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Journal articles on the topic 'Endoxylanase'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Beliën, Tim, Steven Van Campenhout, Maarten Van Acker, et al. "Mutational Analysis of Endoxylanases XylA and XylB from the Phytopathogen Fusarium graminearum Reveals Comprehensive Insights into Their Inhibitor Insensitivity." Applied and Environmental Microbiology 73, no. 14 (2007): 4602–8. http://dx.doi.org/10.1128/aem.00442-07.

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ABSTRACT Endo-β-1,4-xylanases (EC 3.2.1.8; endoxylanases), key enzymes in the degradation of xylan, are considered to play an important role in phytopathogenesis, as they occupy a prominent position in the arsenal of hydrolytic enzymes secreted by phytopathogens to breach the cell wall and invade the plant tissue. Plant endoxylanase inhibitors are increasingly being pinpointed as part of a counterattack mechanism. To understand the surprising XIP-type endoxylanase inhibitor insensitivity of endoxylanases XylA and XylB from the phytopathogen Fusarium graminearum, an extensive mutational study o

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2

GEBRUERS, Kurt, Winok DEBYSER, Hans GOESAERT, Paul PROOST, Jozef VAN DAMME, and Jan A. DELCOUR. "Triticum aestivum L. endoxylanase inhibitor (TAXI) consists of two inhibitors, TAXI I and TAXI II, with different specificities." Biochemical Journal 353, no. 2 (2001): 239–44. http://dx.doi.org/10.1042/bj3530239.

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The Triticum aestivum L. endoxylanase inhibitor (TAXI) discovered by Debyser and Delcour [(1997) Eur. Pat. filed April 1997, published as WO 98/49278] and Debyser, Derdelinckx and Delcour [(1997) J. Am. Soc. Brew. Chem. 55, 153Ő156] seems to be a mixture of two different endoxylanase inhibitors, called TAXI I and TAXI II. By using Aspergillus niger as well as Bacillus subtilis endoxylanases for assaying inhibition activity, both inhibitors could be purified to homogeneity from wheat (Triticum aestivum L., var. Soissons). TAXI I and TAXI II have similar molecular structures. They both have a mo

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3

St. John, Franz J., John D. Rice, and James F. Preston. "Characterization of XynC from Bacillus subtilis subsp. subtilis Strain 168 and Analysis of Its Role in Depolymerization of Glucuronoxylan." Journal of Bacteriology 188, no. 24 (2006): 8617–26. http://dx.doi.org/10.1128/jb.01283-06.

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ABSTRACT Secretion of xylanase activities by Bacillus subtilis 168 supports the development of this well-defined genetic system for conversion of methylglucuronoxylan (MeGAXn [where n represents the number of xylose residues]) in the hemicellulose component of lignocellulosics to biobased products. In addition to the characterized glycosyl hydrolase family 11 (GH 11) endoxylanase designated XynA, B. subtilis 168 secretes a second endoxylanase as the translated product of the ynfF gene. This sequence shows remarkable homology to the GH 5 endoxylanase secreted by strains of Erwinia chrysanthemi.

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4

Blanchard, P. J., J. H. Ward, D. Feuerstein, and A. Knox. "NSP Enzymes For Broiler Diets Containing Barley." Proceedings of the British Society of Animal Science 2002 (2002): 207. http://dx.doi.org/10.1017/s1752756200008632.

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Non-starch polysaccharide (NSP) content of barley is predominately in the form of β-glucan, whereas in wheat it is predominately pentosans (containing the sugars arabinose and xylose). It has generally been accepted therefore that a high level of β-glucanase is needed in broiler diets containing barley, whereas wheat based diets require a high level of endoxylanase. Trials have however previously suggested that including an endoxylanase based enzyme in broiler diets will perform at least as well as enzyme containing highlevels of β-glucanase in diets containing up to 30% barley. To confirm thi

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5

Beliën, Tim, Steven Van Campenhout, Johan Robben, and Guido Volckaert. "Microbial Endoxylanases: Effective Weapons to Breach the Plant Cell-Wall Barrier or, Rather, Triggers of Plant Defense Systems?" Molecular Plant-Microbe Interactions® 19, no. 10 (2006): 1072–81. http://dx.doi.org/10.1094/mpmi-19-1072.

