cbxyn10a Search Results


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  • 99
    Millipore rnase a
    Thermostability of CbCelA-TM1 in presence of CbHsp18 (A), MkHistone1 (B), and <t>RNase</t> A (C) and hydrolysis of Avicel with CbCelA-TM1 in presence of CbHsp18 (D), MkHistone1 (E), and RNase A (F). For the thermostability assay, 1 µM of CbCelA-TM1 was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The mixtures were shaken end-over-end at 70°C for 24 hr. As a control, 1 µM of CbCelA-TM1 in the same buffer was incubated without shaking at 4°C. For hydrolysis of Avicel, 1 µM of CbCelA-TM1 was incubated with 20 mg/ml Avicel in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The reaction mixtures were shaken end-over-end at 70°C for 24 hr.
    Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 29470 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    TaKaRa primestar hs dna polymerase
    Thermostability of CbCelA-TM1 in presence of CbHsp18 (A), MkHistone1 (B), and <t>RNase</t> A (C) and hydrolysis of Avicel with CbCelA-TM1 in presence of CbHsp18 (D), MkHistone1 (E), and RNase A (F). For the thermostability assay, 1 µM of CbCelA-TM1 was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The mixtures were shaken end-over-end at 70°C for 24 hr. As a control, 1 µM of CbCelA-TM1 in the same buffer was incubated without shaking at 4°C. For hydrolysis of Avicel, 1 µM of CbCelA-TM1 was incubated with 20 mg/ml Avicel in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The reaction mixtures were shaken end-over-end at 70°C for 24 hr.
    Primestar Hs Dna Polymerase, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 7828 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Megazyme arabinan
    Activity analyses of accessory xylan-degrading enzymes (CbAra51A, CbXyl3A, and CbAgu67A) from C. bescii . (A) CbAra51A released arabinose from five arabinose-containing polysaccharides (WAX, RAX, OSX, debranched <t>arabinan,</t> and arabinan). CbAra51A (0.5 μM) was incubated with each polysaccharide (2.5 mg/ml) at 75°C for 14 h. The samples were heated at 100°C to inactivate the enzyme, and appropriately diluted samples were applied to HPLC analysis. (B) Thin-layer chromatography analysis of xylo-oligosaccharides hydrolyzed by CbXyl3A. X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose; X6, xylohexaose. (C) HPLC analysis of an aldouronic acid mixture hydrolyzed by CbAgu67A, CbXyl3A, or a combination of the two enzymes. The aldouronic acid mixture (1 mg/ml) was incubated with CbXyl3A (0.5 μM) and/or CbAgu67A (0.5 μM) in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at 75°C for 14 h.
    Arabinan, supplied by Megazyme, used in various techniques. Bioz Stars score: 89/100, based on 119 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Agilent technologies cary 300 uv visible spectrophotometer
    Activity analyses of accessory xylan-degrading enzymes (CbAra51A, CbXyl3A, and CbAgu67A) from C. bescii . (A) CbAra51A released arabinose from five arabinose-containing polysaccharides (WAX, RAX, OSX, debranched <t>arabinan,</t> and arabinan). CbAra51A (0.5 μM) was incubated with each polysaccharide (2.5 mg/ml) at 75°C for 14 h. The samples were heated at 100°C to inactivate the enzyme, and appropriately diluted samples were applied to HPLC analysis. (B) Thin-layer chromatography analysis of xylo-oligosaccharides hydrolyzed by CbXyl3A. X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose; X6, xylohexaose. (C) HPLC analysis of an aldouronic acid mixture hydrolyzed by CbAgu67A, CbXyl3A, or a combination of the two enzymes. The aldouronic acid mixture (1 mg/ml) was incubated with CbXyl3A (0.5 μM) and/or CbAgu67A (0.5 μM) in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at 75°C for 14 h.
    Cary 300 Uv Visible Spectrophotometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher cmc
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Cmc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 100 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Megazyme cellulose substrate
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Cellulose Substrate, supplied by Megazyme, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Stratagene e coli bl21 codonplus de3 ripl competent cells
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    E Coli Bl21 Codonplus De3 Ripl Competent Cells, supplied by Stratagene, used in various techniques. Bioz Stars score: 88/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Stratagene escherichia coli strain xl10 gold
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Escherichia Coli Strain Xl10 Gold, supplied by Stratagene, used in various techniques. Bioz Stars score: 88/100, based on 112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Merck KGaA pet 46 ek lic plasmid
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Pet 46 Ek Lic Plasmid, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 85/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare hiload 16 60 superdex 200 gel filtration column
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Hiload 16 60 Superdex 200 Gel Filtration Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 600 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare hitrap q hp column
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Hitrap Q Hp Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 4203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare hitrap sp hp column
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; <t>OSX,</t> oat spelt xylan; BWX, birchwood xylan; <t>CMC,</t> sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Hitrap Sp Hp Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1849 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Megazyme kgm
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at <t>75°C</t> for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; <t>KGM,</t> konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Kgm, supplied by Megazyme, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Qiagen qiaquick gel extraction kit
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at <t>75°C</t> for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; <t>KGM,</t> konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Qiaquick Gel Extraction Kit, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 113321 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA t4 dna polymerase
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at <t>75°C</t> for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; <t>KGM,</t> konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    T4 Dna Polymerase, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Promega ta cloning vector pgem t
    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at <t>75°C</t> for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; <t>KGM,</t> konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.
    Ta Cloning Vector Pgem T, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Thermostability of CbCelA-TM1 in presence of CbHsp18 (A), MkHistone1 (B), and RNase A (C) and hydrolysis of Avicel with CbCelA-TM1 in presence of CbHsp18 (D), MkHistone1 (E), and RNase A (F). For the thermostability assay, 1 µM of CbCelA-TM1 was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The mixtures were shaken end-over-end at 70°C for 24 hr. As a control, 1 µM of CbCelA-TM1 in the same buffer was incubated without shaking at 4°C. For hydrolysis of Avicel, 1 µM of CbCelA-TM1 was incubated with 20 mg/ml Avicel in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The reaction mixtures were shaken end-over-end at 70°C for 24 hr.

