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Xylan (Beechwood)

Xylan Beechwood P-XYLNBE
Product code: P-XYLNBE-10G



10 g

Prices exclude VAT

Available for shipping

Content: 10 g or 50 g
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: 9014-63-5
Source: Beechwood
Purity: > 95%
Monosaccharides (%): Xylose: Glucuronic Acid: Other sugars = 80.8: 11.4: 7.8
Main Chain Glycosidic Linkage: β-1,4 and α-1,2
Substrate For (Enzyme): endo-1,4-β-Xylanase

Highly purified xylan from beechwood for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Suitable as a replacement for birchwood xylan as a substrate for β-xylanase in DNSA reducing sugar assay.

Data booklets for each pack size are located in the Documents tab.

Megazyme publication
Novel substrates for the automated and manual assay of endo-1,4-β-xylanase.

Mangan, D., Cornaggia, C., Liadova, A., McCormack, N., Ivory, R., McKie, V. A., Ormerod, A. & McCleary, D. V. (2017). Carbohydrate Research, 445, 14-22.

endo-1,4-β-Xylanase (EC is employed across a broad range of industries including animal feed, brewing, baking, biofuels, detergents and pulp (paper). Despite its importance, a rapid, reliable, reproducible, automatable assay for this enzyme that is based on the use of a chemically defined substrate has not been described to date. Reported herein is a new enzyme coupled assay procedure, termed the XylX6 assay, that employs a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitrophenyl-β-45-O-glucosyl-xylopentaoside. The development of the substrate and associated assay is discussed here and the relationship between the activity values obtained with the XylX6 assay versus traditional reducing sugar assays and its specificity and reproducibility were thoroughly investigated.

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Megazyme publication
A Comparison of Polysaccharide Substrates and Reducing Sugar Methods for the Measurement of endo-1,4-β-Xylanase.

McCleary, B. V. & McGeough, P. (2015). Appl. Biochem. Biotechnol., 177(5), 1152-1163.

The most commonly used method for the measurement of the level of endo-xylanase in commercial enzyme preparations is the 3,5-dinitrosalicylic acid (DNS) reducing sugar method with birchwood xylan as substrate. It is well known that with the DNS method, much higher enzyme activity values are obtained than with the Nelson-Somogyi (NS) reducing sugar method. In this paper, we have compared the DNS and NS reducing sugar assays using a range of xylan-type substrates and accurately compared the molar response factors for xylose and a range of xylo-oligosaccharides. Purified beechwood xylan or wheat arabinoxylan is shown to be a suitable replacement for birchwood xylan which is no longer commercially available, and it is clearly demonstrated that the DNS method grossly overestimates endo-xylanase activity. Unlike the DNS assay, the NS assay gave the equivalent colour response with equimolar amounts of xylose, xylobiose, xylotriose and xylotetraose demonstrating that it accurately measures the quantity of glycosidic bonds cleaved by the endo-xylanase. The authors strongly recommend cessation of the use of the DNS assay for measurement of endo-xylanase due to the fact that the values obtained are grossly overestimated due to secondary reactions in colour development.

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Feruloyl esterase (FAE-1) sourced from a termite hindgut and GH10 xylanases synergy improves degradation of arabinoxylan.

Mafa, M. S., Malgas, S. & Pletschke, B. I. (2021). AMB Express, 11(1), 1-9.