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Endo-β-1,4-xylanases (EC 3.2.1.8) are key enzymes in the degradation of xylan, the predominant hemicellulose in the cell walls of plants and the second most abundant polysaccharide on earth. A number of endoxylanases are produced by microbial phytopathogens responsible for severe crop losses. These enzymes are considered to play an important role in phytopathogenesis, as they provide essential means to the attacking organism to break through the plant cell wall. Plants have evolved numerous defense mechanisms to protect themselves against invading pathogens, amongst which are proteinaceous inh

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6

Helianti, Is, Niknik Nurhayati, Maria Ulfah, Budiasih Wahyuntari, and Siswa Setyahadi. "Constitutive High Level Expression of an Endoxylanase Gene from the Newly IsolatedBacillus subtilisAQ1 inEscherichia coli." Journal of Biomedicine and Biotechnology 2010 (2010): 1–12. http://dx.doi.org/10.1155/2010/980567.

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A xylanolytic bacterium was isolated from the sediment of an aquarium. Based on the 16S rDNA sequence as well as morphological and biochemical properties the isolate was identified and denoted asBacillus subtilis(B. subtilis) AQ1 strain. An endoxylanase-encoding gene along with its indigenous promoter was PCR amplified and after cloning expressed inE. coli. InE. colithe recombinant enzyme was found in the extracellular, in the cytoplasmic, and in the periplasmic fraction. The specific activity of the extracellular AQ1 recombinant endoxylanase after 24-hour fermentation was very high, namely,21

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7

Alvarez-Navarrete, Mariana, Katia L. Alonso-Hurtado, Alberto Flores-García, Josué Altamirano-Hernández, Mauro M. Martínez-Pacheco, and Crisanto Velázquez-Becerra. "Comparative Study of the Extracellular Holocellulolytic Activity of Fusarium solani and Aspergillus sp. in Corn Stover." Fermentation 10, no. 2 (2024): 84. http://dx.doi.org/10.3390/fermentation10020084.

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Fungal holocellulases are interesting for their possible applications in the bioconversion of corn crop residues into molecules with technological significance. Holocellulase (xylanases and cellulases) production from Fusarium solani and Aspergillus sp. with corn stover as a carbon source was compared using a Box–Wilson design. The fungal holocellulase production was different in both fungi. For F. solani, the maximum endoxylanase and β-xylosidase activities were 14.15 U/mg and 0.75 U/mg at 84 h of fermentation on 350 g/L corn stover, while Aspergillus sp. was 5.90 U/mg and 0.03 U/mg, respecti

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8

Gil-Durán, Carlos, Romina V. Sepúlveda, Maximiliano Rojas, et al. "The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region." International Journal of Molecular Sciences 23, no. 4 (2022): 2315. http://dx.doi.org/10.3390/ijms23042315.

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Endoxylanases belonging to family 10 of the glycoside hydrolases (GH10) are versatile in the use of different substrates. Thus, an understanding of the molecular mechanisms underlying substrate specificities could be very useful in the engineering of GH10 endoxylanases for biotechnological purposes. Herein, we analyzed XynA, an endoxylanase that contains a (β/α)8-barrel domain and an intrinsically disordered region (IDR) of 29 amino acids at its amino end. Enzyme activity assays revealed that the elimination of the IDR resulted in a mutant enzyme (XynAΔ29) in which two new activities emerged:

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9

St John, Franz J., Diane Dietrich, Casey Crooks, et al. "A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenic Clostridium." Biochemical Journal 475, no. 9 (2018): 1533–51. http://dx.doi.org/10.1042/bcj20180050.

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Glycoside hydrolase family 30 subfamily 8 (GH30-8) β-1,4-endoxylanases are known for their appendage-dependent function requiring recognition of an α-1,2-linked glucuronic acid (GlcA) common to glucuronoxylans for hydrolysis. Structural studies have indicated that the GlcA moiety of glucuronoxylans is coordinated through six hydrogen bonds and a salt bridge. These GlcA-dependent endoxylanases do not have significant activity on xylans that do not bear GlcA substitutions such as unsubstituted linear xylooligosaccharides or cereal bran arabinoxylans. In the present study, we present the structur

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10

Lemos, Judith Liliana Solórzano, and Nei Pereira Junior. "Influence of some sugars on xylanase production by Aspergillus awamori in solid state fermentation." Brazilian Archives of Biology and Technology 45, no. 4 (2002): 431–37. http://dx.doi.org/10.1590/s1516-89132002000600005.