    Journal: PLoS ONE

    Article Title: Supplementing with Non-Glycoside Hydrolase Proteins Enhances Enzymatic Deconstruction of Plant Biomass

    doi: 10.1371/journal.pone.0043828

    Figure Lengend Snippet: Thermostability of CbCelA-TM1 in presence of CbHsp18 (A), MkHistone1 (B), and RNase A (C) and hydrolysis of Avicel with CbCelA-TM1 in presence of CbHsp18 (D), MkHistone1 (E), and RNase A (F). For the thermostability assay, 1 µM of CbCelA-TM1 was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The mixtures were shaken end-over-end at 70°C for 24 hr. As a control, 1 µM of CbCelA-TM1 in the same buffer was incubated without shaking at 4°C. For hydrolysis of Avicel, 1 µM of CbCelA-TM1 was incubated with 20 mg/ml Avicel in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer. The reaction mixtures were shaken end-over-end at 70°C for 24 hr.

    Article Snippet: Hydrolysis of Birchwood Xylan and Miscanthus by CbXyn10A To determine the effect of CbHsp18, MkHistone1, and RNase A on birchwood xylan (BWX, purchased from Sigma-Aldrich, St. Louis, MO) and Miscanthus hydrolysis by the xylanase CbXyn10A, the enzyme at a final concentration of 0.25 µM (for BWX) or 1 µM (for Miscanthus) was incubated with 20 mg/ml final concentration of BWX or Miscanthus in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at a total volume of 500 µl.

    Techniques: Incubation

    Thermostability of CbXyn10A (A, B, and C) and hydrolysis of Miscanthus by CbXyn10A (D, E, and F). A–C: Thermostability of CbXyn10A in the presence of CbHsp18 (A), MkHistone1 (B), and RNase A (C). One micromolar of CbXyn10A was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer in a total volume of 500 µl. The mixtures were shaken end-over-end at 70°C for 24 hr. D–E: 1 µM of CbXyn10A was incubated with 20 mg/ml Miscanthus in the absence or presence of 8 µM, 16 µM, and 32 µM each of CbHsp18 (D), MkHistone1 (E), and RNase A (F) in a pH 6.0 citrate buffer in a total volume of 500 µl. The reaction mixtures were rotated end-over-end at 70°C for 24 hr.

