β-Xylosidases from filamentous fungi: an overview

Knob, Adriana; Terrasan, César Rafael Fanchini; Carmona, Eleonora Cano

doi:10.1007/s11274-009-0190-4

Cited by 163 publications

(108 citation statements)

References 171 publications

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“…The difference between the molecular masses determined by size-exclusion chromatography and SDS-PAGE suggests that BxTW1 works as a noncovalent dimer in its native conformation. Isoelectrofocusing indicated that the pI of the protein was 7.6, a value similar to those reported for other ␤-xylosidases (20). Nevertheless, the theoretical value obtained from the BxTW1 sequence was 4.75.…”

Section: Fig 2 Estimation Of Bxtw1 Molecular Mass By Sds-page (A) Andsupporting

confidence: 84%

“…Figure 1A shows the ␤-xylosidase inducer effect of 1% Avicel, 1% D-xylose, or 1%, 2%, or 3% beechwood xylan over 6 days. A control culture with 1% Dglucose as the carbon source, which inhibits xylanase production by carbon catabolite repression (20), was also tested. The highest ␤-xylosidase activity was detected when 2% beechwood xylan was used as the inductor, and the profile of total secreted proteins was similar to that detected with 3% xylan.…”

Section: Resultsmentioning

confidence: 99%

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Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Nieto-Domínguez

Eugenio

Barriuso

et al. 2015

Appl Environ Microbiol

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This paper reports on a novel ␤-xylosidase from the hemicellulolytic fungus Talaromyces amestolkiae. The expression of this enzyme, called BxTW1, could be induced by beechwood xylan and was purified as a glycoprotein from culture supernatants. We characterized the gene encoding this enzyme as an intronless gene belonging to the glycoside hydrolase gene family 3 (GH3). BxTW1 exhibited transxylosylation activity in a regioselective way. This feature would allow the synthesis of oligosaccharides or other compounds not available from natural sources, such as alkyl glycosides displaying antimicrobial or surfactant properties. Regioselective transxylosylation, an uncommon combination, makes the synthesis reproducible, which is desirable for its potential industrial application. BxTW1 showed high pH stability and Cu 2؉ tolerance. The enzyme displayed a pI of 7.6, a molecular mass around 200 kDa in its active dimeric form, and K m and V max values of 0.17 mM and 52.0 U/mg, respectively, using commercial p-nitrophenyl-␤-D-xylopyranoside as the substrate. The catalytic efficiencies for the hydrolysis of xylooligosaccharides were remarkably high, making it suitable for different applications in food and bioenergy industries. P lant biomass represents the most abundant renewable energy resource available on earth. It is composed mainly of cellulose and hemicellulose, two polysaccharides that constitute the raw material for the so-called second-generation (2G) bioethanol industry. The production of this biofuel has received special attention in recent years because it is based on the use of nonfood sources of cellulosic biomass (1). It has been pointed out that energy crops should be restricted to metal-contaminated soils in order to avoid cultivation competition against the food industry (2, 3).In order to make the production of this biofuel economically viable, many modifications have been introduced into the industrial process in recent years. Among them, the strategy of combining enzymatic hydrolysis of lignocellulose with ethanol fermentation in a single process known as simultaneous saccharification and fermentation (SSF) is a significant step forward, but reduced production costs and improved yields are still necessary (1). Most studies have been using agricultural wastes as raw materials, usually after a physicochemical pretreatment to disrupt the lignocellulose structure to enhance cellulose and hemicellulose accessibility. Nevertheless, the industrial procedure currently used to produce 2G ethanol consists of fermenting glucose, which is enzymatically released from cellulose by using Saccharomyces cerevisiae as a biocatalyst (4). To increase process yields, hemicellulose hydrolysis and pentose fermentation are extremely relevant. Within this heterogeneous group of polysaccharides, xylans are most abundant in hardwoods and grass. They are composed of a backbone of ␤-1,4-linked D-xylopyranosyl units highly substituted with arabinofuranose, glucose, glucuronic or methyl-glucuronic acid, and acetyl side groups. The enz...