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Aspergillus awamori showed high extracellular endoxylanase (100 U/ml) and beta-xylosidase activities (3.5 U/ml) when grown on milled sugar cane bagasse as the principal carbon source without treatment. Partial characterization of xylanases showed that the apparent values of Km were 3.12 ± 0.05 mg/ml for endoxylanase (in birchwood xylan) and 0.45 ± 0.05 mM for beta-xylosidase (in p -nitrophenyl beta-D-xylanopiranoside). Corresponding values of Vmax were 6.63 ± 0.02 and 0.078 ± 0.02 mumol/min. Gradual repression of endoxylanase activity was observed when increasing concentrations of glucose and

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11

Moon, Young Hwan, Michael Iakiviak, Stefan Bauer, Roderick I. Mackie, and Isaac K. O. Cann. "Biochemical Analyses of Multiple Endoxylanases from the Rumen Bacterium Ruminococcus albus 8 and Their Synergistic Activities with Accessory Hemicellulose-Degrading Enzymes." Applied and Environmental Microbiology 77, no. 15 (2011): 5157–69. http://dx.doi.org/10.1128/aem.00353-11.

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ABSTRACTRuminococcus albus8 is a ruminal bacterium capable of metabolizing hemicellulose and cellulose, the major components of the plant cell wall. The enzymes that allow this bacterium to capture energy from the two polysaccharides, therefore, have potential application in plant cell wall depolymerization, a process critical to biofuel production. For this purpose, a partial genome sequence ofR. albus8 was generated. The genomic data depicted a bacterium endowed with multiple forms of plant cell wall-degrading enzymes. The endoxylanases ofR. albus8 exhibited diverse modular architectures, in

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12

Adeoyo, Olusegun Richard, Brett Ivan Pletschke, and Joanna Felicity Dames. "Partial Purification and Characterization of Endoxylanase from a fungus, Leohumicola incrustata." Bio-Research 19, no. 1 (2021): 1192–201. http://dx.doi.org/10.4314/br.v19i1.2.

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Xylanases are glycoside hydrolases (GH) that degrade β-1,4-xylan, a linear polysaccharide found as hemicellulose in cell wall of plants. Endoxylanase (Endo-1,4-β-xylanase, EC 3.2.1.8) randomly catalyses xylan to produce varying short xylooligosaccharides (XOS). This study aimed to determine the characteristics of a partially purified endoxylanase from Leohumicola incrustata. Enzyme production was carried out using beechwood (BW) xylan, after which the cell-free crude filtrate was concentrated using the ammonium sulphate precipitation method. The hydrolysed products were analysed by thin-layer

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13

Gupta, Naveen, Vanga Shiva Reddy, Sankar Maiti, and Amit Ghosh. "Cloning, Expression, and Sequence Analysis of the Gene Encoding the Alkali-Stable, Thermostable Endoxylanase from Alkalophilic, Mesophilic Bacillus sp. Strain NG-27." Applied and Environmental Microbiology 66, no. 6 (2000): 2631–35. http://dx.doi.org/10.1128/aem.66.6.2631-2635.2000.

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ABSTRACT Alkalophilic Bacillus sp. strain NG-27 produces a 42-kDa endoxylanase active at 70°C and at a pH of 8.4. The gene for this endoxylanase was cloned and sequenced. The gene contained one open reading frame of 1,215 bases. An active site characteristic of the family 10 β-glycanases was recognized between amino acids 303 and 313, with the active glutamate at position 310. Though highly thermostable, the enzyme contains no cysteine residue.

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14

Thirametoakkhara, Chanakan, Yi-Cheng Hong, Nuttapol Lerkkasemsan, Jian-Mao Shih, Chien-Yen Chen, and Wen-Chien Lee. "Application of Endoxylanases of Bacillus halodurans for Producing Xylooligosaccharides from Empty Fruit Bunch." Catalysts 13, no. 1 (2022): 39. http://dx.doi.org/10.3390/catal13010039.