Cereal feedstocks have high arabinoxylan content as their main hemicellulose, which is linked to lignin by hydroxycinnamic acids such as ferulic acid. The ferulic acid is linked to arabinoxylan by ester bonds, and generally, the high substitution of ferulic acid leads to a loss of activity of xylanases targeting the arabinoxylan. In the current study, a feruloyl esterase (FAE-1) from a termite hindgut bacteria was functionally characterised and used in synergy with xylanases during xylan hydrolysis. The FAE-1 displayed temperature and pH optima of 60℃ and 7.0, respectively. FAE-1 did not release reducing sugars from beechwood xylan (BWX), wheat arabinoxylan (WAX) and oat spelt xylan (OX), however, displayed high activity of 164.74 U/mg protein on p-nitrophenyl-acetate (pNPA). In contrast, the GH10 xylanases; Xyn10 and XT6, and a GH11 xylanase, Xyn2A, showed more than two-fold increased activity on xylan substrates with low sidechain substitutions; BWX and OX, compared to the highly branched substrate, WAX. Interestingly, the FAE-1 and GH10 xylanases (Xyn10D and XT6) displayed a degree of synergy (DS) that was higher than 1 in all enzyme loading combinations during WAX hydrolysis. The 75%XT6:25%FAE-1 synergistic enzyme combination increased the release of reducing sugars by 1.34-fold from WAX compared to the control, while 25%Xyn10D:75%FAE-1 synergistic combination released about 2.1-fold of reducing sugars from WAX compared to controls. These findings suggest that FAE-1 can be used in concert with xylanases, particularly those from GH10, to efficiently degrade arabinoxylans contained in cereal feedstocks for various industrial settings such as in animal feeds and baking.

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Characterization of efficient xylanases from industrial-scale pulp and paper wastewater treatment microbiota.

Wang, J., Liang, J., Li, Y., Tian, L. & Wei, Y. (2021). AMB Express, 11(1), 1-11.

Xylanases are widely used enzymes in the food, textile, and paper industries. Most efficient xylanases have been identified from lignocellulose-degrading microbiota, such as the microbiota of the cow rumen and the termite hindgut. Xylanase genes from efficient pulp and paper wastewater treatment (PPWT) microbiota have been previously recovered by metagenomics, assigning most of the xylanase genes to the GH10 family. In this study, a total of 40 GH10 family xylanase genes derived from a certain PPWT microbiota were cloned and expressed in Escherichia coli BL21 (DE3). Among these xylanase genes, 14 showed xylanase activity on beechwood substrate. Two of these, PW-xyl9 and PW-xyl37, showed high activities, and were purified to evaluate their xylanase properties. Values of optimal pH and temperature for PW-xyl9 were pH 7 and 60℃, respectively, while those for PW-xyl37 were pH 7 and 55℃, respectively; their specific xylanase activities under optimal conditions were 470.1 U/mg protein and 113.7 U/mg protein, respectively. Furthermore, the Km values of PW-xyl9 and PW-xyl37 were determined as 8.02 and 18.8 g/L, respectively. The characterization of these two xylanases paves the way for potential application in future pulp and paper production and other industries, indicating that PPWT microbiota has been an undiscovered reservoir of efficient lignocellulase genes. This study demonstrates that a metagenomic approach has the potential to screen efficient xylanases of uncultured microorganisms from lignocellulose-degrading microbiota. In a similar way, other efficient lignocellulase genes might be identified from PPWT treatment microbiota in the future.

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Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species.

Li, J., Solhi, L., Goddard-Borger, E. D., Mathieu, Y., Wakarchuk, W. W., Withers, S. G. & Brumer, H. (2021). Biotechnology for Biofuels, 14(1), 1-19.

Background: The discovery of lytic polysaccharide monooxygenases (LPMOs) has fundamentally changed our understanding of microbial lignocellulose degradation. Cellulomonas bacteria have a rich history of study due to their ability to degrade recalcitrant cellulose, yet little is known about the predicted LPMOs that they encode from Auxiliary Activity Family 10 (AA10). Results: Here, we present the comprehensive biochemical characterization of three AA10 LPMOs from Cellulomonas flavigena (CflaLPMO10A, CflaLPMO10B, and CflaLPMO10C) and one LPMO from Cellulomonas fimi (CfiLPMO10). We demonstrate that these four enzymes oxidize insoluble cellulose with C1 regioselectivity and show a preference for substrates with high surface area. In addition, CflaLPMO10B, CflaLPMO10C, and CfiLPMO10 exhibit limited capacity to perform mixed C1/C4 regioselective oxidative cleavage. Thermostability analysis indicates that these LPMOs can refold spontaneously following denaturation dependent on the presence of copper coordination. Scanning and transmission electron microscopy revealed substrate-specific surface and structural morphological changes following LPMO action on Avicel and phosphoric acid-swollen cellulose (PASC). Further, we demonstrate that the LPMOs encoded by Cellulomonas flavigena exhibit synergy in cellulose degradation, which is due in part to decreased autoinactivation. Conclusions: Together, these results advance understanding of the cellulose utilization machinery of historically important Cellulomonas species beyond hydrolytic enzymes to include lytic cleavage. This work also contributes to the broader mapping of enzyme activity in Auxiliary Activity Family 10 and provides new biocatalysts for potential applications in biomass modification.

