activity of fungal strains is observed by decomposition of ABTS (2, 2'azino-bis-3-ethylbenz-thiazoline-6-sulfonic acid) 12 . The fungal strains were tested for laccase production by growing them on LME Basal Medium agar plates containing 0.1% (w/v) of ABTS as a substrate.…”

Section: Minimum Inhibitory Concentration (Mic) Of Fungal Strainmentioning

confidence: 99%

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2017

IJPSR

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The present study was planned with the aim to remove various dye decolorization using fungal strains. The fungi was isolated from soil samples collected from waste disposal areas and agricultural fields. Nine isolates were initially selected for testing their decolorization potential in the liquid medium. Three most effective strains were used to study the decolorization of four different dyes i.e Reactive Red, Navy Blue HER, Reactive Magenta B and Orange 3R. The strain belonging to Talaromyces funiculosum (M2F) was found to be the most potent strain. More than 70% decolorization was observed under optimal incubation conditions of temperature and pH. Overall, the dye decolorization was maximum at 250 mg/L dye concentrations at pH 5-6 under continuous shaking conditions. The culture conditions like pH, temperature, inoculum size and NaCl concentrations were also found effective in decolorization efficacy of the fungal strain which was studied using Response surface methodology (RSM) with Minitab 16 software. Qualitative and quantitative assays for determining the production of lignolytic enzymes such as laccases and peroxidises by the fungal strains were studied and a comparison of degraded and undegraded forms of the dye were done by using analytical techniques like FTIR, UV Vis spectroscopy and GCMS.

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“…These esterase substrates were purified and identified as described previously (24,25). Coffee was obtained from Tchibo (Hamburg, Germany), and wheat bran was obtained from Alnatura (Lorsch, Germany).…”

Section: Chemicals and Substratesmentioning

confidence: 99%

“…Amino acid sequences of tryptic peptides of UmChlE were deduced by electrospray ionization-tandem mass spectrometry (ESI-MS/MS) using a maXis quadrupole time of flight (QTOF) mass spectrometer (Bruker, Bremen, Germany). The procedure was described in detail previously (25). NCBI BLAST (blastp program) searches were performed with the obtained amino acid sequences.…”

Section: Chemicals and Substratesmentioning

confidence: 99%

A Chlorogenic Acid Esterase with a Unique Substrate Specificity from Ustilago maydis

Nieter

Haase-Aschoff

Kelle

et al. 2015

Appl Environ Microbiol

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An extracellular chlorogenic acid esterase from Ustilago maydis (UmChlE) was purified to homogeneity by using three separation steps, including anion-exchange chromatography on a Q Sepharose FF column, preparative isoelectric focusing (IEF), and, finally, a combination of affinity chromatography and hydrophobic interaction chromatography on polyamide. SDS-PAGE analysis suggested a monomeric protein of ϳ71 kDa. The purified enzyme showed maximal activity at pH 7.5 and at 37°C and was active over a wide pH range (3.5 to 9.5). Previously described chlorogenic acid esterases exhibited a comparable affinity for chlorogenic acid, but the enzyme from Ustilago was also active on typical feruloyl esterase substrates. Kinetic , respectively. UmChlE released ferulic, p-coumaric, and caffeic acids from natural substrates such as destarched wheat bran (DSWB) and coffee pulp (CP), confirming activity on complex plant biomass. The full-length gene encoding UmChlE consisted of 1,758 bp, corresponding to a protein of 585 amino acids, and was functionally produced in Pichia pastoris GS115. Sequence alignments with annotated chlorogenic acid and feruloyl esterases underlined the uniqueness of this enzyme. P lant cell walls consist of a heterogeneous mixture of polymers, including cellulose, hemicellulose, pectin, and lignin. In addition to these main components, hydroxycinnamates play a key role in the formation of a complex network of these polymers. While hydroxycinnamates covalently cross-link plant cell wall polysaccharides to each other by ester bonds, links between polysaccharides and lignin are formed mainly by ether linkages (1). Thus, these phenolic acids (mainly ferulic, p-coumaric, and caffeic acids) not only influence the rigidity and mechanical properties of the cell wall but also play a role in plant defense (2). They are linked differently to sugar residues in plants: in grasses such as wheat, barley, or maize, ferulates and p-coumarates are mainly found esterified to the O-5 position of arabinose residues, whereas in pectin of dicotyledons, such as spinach or sugar beet, ferulic acid is esterified to the O-2 position of arabinose and the O-6 position of galactose residues (3). Furthermore, hydroxycinnamates also exist as soluble ester conjugates of quinic acid, the best-known example being chlorogenic acid [3-(3,4-dihydroxycinnamoyl)quinic acid] (4). Particularly high concentrations of chlorogenic acid are present in coffee, apple, pear, and potato tuber (4). The health, cosmetic, and pharmaceutical industries are especially interested in hydroxycinnamates due to their anticarcinogenic, anti-inflammatory, and antioxidant properties (5). Consequently, enzymes that are able to release these phenolic compounds are not only essential for the degradation of plant biomass but also of interest for potential food and medical applications of the released products.One group of these enzymes is the feruloyl esterases (FAEs) (EC 3.1.1.73), a subclass of the carboxylic ester hydrolases (EC 3.1.1). They hydrolyze the ester lin...

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An esterase from the basidiomycete Pleurotus sapidus hydrolyzes feruloylated saccharides

Cited by 39 publications

References 36 publications

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Untitled

A Chlorogenic Acid Esterase with a Unique Substrate Specificity from Ustilago maydis

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