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Endo-1,4-β-xylanase catalyzes the random hydrolysis of β-1,4-D-xylosidic bonds in xylan, resulting in the formation of oligomers of xylose. This study aims to demonstrate the promise of endoxylanases from alkaliphilic Bacillus halodurans for the production of xylooligosaccharides (XOS) from oil palm empty fruit bunch (EFB) at high pH. Two enzyme preparations were employed: recombinant endoxylanase Xyn45 (GH10 xylanase) and nonrecombinant endoxylanases, a mixture of two extracellular endo-1,4-β-xylanases Xyn45 and Xyn23 (GH11 xylanase) produced by B. halodurans. EFB was first treated with an al

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15

Dornez, Emmie, Iris J. Joye, Kurt Gebruers, et al. "Insight into variability of apparent endoxylanase and endoxylanase inhibitor levels in wheat kernels." Journal of the Science of Food and Agriculture 86, no. 11 (2006): 1610–17. http://dx.doi.org/10.1002/jsfa.2505.

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16

Méndez-Líter, Juan A., Laura I. de Eugenio, Manuel Nieto-Domínguez, Alicia Prieto та María Jesús Martínez. "Expression and Characterization of Two α-l-Arabinofuranosidases from Talaromyces amestolkiae: Role of These Enzymes in Biomass Valorization". International Journal of Molecular Sciences 24, № 15 (2023): 11997. http://dx.doi.org/10.3390/ijms241511997.

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α-l-arabinofuranosidases are glycosyl hydrolases that catalyze the break between α-l-arabinofuranosyl substituents or between α-l-arabinofuranosides and xylose from xylan or xylooligosaccharide backbones. While they belong to several glycosyl hydrolase (GH) families, there are only 24 characterized GH62 arabinofuranosidases, making them a small and underrepresented group, with many of their features remaining unknown. Aside from their applications in the food industry, arabinofuranosidases can also aid in the processing of complex lignocellulosic materials, where cellulose, hemicelluloses, and

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17

Chow, Virginia, Guang Nong, and James F. Preston. "Structure, Function, and Regulation of the Aldouronate Utilization Gene Cluster from Paenibacillus sp. Strain JDR-2." Journal of Bacteriology 189, no. 24 (2007): 8863–70. http://dx.doi.org/10.1128/jb.01141-07.

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ABSTRACT Direct bacterial conversion of the hemicellulose fraction of hardwoods and crop residues to biobased products depends upon extracellular depolymerization of methylglucuronoxylan (MeGAXn), followed by assimilation and intracellular conversion of aldouronates and xylooligosaccharides to fermentable xylose. Paenibacillus sp. strain JDR-2, an aggressively xylanolytic bacterium, secretes a multimodular cell-associated GH10 endoxylanase (XynA1) that catalyzes depolymerization of MeGAXn and rapidly assimilates the principal products, β-1,4-xylobiose, β-1,4-xylotriose, and MeGAX3, the aldotet

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18

Kundu, Aditi, and Rina Rani Ray. "Endoxylanase production from the solid state fermentation of Mustard pod husk by Penicillium janthinellum." South Asian Journal of Experimental Biology 2, no. 2 (2012): 44–50. http://dx.doi.org/10.38150/sajeb.2(2).p44-50.

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With an aim to dispose huge amount of mustard pod husk generated after oil seed extraction in an economical way, it was used as the sole carbon source in a fed batch culture of a locally isolated strain of Penicillium janthinellum for the production of endoxylanase (EC 3.2.1.8) on solidâ€state fermentation. The influence of mustard pod husk concentration, cultivation temperature, initial pH, moisture content, organic and inorganic nitrogen sources, surfactants and metal ions were evaluated with respect to endoxylanase production. Attempts were also made to increase the enzyme production by ac

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19

Dornez, Emmie, Kurt Gebruers, Stefan Wiame, Jan A. Delcour, and Christophe M. Courtin. "Insight into the Distribution of Arabinoxylans, Endoxylanases, and Endoxylanase Inhibitors in Industrial Wheat Roller Mill Streams." Journal of Agricultural and Food Chemistry 54, no. 22 (2006): 8521–29. http://dx.doi.org/10.1021/jf061728n.