    Journal: PLoS ONE

    Article Title: Supplementing with Non-Glycoside Hydrolase Proteins Enhances Enzymatic Deconstruction of Plant Biomass

    doi: 10.1371/journal.pone.0043828

    Figure Lengend Snippet: Thermostability of CbXyn10A (A, B, and C) and hydrolysis of Miscanthus by CbXyn10A (D, E, and F). A–C: Thermostability of CbXyn10A in the presence of CbHsp18 (A), MkHistone1 (B), and RNase A (C). One micromolar of CbXyn10A was incubated with 8 µM, 16 µM, or 32 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer in a total volume of 500 µl. The mixtures were shaken end-over-end at 70°C for 24 hr. D–E: 1 µM of CbXyn10A was incubated with 20 mg/ml Miscanthus in the absence or presence of 8 µM, 16 µM, and 32 µM each of CbHsp18 (D), MkHistone1 (E), and RNase A (F) in a pH 6.0 citrate buffer in a total volume of 500 µl. The reaction mixtures were rotated end-over-end at 70°C for 24 hr.

    Article Snippet: Hydrolysis of Birchwood Xylan and Miscanthus by CbXyn10A To determine the effect of CbHsp18, MkHistone1, and RNase A on birchwood xylan (BWX, purchased from Sigma-Aldrich, St. Louis, MO) and Miscanthus hydrolysis by the xylanase CbXyn10A, the enzyme at a final concentration of 0.25 µM (for BWX) or 1 µM (for Miscanthus) was incubated with 20 mg/ml final concentration of BWX or Miscanthus in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at a total volume of 500 µl.

    Techniques: Incubation

    Hydrolysis of Avicel by a binary mixture of CbCelA-TM1 and CbCdx1A. Avicel (20 mg/ml) was hydrolyzed with 1 µM each of CbCelA-TM1 and CbCdx1A in the absence or presence of 16 µM, 32 µM, and 64 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer at a total volume of 500 µl. The reactions were carried out by shaking the mixtures end-over-end at 70°C for 24 hr. The reducing ends released in all samples were determined by the PAHBAH method.

    Journal: PLoS ONE

    Article Title: Supplementing with Non-Glycoside Hydrolase Proteins Enhances Enzymatic Deconstruction of Plant Biomass

    doi: 10.1371/journal.pone.0043828

    Figure Lengend Snippet: Hydrolysis of Avicel by a binary mixture of CbCelA-TM1 and CbCdx1A. Avicel (20 mg/ml) was hydrolyzed with 1 µM each of CbCelA-TM1 and CbCdx1A in the absence or presence of 16 µM, 32 µM, and 64 µM of CbHsp18, MkHistone1, or RNase A in a pH 6.0 citrate buffer at a total volume of 500 µl. The reactions were carried out by shaking the mixtures end-over-end at 70°C for 24 hr. The reducing ends released in all samples were determined by the PAHBAH method.

    Article Snippet: Hydrolysis of Birchwood Xylan and Miscanthus by CbXyn10A To determine the effect of CbHsp18, MkHistone1, and RNase A on birchwood xylan (BWX, purchased from Sigma-Aldrich, St. Louis, MO) and Miscanthus hydrolysis by the xylanase CbXyn10A, the enzyme at a final concentration of 0.25 µM (for BWX) or 1 µM (for Miscanthus) was incubated with 20 mg/ml final concentration of BWX or Miscanthus in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at a total volume of 500 µl.

