Characterization of a highly efficient heterodimeric xylosidase from Humicola insolens

Mozolowski, Guy; Connerton, Ian F.

doi:10.1016/j.enzmictec.2009.08.011

Cited by 15 publications

(7 citation statements)

References 31 publications

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“…The released xylo-oligosaccharides are degraded by β-xylosidases. Most fungal β-xylosidases belong to GH3 (Mozolowski and Connerton 2009 ), but several putative β-xylosidases are assigned to GH43 (e.g., in Penicillium herquei and A. oryzae (Ito et al 2003 ; Machida et al 2005 )). GH3 is a conserved family containing mainly BGLs.…”

Section: Hemicellulose Degradationmentioning

confidence: 99%

Fungal enzyme sets for plant polysaccharide degradation

Brink

Vries

2011

Appl Microbiol Biotechnol

507

313

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Enzymatic degradation of plant polysaccharides has many industrial applications, such as within the paper, food, and feed industry and for sustainable production of fuels and chemicals. Cellulose, hemicelluloses, and pectins are the main components of plant cell wall polysaccharides. These polysaccharides are often tightly packed, contain many different sugar residues, and are branched with a diversity of structures. To enable efficient degradation of these polysaccharides, fungi produce an extensive set of carbohydrate-active enzymes. The variety of the enzyme set differs between fungi and often corresponds to the requirements of its habitat. Carbohydrate-active enzymes can be organized in different families based on the amino acid sequence of the structurally related catalytic modules. Fungal enzymes involved in plant polysaccharide degradation are assigned to at least 35 glycoside hydrolase families, three carbohydrate esterase families and six polysaccharide lyase families. This mini-review will discuss the enzymes needed for complete degradation of plant polysaccharides and will give an overview of the latest developments concerning fungal carbohydrate-active enzymes and their corresponding families.

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Section: Hemicellulose Degradationmentioning

confidence: 99%

Fungal enzyme sets for plant polysaccharide degradation

Brink

Vries

2011

Appl Microbiol Biotechnol

507

313

View full text Add to dashboard Cite

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“…Similar molecular masses have been reported for some GH3 β-xylosidases [ 4 , 18 ]. Mozolowski and Connerton [ 20 ] purified a GH3 β-xylosidase from H . insolens culture, which was composed of two protein subunits of 64 kDa and 17 kDa with a total molecular mass of approximately 81 kDa.…”

Section: Resultsmentioning

confidence: 99%

“…3D ). The enzymatic properties of Humicola GHs are much similar [ 12 , 14 , 20 , 22 ], which might be due to their grown surroundings of neutral pH and high temperature.…”

Section: Resultsmentioning

confidence: 99%

“…However, the 64 kDa subunit of H . insolens β-xylosidase had no activity towards p NPAf [ 20 ], which was probably due to the deletion of the C-terminus. No activity was detected when using other polysaccharides as the substrate.…”

Section: Resultsmentioning

confidence: 99%

“…The same conclusion applied to the comparison among four β-xylosidases produced by H . insolens [ 13 , 20 ].…”

Section: Resultsmentioning

confidence: 99%

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High Level Expression of a Novel Family 3 Neutral β-Xylosidase from Humicola insolens Y1 with High Tolerance to D-Xylose

Xia

Shi

et al. 2015

PLoS ONE

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A novel β-xylosidase gene of glycosyl hydrolase (GH) family 3, xyl3A, was identified from the thermophilic fungus Humicola insolens Y1, which is an innocuous and non-toxic fungus that produces a wide variety of GHs. The cDNA of xyl3A, 2334 bp in length, encodes a 777-residue polypeptide containing a putative signal peptide of 19 residues. The gene fragment without the signal peptide-coding sequence was cloned and overexpressed in Pichia pastoris GS115 at a high level of 100 mg/L in 1-L Erlenmeyer flasks without fermentation optimization. Recombinant Xyl3A showed both β-xylosidase and α-arabinfuranosidase activities, but had no hydrolysis capacity towards polysaccharides. It was optimally active at pH 6.0 and 60°C with a specific activity of 11.6 U/mg. It exhibited good stability over pH 4.0–9.0 (incubated at 37°C for 1 h) and at temperatures of 60°C and below, retaining over 80% maximum activity. The enzyme had stronger tolerance to xylose than most fungal GH3 β-xylosidases with a high Ki value of 29 mM, which makes Xyl3A more efficient to produce xylose in fermentation process. Sequential combination of Xyl3A following endoxylanase Xyn11A of the same microbial source showed significant synergistic effects on the degradation of various xylans and deconstructed xylo-oligosaccharides to xylose with high efficiency. Moreover, using pNPX as both the donor and acceptor, Xyl3A exhibited a transxylosylation activity to synthesize pNPX2. All these favorable properties suggest that Xyl3A has good potential applications in the bioconversion of hemicelluloses to biofuels.

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Eco-micropunching Techniques for Bioenergy Application

Guo

2021

Clean Energy Production Technologies

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Characterization of a highly efficient heterodimeric xylosidase from Humicola insolens

Cited by 15 publications

References 31 publications

Fungal enzyme sets for plant polysaccharide degradation

Fungal enzyme sets for plant polysaccharide degradation

High Level Expression of a Novel Family 3 Neutral β-Xylosidase from Humicola insolens Y1 with High Tolerance to D-Xylose

Eco-micropunching Techniques for Bioenergy Application

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