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Location of uronic acid group in Japanese cedar and Japanese beech wood cell walls as evaluated by the influences of minerals on thermal reactivity.

Wang, J., Minami, E. & Kawamoto, H. (2021). Journal of Wood Science, 67(1), 1-8.

The thermal reactivities of cellulose and hemicellulose are significantly different in cell walls when compared with isolated components and differ in Japanese cedar (softwood) and Japanese beech (hardwood). Uronic acid bound to xylan promotes the thermal degradation of cellulose and hemicellulose, and its effect is different depending on the form of free acid (acting as an acid catalyst) or metal uronate (acting as a base catalyst). We evaluated the location of uronic acid in the cell wall by identifying the components affected by demineralization in pyrolysis of cedar and beech wood. The thermal reactivities of xylan and glucomannan in beech were changed by demineralization, but in cedar, glucomannan and cellulose reactivities were changed. Therefore, the location of uronic acid in the cell wall was established and differed between cedar and beech; close to glucomannan and xylan in beech, but close to glucomannan and cellulose in cedar. Such information is important for understanding the ultrastructure and pyrolysis behavior of softwood and hardwood cell walls.

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Functional analyses of xylanolytic enzymes involved in xylan degradation and utilization in Neurospora crassa.

Wang, R. & Arioka, M. (2020). International Journal of Biological Macromolecules, 169, 302-310.

Neurospora crassa possesses six putative xylanases and four putative xylosidases. qRT-PCR results showed that the expression of all these xylanolytic enzymes was induced by xylan. Except for two intracellular β-xylosidases, others were shown to be secreted enzymes based on the localization analysis of EGFP-fusion proteins. Among them, GH10-1, GH10-2, GH11-1, and GH11-2 were successfully expressed and characterized as typical endo-β-1,4-xylanases that hydrolyze the xylooligosaccharides with a polymeric degree not less than three or four. Strains deleted for either gh10-1, gh10-2, gh3-7, or gh3-8 displayed decreased growth in xylan and biomass media. Disruption of gh3-7 or gh43-1 resulted in enhanced-xylanolytic enzyme activity when cultivated in biomass medium. Collectively, these results suggest that xylooligosaccharides released by the actions of xylanases and xylosidases not only serve as the carbon sources to maintain the growth of N. crassa, but they also act as inducers to trigger the expression of hydrolytic enzymes in vivo.

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Saccharogenic refining of Ginkgo biloba leaf residues using a cost-effective enzyme cocktail prepared by the fungal strain A32 isolated from ancient ginkgo biloba tree.

Wang, J., Lei, Z., Zhang, Y., Lu, W., Li, S., Luo, W. & Song, P. (2020). Bioresource Technology, 317, 123980.

To reduce environmental pollution and waste of biomass from Ginkgo biloba leaf residues (GBLRs), we developed a cost-effective enzyme system to hydrolyze GBLRs into available reducing sugars (RS). Biomass characteristics of GBLRs were investigated, which indicated that the acid hydrolyzed fraction was 49.43% of the dry weight of GBLRs. The fraction could be effectively converted into RS by an enzyme cocktail with high polygalacturonase activity without traditionally intricate pretreatment. The strain A32 isolated from the ancient ginkgo soil was used for the production of the enzyme cocktail, and a response surface methodology was used to optimize the enzymatic production. The enzyme cocktail released 87.2% of RS from GBLRs at 35°C for 72 h with 1% (m/v) of loading, and the RS concentration arrived 8.95 ± 0.39 mg/ml with 9% of GBLRs loading. The cost-effective system of self-prepared enzyme cocktail is promising for facilitating GBLRs' bio-based industry.

