Measurement of xylanase activity with insoluble xylan substrate

Nummi, Martti; Perrin, Jennifer; Niku‐Paavola, Marja‐Leena; Enari, Tor-Magnus

doi:10.1042/bj2260617

Cited by 28 publications

(13 citation statements)

References 4 publications

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“…In the hydrolysis with T. reesei enzymes the rapid removal of the hydrophilic acidic side groups may render the substrates less soluble. However, the good solubilizing activity of T. reesei xylanase has already been demonstrated (Nummi et al 1985).…”

Section: Resultsmentioning

confidence: 98%

The hydrolysis of steamed birchwood hemicellulose by enzymes produced byTrichoderma reesei andAspergillus awamori

Poutanen

Puls²,

Linko

1986

Appl Microbiol Biotechnol

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Section: Resultsmentioning

confidence: 98%

The hydrolysis of steamed birchwood hemicellulose by enzymes produced byTrichoderma reesei andAspergillus awamori

Poutanen

Puls²,

Linko

1986

Appl Microbiol Biotechnol

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“…Alkali-extractable xylans from rice straw were prepared as described previously [19]. Recombinant endoxylanase xynR8 (0.4 U) [16] alone or with 1 U RuXyn1 was incubated with 1 ml 2% (w/v) birchwood xylan (Sigma) or rice straw xylan in 50 mM phosphate/citrate buffer at pH 6.5 and 40°C for 3 h. Hydrolysis of xylans by endoxylanase coupled with RuXyn2 was conducted under the same substrate concentrations and units of enzymes unless the reaction condition was set at pH 5.5 and 40°C.…”

Section: Hydrolysis Of Hemicellulosic Substratesmentioning

confidence: 99%

Biochemical and kinetic characterization of GH43 β-d-xylosidase/α-l-arabinofuranosidase and GH30 α-l-arabinofuranosidase/β-d-xylosidase from rumen metagenome

Zhou

Bao

Chang

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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The present study focuses on characterization of two hemicellulases, RuXyn1 and RuXyn2, from rumen bacterial metagenome and their capabilities for degradation of xylans. Glycosyl hydrolase (GH) family 43 β-D -xylosidase/α-L -arabinofuranosidase RuXyn1 can hydrolyze p-nitrophenyl-β-D -xylopyranoside (pNPX), p-nitrophenyl-α-L -arabinofuranoside (pNPA), and xylo-oligosaccharide substrates, while GH30 1,5-α-L -arabinofuranosidase/β-D -xylosidase RuXyn2, the first α-L -arabinofuranosidase assigned to this GH family, shows activities towards 1,5-α-L -arabinobiose and pNPX substrates but no activity for pNPA. Kinetic analysis for aryl-glycosides revealed that RuXyn2 had higher catalytic efficiency than RuXyn1 toward pNPX substrate. RuXyn1 shows high synergism with endoxylanase, elevating by 73% the reducing sugars released from brichwood xylans, and converted most intermediate xylo-oligosaccharide hydrolysate into xylose. The high xylose conversion capability of RuXyn1 suggests it has potential applications in enzymatic production of xylose and improvement of hemicellulose saccharification for production of biofuels. RuXyn2 shows no obviously synergistic effect in the endoxylanase-coupled assay for enzymatic saccharification of xylan. Further cosmid DNA sequencing revealed a neighboring putative GH43 α-L -arabinofuranosidase RuAra1 and two putative GH3 β-xylosidase/arabinosidases, RuXyn3 and RuXyn5, downstream of RuXyn2, indicating that this hemicellulase gene cluster may be responsible for production of end-product, xylose and arabinose, from hemicellulose biomass.

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“…The dinitrosalicylic acid (DNS) method was used, and one enzymatic activity unit was defined as that required for the generation of 1 μmol of glucose or xylose per min in 1 ml of enzyme solution (IUPAC 1987; Zhang et al 2009; Nummi et al 1985). …”

Section: Methodsmentioning

confidence: 99%

Construction of recombinant sestc Saccharomyces cerevisiae for consolidated bioprocessing, cellulase characterization, and ethanol production by in situ fermentation

2016

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Bioethanol is an important oil substitute produced by the sugar fermentation process. To improve the efficiency of cellulase expression of Saccharomyces cerevisiae, a eukaryotic expression vector harboring a singleenzyme-system-three-cellulase gene (sestc) was integrated into the S. cerevisiae genome by the protoplast method. Using PCR screening, RT-PCR, and ''transparent circle'' detection, several recombinant S. cerevisiae strains, capable of efficiently expressing the heterogeneous cellulase, were selected. The total activity of cellulase, endo-b-Dglucanase, exo-b-D-glucanase, and xylanase of the recombinant S. cerevisiae transformant (designated number 14) was 1.1, 378, 1.44, and 164 U ml -1 , respectively, which was 27.5-, 63-, 24-, and 19-fold higher than that of the wild-type strain. The concentration of ethanol produced by the engineered S. cerevisiae strain was 8.1 gl -1 , with wheat bran as the carbon source, under submerged conditions; this was 57.86-fold higher than that produced by the wild-type strain (0.14 gl -1 ).

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Measurement of xylanase activity with insoluble xylan substrate

Cited by 28 publications

References 4 publications

The hydrolysis of steamed birchwood hemicellulose by enzymes produced byTrichoderma reesei andAspergillus awamori

The hydrolysis of steamed birchwood hemicellulose by enzymes produced byTrichoderma reesei andAspergillus awamori

Biochemical and kinetic characterization of GH43 β-d-xylosidase/α-l-arabinofuranosidase and GH30 α-l-arabinofuranosidase/β-d-xylosidase from rumen metagenome

Construction of recombinant sestc Saccharomyces cerevisiae for consolidated bioprocessing, cellulase characterization, and ethanol production by in situ fermentation

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