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20

Fierens, Katleen, Ann Gils, Stefaan Sansen, et al. "His374 of wheat endoxylanase inhibitor TAXI-I stabilizes complex formation with glycoside hydrolase family 11 endoxylanases." FEBS Journal 272, no. 22 (2005): 5872–82. http://dx.doi.org/10.1111/j.1742-4658.2005.04987.x.

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21

Wijaya, Hans, Kengo Sasaki, Prihardi Kahar, et al. "High Enzymatic Recovery and Purification of Xylooligosaccharides from Empty Fruit Bunch via Nanofiltration." Processes 8, no. 5 (2020): 619. http://dx.doi.org/10.3390/pr8050619.

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Xylooligosaccharides (XOS) are attracting an ever-increasing amount of interest for use as food prebiotics. In this study, we used efficient membrane separation technology to convert lignocellulosic materials into a renewable source of XOS. This study revealed a dual function of nanofiltration membranes by first achieving a high yield of xylobiose (a main component of XOS) from alkali-pretreated empty fruit bunch (EFB) hydrolysate, and then by achieving a high degree of separation for xylose as a monosaccharide product. Alkali pretreatment could increase the xylan content retention of raw EFB

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22

Podkaminer, Kara K., Adam M. Guss, Heather L. Trajano, David A. Hogsett, and Lee R. Lynd. "Characterization of Xylan Utilization and Discovery of a New Endoxylanase in Thermoanaerobacterium saccharolyticum through Targeted Gene Deletions." Applied and Environmental Microbiology 78, no. 23 (2012): 8441–47. http://dx.doi.org/10.1128/aem.02130-12.

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ABSTRACTThe economical production of fuels and commodity chemicals from lignocellulose requires the utilization of both the cellulose and hemicellulose fractions. Xylanase enzymes allow greater utilization of hemicellulose while also increasing cellulose hydrolysis. Recent metabolic engineering efforts have resulted in a strain ofThermoanaerobacterium saccharolyticumthat can convert C5and C6sugars, as well as insoluble xylan, into ethanol at high yield. To better understand the process of xylan solubilization in this organism, a series of targeted deletions were constructed in the homoethanolo

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23

Gebruers, Kurt, Kristof Brijs, Christophe M. Courtin, et al. "Properties of TAXI-type endoxylanase inhibitors." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, no. 2 (2004): 213–21. http://dx.doi.org/10.1016/j.bbapap.2003.08.013.

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24

Gebruers, K., K. Brijs, C. M. Courtin, et al. "Affinity Chromatography with Immobilised Endoxylanases Separates TAXI- and XIP-type Endoxylanase Inhibitors from Wheat (Triticum aestivum L.)." Journal of Cereal Science 36, no. 3 (2002): 367–75. http://dx.doi.org/10.1006/jcrs.2002.0472.

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25

Majumdar, Sayari, D. K. Bhattacharyya, and Jayati Bhowal. "Evaluation of nutraceutical application of xylooligosaccharide enzymatically produced from cauliflower stalk for its value addition through a sustainable approach." Food & Function 12, no. 12 (2021): 5501–23. http://dx.doi.org/10.1039/d0fo03120h.

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The present study indicated the cost-effective production of endoxylanase, as well as xylooligosaccharide, a prebiotic functional food ingredient utilizing xylan extracted from cauliflower stalk through steam coupled alkaline treatment.

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26

Rajagopalan, Gobinath, Kavitha Shanmugavelu, and Kun-Lin Yang. "Production of xylooligosaccharides from hardwood xylan by using immobilized endoxylanase of Clostridium strain BOH3." RSC Advances 6, no. 85 (2016): 81818–25. http://dx.doi.org/10.1039/c6ra17085d.

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Endoxylanase ofClostridiumsp. BOH3 was immobilized in calcium alginate/silica gel matrix with a 100% yield. This immobilized xylanase can be reused 7 times to produce prebiotic xylooligosaccharides from hardwood xylan with 62% of activity recovery.