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Improving the catalytic activity of thermostable xylanase from Thermotoga maritima via mutagenesis of non-catalytic residues at glycone subsites.

Yang, J., Ma, T., Shang-guan, F. & Han, Z. (2020). Enzyme and Microbial Technology, 139, 109579.

Endo-β-1,4-xylanase from Thermotoga maritima, TmxB, is an industrially attractive enzyme due to its extreme thermostability. To improve its application value, four variants were designed on the basis of multiple sequence and three-dimensional structure alignments. Wild-type TmxB (wt-TmxB) and its mutants were produced via a Pichia pastoris expression system. Among four single-site mutants, the tyrosine substitution of a threonine residue (T74Y) at putative -3/-4 subsite led to a 1.3-fold increase in specific activity at 40°C - 100°C and pH 5 for 5 min, with beechwood xylan as the substrate. T74Y had an improved catalytic efficiency (k>cat/K>m), being 1.6 times that of wt-TmxB. Variants DY (two amino acid insertions) and N68Q displayed a slight increase (1.2 fold) and dramatic decline (1.7 fold) in catalytic efficiency, respectively. Mutant E67Y was totally inactive under all test conditions. Structural modeling and docking simulation elucidated structural insights into the molecular mechanism of activity changes for these TmxB variants. This study helps in further understanding the roles of the non-catalytic amino acids at the glycone subsites of xylanases from glycoside hydrolase family 10.

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Biochemical Characterization of an Extracellular Xylanase from Aestuariibacter sp. PX-1 Newly Isolated from the Coastal Seawater of Jeju Island in Korea.

Kim, J. H. (2020). Microbiology and Biotechnology Letters, 48(2), 215-222.

The marine microorganism PX-1, which can hydrolyze xylan, was isolated from coastal sea water of Jeju Island, Korea. Based on the 16S rRNA gene sequence and chemotaxonomy analysis, PX-1 was identified as a species of the genus Aestuariibacter and named Aestuariibacter sp PX-1. From the culture broth of PX-1, an extracellular xylanase was purified to homogeneity through ammonium sulfate precipitation and subsequent adsorption chromatography using insoluble xylan. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography estimated the molecular weight of the purified putative xylanase (XylA) as approximately 64 kDa. XylA showed xylanase activity toward beechwood xylan, with a maximum enzymatic activity at pH 6.0 and 45°C. Through thin-layer chromatographic analysis of the xylan hydrolysate produced by XylA, it was confirmed that XylA is an endo-type xylanase that decomposes xylan into xylose and xyloligosaccharides of various lengths. The Km and Vmax values of XylA for beechwood xylan were 27.78 mM and 78.13 μM/min, respectively.

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Identification of a unique 1, 4-β-d-glucan glucohydrolase of glycoside hydrolase family 9 from Cytophaga hutchinsonii.

Jiang, N., Ma, X. D., Fu, L. H., Li, C. X., Feng, J. X. & Duan, C. J. (2020). Applied Microbiology and Biotechnology, 1-16.

Cytophaga hutchinsonii is an aerobic cellulolytic soil bacterium that rapidly digests crystalline cellulose. The predicted mechanism by which C. hutchinsonii digests cellulose differs from that of other known cellulolytic bacteria and fungi. The genome of C. hutchinsonii contains 22 glycoside hydrolase (GH) genes, which may be involved in cellulose degradation. One predicted GH with uncertain specificity, CHU_0961, is a modular enzyme with several modules. In this study, phylogenetic tree of the catalytic modules of the GH9 enzymes showed that CHU_0961 and its homologues formed a new group (group C) of GH9 enzymes. The catalytic module of CHU_0961 (CHU_0961B) was identified as a 1,4-β-D-glucan glucohydrolase (EC that has unique properties compared with known GH9 cellulases. CHU_0961B showed highest activity against barley glucan, but low activity against other polysaccharides. Interestingly, CHU_0961B showed similar activity against ρ-nitrophenyl β-D-cellobioside (ρ-NPC) and ρ-nitrophenyl β-D-glucopyranoside. CHU_0961B released glucose from the nonreducing end of cello-oligosaccharides, ρ-NPC, and barley glucan in a nonprocessive exo-type mode. CHU_0961B also showed same hydrolysis mode against deacetyl-chitooligosaccharides as against cello-oligosaccharides. The kcat/Km values for CHU_0961B against cello-oligosaccharides increased as the degree of polymerization increased, and its kcat/Km for cellohexose was 750 times higher than that for cellobiose. Site-directed mutagenesis showed that threonine 321 in CHU_0961 played a role in hydrolyzing cellobiose to glucose. CHU_0961 may act synergistically with other cellulases to convert cellulose to glucose on the bacterial cell surface. The end product, glucose, may initiate cellulose degradation to provide nutrients for bacterial proliferation in the early stage of C. hutchinsonii growth.