    Techniques:

    Hydrolysis of cellopentaose by CbCdx1A in the absence or presence of non-GH proteins. A: Hydrolysis of cellopentaose byCbCdx1A in absence of the non-GH proteins. Control: cellopentaose incubated alone; CbCdx1A: cellopentaose incubated with 1 µM of CbCdx1A. B–D: Hydrolysis of cellopentaose in the presence of 8 µM, 16 µM, and 32 µM of CbHsp1 (B), MkHistone1 (C), or RNase A (D). For these reactions, cellopentaose (0.68 mM) was incubated with 1 µM of CbCdx1A in the absence or presence of the non-GH proteins at 70°C for 9 min. The cellopentaose was also incubated individually with each of the three non-GH proteins (32 µM). The samples were then immediately diluted 100 times with HPLC buffer (100 mM NaOH) to inactivate the enzyme and subjected to HPLC analysis. E: The activity of CbCdx1A in absence of non-GH proteins was set as 100%, and the relative activities from the other reactions were calculated by dividing their corresponding activities with this reference activity. F: Thermostability of CbCdx1A at 70°C. One micromolar of CbCdx1A was shaken end-over-end at 70°C in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp1, MkHistone1, or RNase A in a volume of 500 µl; at the same time, 1 µM of CbCdx1A was kept incubated without shaking at 4°C as a control. After 24 hr, the residual activities were measured for all samples using p -NP-β-D-glucopyranoside as the substrate. The activity of the sample at 4°C was set as 100%, and the residual activities for the other samples were calculated by dividing their activities by that of the sample incubated at 4°C.

    Journal: PLoS ONE

    Article Title: Supplementing with Non-Glycoside Hydrolase Proteins Enhances Enzymatic Deconstruction of Plant Biomass

    doi: 10.1371/journal.pone.0043828

    Figure Lengend Snippet: Hydrolysis of cellopentaose by CbCdx1A in the absence or presence of non-GH proteins. A: Hydrolysis of cellopentaose byCbCdx1A in absence of the non-GH proteins. Control: cellopentaose incubated alone; CbCdx1A: cellopentaose incubated with 1 µM of CbCdx1A. B–D: Hydrolysis of cellopentaose in the presence of 8 µM, 16 µM, and 32 µM of CbHsp1 (B), MkHistone1 (C), or RNase A (D). For these reactions, cellopentaose (0.68 mM) was incubated with 1 µM of CbCdx1A in the absence or presence of the non-GH proteins at 70°C for 9 min. The cellopentaose was also incubated individually with each of the three non-GH proteins (32 µM). The samples were then immediately diluted 100 times with HPLC buffer (100 mM NaOH) to inactivate the enzyme and subjected to HPLC analysis. E: The activity of CbCdx1A in absence of non-GH proteins was set as 100%, and the relative activities from the other reactions were calculated by dividing their corresponding activities with this reference activity. F: Thermostability of CbCdx1A at 70°C. One micromolar of CbCdx1A was shaken end-over-end at 70°C in the absence or presence of 8 µM, 16 µM, or 32 µM of CbHsp1, MkHistone1, or RNase A in a volume of 500 µl; at the same time, 1 µM of CbCdx1A was kept incubated without shaking at 4°C as a control. After 24 hr, the residual activities were measured for all samples using p -NP-β-D-glucopyranoside as the substrate. The activity of the sample at 4°C was set as 100%, and the residual activities for the other samples were calculated by dividing their activities by that of the sample incubated at 4°C.

    Article Snippet: Hydrolysis of Birchwood Xylan and Miscanthus by CbXyn10A To determine the effect of CbHsp18, MkHistone1, and RNase A on birchwood xylan (BWX, purchased from Sigma-Aldrich, St. Louis, MO) and Miscanthus hydrolysis by the xylanase CbXyn10A, the enzyme at a final concentration of 0.25 µM (for BWX) or 1 µM (for Miscanthus) was incubated with 20 mg/ml final concentration of BWX or Miscanthus in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at a total volume of 500 µl.

