Functional diversity and properties of multiple xylanases from Penicillium oxalicum GZ-2

Liao, Hanpeng; Zheng, Haiping; Li, Shuixian; Wei, Zhong; Mei, Xinlan; Ma, Hongyu; Shen, Qirong; Xu, Yangchun

doi:10.1038/srep12631

Cited by 62 publications

(50 citation statements)

References 47 publications

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“…GH11 xylanases usually lack CBM1 domains, although some contrary cases have been described (Watanabe et al ., ; Liao et al ., ; Shi et al ., ). Yet Xyn11A showed the ability to bind xylan, which was lost by fusing a CBM1 domain to it while the xylanase activity remained unaffected.…”

Section: Discussionmentioning

confidence: 98%

Two degradation strategies for overcoming the recalcitrance of natural lignocellulosic xylan by polysaccharides‐binding GH10 and GH11 xylanases of filamentous fungi

Miao

et al. 2017

Environmental Microbiology

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The recalcitrance of lignocellulose forms a strong barrier for the bioconversion of lignocellulosic biomass in chemical or biofuel industries. Filamentous fungi are major plant biomass decomposer, and capable of forming all the required enzymes. Here, they characterized the GH10 and GH11 endo-xylanases and a CE1 acetyl-xylan esterase (Axe1) from a superior biomass-degrading strain, Aspergillus fumigatus Z5, and examined how they interact in xylan degradation. Cellulose-binding (CBM1) domain inhibited GH10 xylanase activities for pure xylan, but afforded them an ability to hydrolyze washed corncob particles (WCCP). CBM1-containing GH10 xylanases also showed synergism with CBM1-containing Axe1 in WCCP hydrolysis, and this synergy was strictly dependent on the presence of their CBM1 domains. In contrast, GH11 xylanases had no CBM1, but still could bind xylan and hydrolyzed WCCP; however, no synergism displayed with Axe1. GH10 xylanases and GH11 xylanases showed a pronounced synergism in WCCP hydrolysis, which was dependent on the presence of the CBM1 in GH10 xylanases and absence from GH11 xylanases. They exhibit different mechanisms to bind to cellulose and xylan, and act in synergy when these two structures are intact. These findings will be helpful for the further development of highly efficient enzyme mixtures for lignocellulosic biomass conversion.

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Section: Discussionmentioning

confidence: 98%

Two degradation strategies for overcoming the recalcitrance of natural lignocellulosic xylan by polysaccharides‐binding GH10 and GH11 xylanases of filamentous fungi

Miao

et al. 2017

Environmental Microbiology

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“…Shah and Madamwar reported three distinct bands of partially purified xylanases produced by Aspergillus foetidus , using Birchwood xylan (0.1% wt/vol), hence indicated the presence of multiple forms of xylanases. Similarly, employment of commercial xylan (0.1% wt/vol) by various researchers resulted in well‐defined activity bands of xylanase enzyme in polyacrylamide gels. PAGE gel containing 0.5% commercial xylan substrate and protein bands of xylanase enzyme was treated with Congo red after electrophoresis for zymogram analysis.…”

Section: Resultsmentioning

confidence: 96%

Development of novel economical methodologies for zymographic analysis of purified xylano–pectinolytic enzymes using agrowaste‐based substrates

Agrawal

Kaur

Varghese

et al. 2019

Biotechnology Progress

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In this study, zymographic analysis for xylanase and pectinase enzymes has been carried out using agrowaste residues, wheat bran and citrus peel as well as their extracts. Isozymic forms of xylanase as well as pectinase enzyme displayed comparable zymographic bands onto agar petriplates containing either commercial substrates (xylan and pectin), agrowaste‐based substrates (wheat bran and citrus peel), or polysaccharides extracted from these agrowastes (crude xylan and pectin extracted from wheat bran and citrus peel, respectively), indicating the fact that agro residues and their extracts can be utilized as a substitute of cost‐intensive commercial substrates, xylan and pectin for zymographic analysis. This is the first report revealing the zymographic analysis of xylano–pectinolytic enzymes using agro‐based solid residues particles or polysaccharides extracted from agro‐based residues.

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“…However, other fungi genera such as Fusarium , Penicillium and Chrysoporthe have been studied for this purpose 3, 5, 11, 12 .…”

Section: Introductionmentioning

confidence: 99%

A Chrysoporthe cubensis enzyme cocktail produced from a low-cost carbon source with high biomass hydrolysis efficiency

Dutra

Guimarães

Varela

et al. 2017

Sci Rep

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Low cost and high efficiency cellulolytic cocktails can consolidate lignocellulosic ethanol technologies. Sugarcane bagasse (SCB) is a low cost agro-industrial residue, and its use as a carbon source can reduce the costs of fungi cultivation for enzyme production. Chrysoporthe cubensis grown under solid state fermentation (SSF) with wheat bran has potential to produce efficient enzymatic extracts for SCB saccharification. This fungus was grown under submersed fermentation (SmF) and SSF with in natura SCB, pretreated with acid or alkali and with others carbon sources. In natura SCB induced the highest carboxymethylcellulase (CMCase), xylanase, β-xylosidase, α-galactosidase and mannanase activities by C. cubensis under SSF. In natura and washed SCB, inducers of enzyme production under SSF, did not induce high cellulases and hemicellulases production by C. cubensis in SmF. The C. cubensis enzymatic extract produced under SSF with in natura SCB as a carbon source was more efficient for lignocelulolic biomass hydrolysis than extracts produced under SSF with wheat bran and commercial cellulolytic extract. Chrysoporthe cubensis showed high potential for cellulases and hemicellulases production, especially when grown under SSF with in natura SCB as carbon source.

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Functional diversity and properties of multiple xylanases from Penicillium oxalicum GZ-2

Cited by 62 publications

References 47 publications

Two degradation strategies for overcoming the recalcitrance of natural lignocellulosic xylan by polysaccharides‐binding GH10 and GH11 xylanases of filamentous fungi

Two degradation strategies for overcoming the recalcitrance of natural lignocellulosic xylan by polysaccharides‐binding GH10 and GH11 xylanases of filamentous fungi

Development of novel economical methodologies for zymographic analysis of purified xylano–pectinolytic enzymes using agrowaste‐based substrates

A Chrysoporthe cubensis enzyme cocktail produced from a low-cost carbon source with high biomass hydrolysis efficiency

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