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Effects of Combined α-Amylase and Endo-Xylanase Treatments on the Properties of Fresh and Frozen Doughs and Final Breads.

Kim, H. J. & Yoo, S. H. (2020). Polymers, 12(6), 1349.

Frozen bread doughs usually exhibit less bread volume and poor texture due to dough weakening as well as reduced yeast viability. The objectives of this study were to improve the textural properties of frozen bread dough by applying carbohydrate-active enzymes, α-amylase and endo-xylanase. Each enzyme was applied to dough formulation at 20 (748 and 3.5 units, respectively) and 100 ppm levels of flour, and their combined treatments were also applied. Enzyme-treated doughs were kept frozen at −20°C for 2 weeks, and then baked following the official American Association of Cereal Chemists (AACC) method. A texture profile analysis of oven-baked breads was performed at 25°C after a 5-day storage period. α-Amylase treatment at a 100 ppm level increased the specific bread volume by 24.5% and 21.9% when compared to untreated fresh and frozen bread doughs, respectively, and decreased crumb hardness by 63.4% and 58.3%; endo-xylanase (100 ppm) also decreased crumb hardness by 56.9% and 26.9%. The combined use of α-amylase and endo-xylanase retarded bread hardening synergistically after a 5-day storage period.

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Purification and characterization of a native lytic polysaccharide monooxygenase from Thermoascus aurantiacus.

Fritsche, S., Hopson, C., Gorman, J., Gabriel, R. & Singer, S. W. (2020). Biotechnology Letters, 1-9.

Lytic polysaccharide monooxygenases (LPMOs) have emerged as key proteins for depolymerization of cellulose. These copper-containing enzymes oxidize C-1 and/or C-4 bonds in cellulose, promoting increased hydrolysis of the oxidized cellulose chains. The LPMO from Thermoascus aurantiacus, a thermophilic ascomycete fungus, has been extensively studied and has served as a model LPMO. A method was developed to purify the LPMO from culture filtrates of T. aurantiacus along with its native cellobiohydrolase and endoglucanase. The activity of the purified LPMO was measured with a colorimetric assay that established the Topt of the native LPMO at 60°C. Purification of the components of the T. aurantiacus cellulase mixture also enabled quantification of the amounts of cellobiohydrolase, endoglucanase and LPMO present in the T. aurantiacus culture filtrate, establishing that the LPMO was the most abundant protein in the culture supernatants. The importance of the LPMO to activity of the mixture was demonstrated by saccharifications with Avicel and acid-pretreated corn stover.

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Comparative characterization of extracellular enzymes secreted by Phanerochaete chrysosporium during solid-state and submerged fermentation.

Liu, J., Yang, J., Wang, R., Liu, L., Zhang, Y., Bao, H., Myong Jang, J., M., Wang, E. & Yuan, H. (2020). International Journal of Biological Macromolecules, 152, 288-294.