    Techniques: Incubation, High Performance Liquid Chromatography, Activity Assay

    Schematic domain structures (A) and SDS-PAGE analysis (B) of the non-GH proteins and glycoside hydrolases. A: A schematic representation of the polypeptides of CbHsp18, MkHistone1, and the three glycoside hydrolases of C. bescii used in this study. GH9: Glycoside hydrolase family 9 domain; CBM3c: Carbohydrate binding module family 3 type C. B: SDS-PAGE analysis of purified recombinant non-GH proteins and the three glycoside hydrolases of C. bescii . Lane 1: molecular mass markers; lane 2: CbHsp18; lane 3: MkHistone1; lane 4: RNase A; lane 5: CbCelA-TM1; lane 6: CbCdx1A; lane 7: CbXyn10A. Two micrograms of each protein were resolved by 12% SDS-PAGE. RNase A was a commercial product (Roche).

    Journal: PLoS ONE

    Article Title: Supplementing with Non-Glycoside Hydrolase Proteins Enhances Enzymatic Deconstruction of Plant Biomass

    doi: 10.1371/journal.pone.0043828

    Figure Lengend Snippet: Schematic domain structures (A) and SDS-PAGE analysis (B) of the non-GH proteins and glycoside hydrolases. A: A schematic representation of the polypeptides of CbHsp18, MkHistone1, and the three glycoside hydrolases of C. bescii used in this study. GH9: Glycoside hydrolase family 9 domain; CBM3c: Carbohydrate binding module family 3 type C. B: SDS-PAGE analysis of purified recombinant non-GH proteins and the three glycoside hydrolases of C. bescii . Lane 1: molecular mass markers; lane 2: CbHsp18; lane 3: MkHistone1; lane 4: RNase A; lane 5: CbCelA-TM1; lane 6: CbCdx1A; lane 7: CbXyn10A. Two micrograms of each protein were resolved by 12% SDS-PAGE. RNase A was a commercial product (Roche).

    Article Snippet: Hydrolysis of Birchwood Xylan and Miscanthus by CbXyn10A To determine the effect of CbHsp18, MkHistone1, and RNase A on birchwood xylan (BWX, purchased from Sigma-Aldrich, St. Louis, MO) and Miscanthus hydrolysis by the xylanase CbXyn10A, the enzyme at a final concentration of 0.25 µM (for BWX) or 1 µM (for Miscanthus) was incubated with 20 mg/ml final concentration of BWX or Miscanthus in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at a total volume of 500 µl.

    Techniques: SDS Page, Binding Assay, Purification, Recombinant

    Activity analyses of accessory xylan-degrading enzymes (CbAra51A, CbXyl3A, and CbAgu67A) from C. bescii . (A) CbAra51A released arabinose from five arabinose-containing polysaccharides (WAX, RAX, OSX, debranched arabinan, and arabinan). CbAra51A (0.5 μM) was incubated with each polysaccharide (2.5 mg/ml) at 75°C for 14 h. The samples were heated at 100°C to inactivate the enzyme, and appropriately diluted samples were applied to HPLC analysis. (B) Thin-layer chromatography analysis of xylo-oligosaccharides hydrolyzed by CbXyl3A. X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose; X6, xylohexaose. (C) HPLC analysis of an aldouronic acid mixture hydrolyzed by CbAgu67A, CbXyl3A, or a combination of the two enzymes. The aldouronic acid mixture (1 mg/ml) was incubated with CbXyl3A (0.5 μM) and/or CbAgu67A (0.5 μM) in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at 75°C for 14 h.

    Journal: Applied and Environmental Microbiology

    Article Title: Reconstitution of a Thermostable Xylan-Degrading Enzyme Mixture from the Bacterium Caldicellulosiruptor bescii

    doi: 10.1128/AEM.03265-12

    Figure Lengend Snippet: Activity analyses of accessory xylan-degrading enzymes (CbAra51A, CbXyl3A, and CbAgu67A) from C. bescii . (A) CbAra51A released arabinose from five arabinose-containing polysaccharides (WAX, RAX, OSX, debranched arabinan, and arabinan). CbAra51A (0.5 μM) was incubated with each polysaccharide (2.5 mg/ml) at 75°C for 14 h. The samples were heated at 100°C to inactivate the enzyme, and appropriately diluted samples were applied to HPLC analysis. (B) Thin-layer chromatography analysis of xylo-oligosaccharides hydrolyzed by CbXyl3A. X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose; X6, xylohexaose. (C) HPLC analysis of an aldouronic acid mixture hydrolyzed by CbAgu67A, CbXyl3A, or a combination of the two enzymes. The aldouronic acid mixture (1 mg/ml) was incubated with CbXyl3A (0.5 μM) and/or CbAgu67A (0.5 μM) in a citrate buffer (50 mM sodium citrate, 150 mM NaCl, pH 6.0) at 75°C for 14 h.