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Section: Fig 2 Estimation Of Bxtw1 Molecular Mass By Sds-page (A) Andsupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Nieto-Domínguez

Eugenio

Barriuso

et al. 2015

Appl Environ Microbiol

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“…1a, c). β-xylosidase plays a key role in the complete hydrolysis of XOS into xylose (Knob et al 2009). As shown in Fig.…”

Section: Analysis Of Xylan-degrading Enzymes From a Niger Be-2 And Hmentioning

confidence: 99%

“…Enzymatic hydrolysis of xylan involves the synergistic action of several main chain-and side group-cleaving enzymes, including endo-β-1,4-xylanases (EC 3.2.1.8), β-xylosidases (EC 3.2.1.37), α-arabinofuranosidases (EC 3.2.1.55), α-glucuronidases (EC 3.2.1.139), acetyl xylan esterases (EC 3.1.1.72), and feruloyl esterases (EC 3.1.1.73) (de Vries and Visser 2001). Endo-β-1,4-xylanases as the main xylan-degrading enzymes randomly cleave the internal β-1,4-glycosyl bonds in the xylan main chain producing xylooligomers (Zhang et al 2011), and β-xylosidases convert xylooligomers to xylose monomers (Knob et al 2009). Species of Trichoderma and Aspergillus are used as producers of enzymes that deconstruct lignocellulosic biomass by various companies (Banerjee et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Comparative Analysis of Enzymatic Hydrolysis of Miscanthus Xylan using Aspergillus niger, Hypocrea orientalis, and Trichoderma reesei Xylan-degrading Enzymes

Liu

et al. 2014

BioRes

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Xylan-degrading enzymes from Aspergillus niger and Hypocrea orientalis were characterized by enzyme activity assays and protein profiling with SDS-PAGE and LC-MS/MS. The hydrolysis of Miscanthus xylan by xylan-degrading enzymes from A. niger, H. orientalis, and Trichoderma reesei were comparatively studied by HPLC analysis. It was found that the glycoside hydrolase families 10 xylanase was the main xylanase secreted by H. orientalis and A. niger when using corn cob and wheat bran as inducers. Compared to the enzymes from T. reesei,the enzymes from A. niger showed better efficiency in the hydrolysis of Miscanthus xylan into monosaccharides. Nevertheless, the enzymes from H. orientalis were more preferable for the hydrolysis of Miscanthus xylan into xylo-oligosaccharides (XOS), especially xylobiose and xylotriose. Miscanthus xylan degradation was significantly influenced by the activities of β-xylosidase and α-L-arabinofuranosidase. Xylan-degrading enzymes with high ratios of β-xylosidase and α-L-arabinofuranosidase are necessary for the efficient conversion of Miscanthus xylan into monosaccharides. However, xylan-degrading enzymes with low β-xylosidase activity and high α-L-arabinofuranosidase activity were required for producing XOS.

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“…Filamentous fungi usually secrete plant cell wall degrading enzymes into the medium, releasing energy and nutrients from plant biopolymers. This physiological characteristic is interesting from the industrial point of view because it eliminates the need for releasing the enzymes by cell disruption in the downstream process; moreover the levels of extracellular enzymes produced by fungi are higher than those from yeasts and bacteria (KNOB et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Solid-state fermentation of brewer’s spent grain for xylanolytic enzymes production by Penicillium janczewskii and analyses of the fermented substrate

Terrasan

Carmona

2015

Biosci. J.

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ABSTRACT:In recent decades, increasing interest has been devoted to xylanolytic enzymes due to their potential use in many industrial processes. This study describes the production of xylanase, β-xylosidase and α-Larabinofuranosidase, belonging to the xylanolytic complex, by Penicillium janczewskii using brewer's spent grain as substrate for solid-state fermentation. The optimized conditions for high levels of xylanase, β-xylosidase and α-Larabinofuranosidase production were: 50% initial moisture, which was provided by Vogel's salt solution, seven days of cultivation at 20-30 °C. Fermentation enriched the bioproduct with some amino acids and did not add mycotoxins to it. The use of brewer's spent grain as substrate for fungal cultivation and enzyme production can both add value to this waste and reduce the production cost of xylanolytic enzymes.

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β-Xylosidases from filamentous fungi: an overview

Cited by 163 publications

References 171 publications

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Novel pH-Stable Glycoside Hydrolase Family 3 β-Xylosidase from Talaromyces amestolkiae: an Enzyme Displaying Regioselective Transxylosylation

Comparative Analysis of Enzymatic Hydrolysis of Miscanthus Xylan using Aspergillus niger, Hypocrea orientalis, and Trichoderma reesei Xylan-degrading Enzymes

Solid-state fermentation of brewer’s spent grain for xylanolytic enzymes production by Penicillium janczewskii and analyses of the fermented substrate

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