Influence of water content on the expression of lignocellulolytic enzymes by Phanerochaete chrysosporium remains unclear. This work compares the enzyme production profiles of P. chrysosporium during solid-state and submerged fermentation. There were 110 and 64 extracellular carbohydrate-active enzymes identified in solid-state and submerged fermentation respectively, among which 57 enzymes were common to both of the secretomes. P. chrysosporium secreted more cellulases (especially lytic polysaccharide monooxygenase) and hemicellulases during solid-state fermentation while the proportion of enzyme containing carbohydrate-binding module was higher for submerged fermentation. Although its activities were weaker, the enzyme cocktail from submerged fermentation was surprisingly more effective in hydrolysis at low substrate loading. This advantage of enzymes from submerged fermentation was mainly attributed to carbohydrate-binding module because more xylanases bound with substrate at the beginning of hydrolysis. These results reveal the influence of fermentation conditions on enzyme produced by P. chrysosporium for the first time and show the importance of carbohydrate-binding module in the hydrolysis process of lignocellulose.

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Characteristics of a XIP‐resistant xylanase from Neocallimastix sp. GMLF 1 and its advantage in barley malt saccharification.

Zhu, D., Liu, X., Xie, X., Yang, S., Lin, H. & Chen, H. (2020). International Journal of Food Science & Technology, 55(5), 2152-2160.

The well‐studied xylanase inhibitor protein (XIP‐I) regularly inhibits fungi‐derived xylanases, yet some fungal xylanases are not inhibited by XIP‐I. Based on the sequence alignment with the known XIP‐I resistant NpXyn11A from Neocallimastix patriciarum, a new annotated xylanase from ruminal fungus Neocallimastix sp. GMLF1 was found, noted as Xyn1B, which shared 77.8% of sequence identity with NpXyn11A and was proved to be resistant to XIP‐I. To evaluate the performance of a XIP resistant xylanase used in barley malt saccharification, a XIP‐I sensitive xylanase ThXyn1 from Trichoderma harzianum was chosen as a control. The barley malt saccharification experiment was carried out on the condition with or without extra XIP‐I added. The results showed that Xyn1B displayed only slight difference in presence and absence of added XIP‐I, with the difference of xylose released (ΔX) and the difference of mash clarity (ΔA) being 0.17 g L-1 (P > 0.05) and 0.007 (P > 0.05), respectively; while those for ThXyn1 group reached 0.96 g L-1 (P < 0.01) and 0.095 (P < 0.05), indicating that XIP‐I did not adversely affect Xyn1B's function, but did affect ThXyn1's function. Our work for the first time suggested that a xylanase with resistance to xylanase inhibitor proteins might have an advantage in barley malt saccharification over an inhibitor sensitive xylanase.

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Utilization of xylan-type polysaccharides in co-culture fermentations of Bifidobacterium and Bacteroides species species..

Zeybek, N., Rastall, R. A. & Büyükkileci, A. O. (2020). Carbohydrate Polymers, 236, 116076.

Although most members of the genus Bifidobacterium are unable to utilize xylan as a carbon source, the growth of these species can be induced by this polysaccharide in the gut environment. This indicates a requirement for an association between Bifidobacterium species and some other members of gut microbiota. In this study, the role of cross-feeding between Bifidobacterium and Bacteroides species in the bifidogenic effect of xylan was investigated using in-vitro pure and co-culture fermentations. The pure culture studies showed that among the Bifidobacterium species tested, only Bifidobacterium animalis subsp. lactis was able to utilize xylooligosaccharides. The co-culture of this strain with Bacteroides species enabled it to grow in the presence of xylan. These results suggest that the ability of Bacteroides species to hydrolyze xylan could allow the proliferation of specific Bifidobacterium species in the gut through substrate cross-feeding.

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Thermal reactivity of hemicellulose and cellulose in cedar and beech wood cell walls.

Wang, J., Minami, E. & Kawamoto, H. (2020).  Journal of Wood Science, 66(1), 1-10.