    Article Snippet: The activities of CbXyn10A and CbXyn10B on different polysaccharides were screened by incubating 0.5 μM each enzyme with 2.5 mg/ml xylan substrates (wheat arabinoxylan, WAX; oat spelt xylan, OSX; birchwood xylan, BWX), cellulose substrate (sodium carboxymethyl cellulose, CMC), 1,4-β- d -mannan, konjac glucomannan (KGM), and arabinan at 75°C for 14 h. WAX, 1,4-β- d -mannan, and KGM were purchased from Megazyme (Wicklow, Ireland), OSX and BWX were from Sigma-Aldrich (St. Louis, MO), and CMC was from Acros Organics (Geel, Belgium).

    Techniques: Activity Assay, Incubation, High Performance Liquid Chromatography, Thin Layer Chromatography

    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.

    Journal: Applied and Environmental Microbiology

    Article Title: Reconstitution of a Thermostable Xylan-Degrading Enzyme Mixture from the Bacterium Caldicellulosiruptor bescii

    doi: 10.1128/AEM.03265-12

    Figure Lengend Snippet: Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.

    Article Snippet: The activities of CbXyn10A and CbXyn10B on different polysaccharides were screened by incubating 0.5 μM each enzyme with 2.5 mg/ml xylan substrates (wheat arabinoxylan, WAX; oat spelt xylan, OSX; birchwood xylan, BWX), cellulose substrate (sodium carboxymethyl cellulose, CMC), 1,4-β- d -mannan, konjac glucomannan (KGM), and arabinan at 75°C for 14 h. WAX, 1,4-β- d -mannan, and KGM were purchased from Megazyme (Wicklow, Ireland), OSX and BWX were from Sigma-Aldrich (St. Louis, MO), and CMC was from Acros Organics (Geel, Belgium).

    Techniques: Thin Layer Chromatography, Incubation

    Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.

    Journal: Applied and Environmental Microbiology

    Article Title: Reconstitution of a Thermostable Xylan-Degrading Enzyme Mixture from the Bacterium Caldicellulosiruptor bescii

    doi: 10.1128/AEM.03265-12

    Figure Lengend Snippet: Screening for the activities of CbXyn10A and CbXyn10B on plant polysaccharides with different glycosidic linkages. (A) Reducing sugar analysis. (B and C) Thin-layer chromatography analysis (CbXyn10A [B] and CbXyn10B [C]). The plant polysaccharides were incubated separately with either CbXyn10A or CbXyn10B at 75°C for 14 h. The amounts of released reducing sugar were determined by the p HBAH method. To determine the components of the released sugars in the hydrolyzed products, the samples were appropriately diluted and subjected to TLC analysis. WAX, wheat arabinoxylan; OSX, oat spelt xylan; BWX, birchwood xylan; CMC, sodium carboxymethyl cellulose; KGM, konjac glucomannan; X1, xylose; X2, xylobiose; X3, xylotriose; X4, xylotetraose; X5, xylopentaose.

    Article Snippet: The activities of CbXyn10A and CbXyn10B on different polysaccharides were screened by incubating 0.5 μM each enzyme with 2.5 mg/ml xylan substrates (wheat arabinoxylan, WAX; oat spelt xylan, OSX; birchwood xylan, BWX), cellulose substrate (sodium carboxymethyl cellulose, CMC), 1,4-β- d -mannan, konjac glucomannan (KGM), and arabinan at 75°C for 14 h. WAX, 1,4-β- d -mannan, and KGM were purchased from Megazyme (Wicklow, Ireland), OSX and BWX were from Sigma-Aldrich (St. Louis, MO), and CMC was from Acros Organics (Geel, Belgium).

    Techniques: Thin Layer Chromatography, Incubation