Wood cell walls have complex ultra-structures, in which cellulose microfibrils are surrounded by a hemicellulose-lignin matrix. This is the first paper to discuss the effect of cell wall on the pyrolytic reactivity of hemicellulose and cellulose in wood by using Japanese cedar (Cryptomeria japonica, a softwood) and Japanese beech (Fagus crenata, a hardwood), along with isolated xylan and glucomannan. Pyrolysis was conducted by subjecting the samples to temperatures in the range of 220-380°C, at a heating rate of 10°C/min, under a N2 flow with the reactor quenched as soon as the temperature reached the set value. The remaining hemicellulose and cellulose in the heat-treated wood were evaluated by determining the yields of hydrolysable sugar. Isolated xylan containing the uronic acid group, probably acting as a catalyst, was more reactive than isolated glucomannan, whereas the xylan in both woods was remarkably stable and degraded across a similar temperature range to the glucomannan degradation. Thus, the majority of the hemicellulose fractions in cedar and beech unexpectedly exhibited similar reactivity, except for glucomannan in beech that degraded at lower temperatures. Differing thermogravimetric (TG) and derivative TG (DTG) profiles, measured for cedar and beech under similar heating conditions, were explained by the different cellulose reactivity, rather than the hemicellulose reactivity; cellulose decomposed with hemicellulose in cedar, while such decomposition was independent in beech. The observed reactivity is a new finding that is different from the currently understood ideas and may originate from the effects of the cell walls. The research herein provides important information on the kinetics and thermochemical conversion of lignocellulosic biomass.

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Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from Echinicola rosea Sp. Nov. JL3085T.

He, J., Liu, L., Liu, X. & Tang, K. (2020). Marine Drugs, 18(5), 245.

We cloned a xylanase gene (xynT) from marine bacterium Echinicola rosea sp. nov. JL3085T and recombinantly expressed it in Escherichia coli BL21. This gene encoded a polypeptide with 379 amino acid residues and a molecular weight of ~43 kDa. Its amino acid sequence shared 45.3% similarity with an endoxylanase from Cellvibrio mixtus that belongs to glycoside hydrolases family 10 (GH10). The XynT showed maximum activity at 40°C and pH 7.0, and a maximum velocity of 62 μmoL min−1 mg−1. The XynT retained its maximum activity by more than 69%, 51%, and 26% at 10°C, 5°C, and 0°C, respectively. It also exhibited the highest activity of 135% in the presence of 4 M NaCl and retained 76% of its activity after 24 h incubation with 4 M NaCl. This novel xylanase, XynT, is a cold-active and halotolerant enzyme that may have promising applications in drug, food, feed, and bioremediation industries.

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Xylanase inhibition by the derivatives of lignocellulosic material.

Hidayatullah, I. M., Setiadi, T., Kresnowati, M. T. A. P. & Boopathy, R. (2020). Bioresource Technology, 300, 122740.

Hydrolysis of lignocellulosic materials into simple sugar plays an important role in biorefinery. Hemicellulosic sugars from the hydrolysis of lignocellulosic materials could be used in xylitol production. However, xylanase activity during hydrolysis process is affected by activators and inhibitors that may present in the reaction system. The pretreatment process was reported to produce compounds that may affect the enzymatic hydrolysis process, such as furans, aliphatic acid, and aromatics. The purpose of this study was to investigate the inhibition effect of these potential inhibitors on xylanase activity. Three groups of potential inhibitors were evaluated including, furan, aliphatic acid, and hydrolysis-fermentation products. The result showed that ethanol, vanillin, and formic acid gave the highest inhibition effect from each group. Ethanol competed with xylanase competitively. Vanillin showed non-competitive inhibition. Formic acid performed mixed-inhibition by reducing maximum hydrolysis rate and giving varied Michaelis constant values at different concentrations.

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Efficient ferulic acid and xylo-oligosaccharides production by a novel multi-modular bifunctional xylanase/feruloyl esterase using agricultural residues as substrates.

Wang, R., Yang, J., Jang, J. M., Liu, J., Zhang, Y., Liu, L. & Yuan, H. (2020). Bioresource Technology, 297, 122487.

Liberating high value-added compounds ferulic acid (FA) and xylo-oligosaccharides (XOSs) from agricultural residues is a promising strategy for the utilization of lignocellulose. In this study, a bifunctional xylanase/feruloyl esterase from bacterial consortium EMSD5 was heterogeneously expressed in Escherichia coli. Depending on the inter-domain synergism of the recombinant enzyme rXyn10A/Fae1A, high yields of FA (2.78, 1.82, 1.15 and 7.31 mg/g substrate, respectively) were obtained from 20 mg in-soluble wheat arabinoxylan, de-starched wheat bran, ultrafine-grinding corn stover and steam-exploded corncob. Meanwhile, 3.210, 1.235, 1.215 and 0.823 mg xylose/XOSs were also released. For cost-saving enzyme production, we firstly constructed a recombinant E. coli, which could secrete the bifunctional xylanase/feruloyl esterase out of cells. When the recombinant E. coli was cultured in medium containing 200 mg de-starched wheat bran, 474 µg FA and 18.2 mg xylose/XOSs were also detected. Hence, rXyn10A/Fae1A and the recombinant strain showed great applied potential for FA and XOSs production.

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Enhanced stability of a rumen-derived xylanase using SpyTag/SpyCatcher cyclization.

Zhou, Y. B., Cao, J. W., Sun, X. B., Wang, H., Gao, D. Y., Li, Y. N., Wu, K. Y., Wang, J. K., Guo-Ying Qian, G. Y. & & Wang, Q. (2020). World Journal of Microbiology and Biotechnology, 36(2), 1-11.

Microbiota from herbivore rumen is of great interest for mining glycoside hydrolases for lignocellulosic biomass biorefinement. We previously isolated a highly active but poorly thermostable xylanase (LXY) from a rumen fluid fosmid library of Hu sheep, a local high-reproductive species in China. In this study, we used a universal enzyme-engineering strategy called SpyTag/SpyCatcher molecular cyclization to improve LXY stability via isopeptide-bond-mediated ligation. Both linear and cyclized LXY (L- and C-LXY, respectively) shared similar patterns of optimal pH and temperature, pH stability, and kinetic constants (km and Vmax). However, the C-LXY showed enhanced thermostability, ion stability, and resilience to aggregation and freeze–thaw treatment than L-LXY, without compromise of its catalytic efficiency. Circular dichroism and intrinsic and 8-anilino-1-naphthalenesulfonic acid-binding fluorescence analysis indicated that the cyclized enzyme was more capable of maintaining its secondary and tertiary structures than the linear enzyme. Taken together, these results promote the cyclized enzyme for potential applications in the feed, food, paper pulp, and bioenergy industries.

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Heterologous expression, purification and biochemical characterization of a new endo-1, 4-β-xylanase from Rhodothermaceae bacterium RA.

Liew, K. J., Ngooi, C. Y., Shamsir, M. S., Sani, R. K., Chong, C. S. & Goh, K. M. (2019). Protein Expression and Purification, 164, 105464.

Xylanases (EC are essential enzymes due to their applications in various industries such as textile, animal feed, paper and pulp, and biofuel industries. Halo-thermophilic Rhodothermaceae bacterium RA was previously isolated from a hot spring in Malaysia. Genomic analysis revealed that this bacterium is likely to be a new genus of the family Rhodothermaceae. In this study, a xylanase gene (1140 bp) that encoded 379 amino acids from the bacterium was cloned and expressed in Escherichia coli BL21(DE3). Based on InterProScan, this enzyme XynRA1 contained a GH10 domain and a signal peptide sequence. XynRA1 shared low similarity with the currently known xylanases (the closest is 57.2-65.4% to Gemmatimonadetes spp.). The purified XynRA1 achieved maximum activity at pH 8 and 60°C. The protein molecular weight was 43.1 kDa XynRA1 exhibited an activity half-life (t1/2) of 1 h at 60°C and remained stable at 50°C throughout the experiment. However, it was NaCl intolerant, and various types of salt reduced the activity. This enzyme effectively hydrolyzed xylan (beechwood, oat spelt, and Palmaria palmata) and xylodextrin (xylotriose, xylotetraose, xylopentaose, and xylohexaose) to produce predominantly xylobiose. This xylanase is the first functionally characterized enzyme from the bacterium, and this work broadens the knowledge of GH10 xylanases.

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