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27

Goesaert, Hans, Kurt Gebruers, Kristof Brijs, Christophe M. Courtin, and Jan A. Delcour. "TAXI Type Endoxylanase Inhibitors in Different Cereals." Journal of Agricultural and Food Chemistry 51, no. 13 (2003): 3770–75. http://dx.doi.org/10.1021/jf0262155.

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Goesaert, H., K. Gebruers, K. Brijs, C. M. Courtin, and J. A. Delcour. "XIP-type endoxylanase inhibitors in different cereals." Journal of Cereal Science 38, no. 3 (2003): 317–24. http://dx.doi.org/10.1016/s0733-5210(03)00046-8.

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29

Goesaert, Hans, Giles Elliott, Paul A. Kroon, et al. "Occurrence of proteinaceous endoxylanase inhibitors in cereals." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, no. 2 (2004): 193–202. http://dx.doi.org/10.1016/j.bbapap.2003.08.015.

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30

Kadi, N., and J. Crouzet. "Transglycosylation reaction of endoxylanase from Trichoderma longibrachiatum." Food Chemistry 106, no. 2 (2008): 466–74. http://dx.doi.org/10.1016/j.foodchem.2007.05.089.

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31

BOURGOIS, T., D. NGUYEN, S. SANSEN, et al. "Targeted molecular engineering of a family 11 endoxylanase to decrease its sensitivity towards Triticum aestivum endoxylanase inhibitor types." Journal of Biotechnology 130, no. 1 (2007): 95–105. http://dx.doi.org/10.1016/j.jbiotec.2007.02.011.

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Pozo-Rodríguez, Ana, Juan A. Méndez-Líter, Laura I. de Eugenio, et al. "A Fungal Versatile GH10 Endoxylanase and Its Glycosynthase Variant: Synthesis of Xylooligosaccharides and Glycosides of Bioactive Phenolic Compounds." International Journal of Molecular Sciences 23, no. 3 (2022): 1383. http://dx.doi.org/10.3390/ijms23031383.

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The study of endoxylanases as catalysts to valorize hemicellulosic residues and to obtain glycosides with improved properties is a topic of great industrial interest. In this work, a GH10 β-1,4-endoxylanase (XynSOS), from the ascomycetous fungus Talaromyces amestolkiae, has been heterologously produced in Pichia pastoris, purified, and characterized. rXynSOS is a highly glycosylated monomeric enzyme of 53 kDa that contains a functional CBM1 domain and shows its optimal activity on azurine cross-linked (AZCL)–beechwood xylan at 70 °C and pH 5. Substrate specificity and kinetic studies confirmed

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Chen, Nancy Jung, and Robert E. Paull. "Endoxylanase expressed during papaya fruit ripening: purification, cloning and characterization." Functional Plant Biology 30, no. 4 (2003): 433. http://dx.doi.org/10.1071/fp02208.

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Papaya (Carica papaya L.) softening during fruit ripening is correlated with the activities of an endoxylanase (EC 3.2.1.8). A 32.5-kDa xylanase (CpaEXY1) from ripening fruit mesocarp was purified 45 871-fold on enzymatic activity and to homogeneity by SDS electrophoresis. The enzyme had endo- and not exo-xylanase activity, a pH optimum of 5–7 and was inhibited by Ca2+, Co2+, and Zn2+. Degenerate primers were constructed from five peptides obtained from the purified enzyme, and a full-length cDNA clone (AY138968) was isolated from a library constructed from ripening mesocarp. CpaEXY1 coded for

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34

Zanoni, J�ssica de Araujo, Isabela Brunozi De Oliveira, Olavo Micali Perrone, et al. "Production and biochemical characterization of xylanases synthesized by the thermophilic fungus Rasamsonia emersonii S10 by solid-state cultivation." Ecl�tica Qu�mica Journal 46, no. 1SI (2021): 53–67. http://dx.doi.org/10.26850/1678-4618eqj.v46.1si.2021.p53-67.

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The xylanolytic enzyme complex hydrolyzes xylan, and these enzymes have various industrial applications. The goal of this work was to characterize the endoxylanases produced by the thermophilic fungus Rasamsonia emersonii in solid-state cultivation. Tests were carried out to evaluate the effects of pH, temperature, glycerol and phenolic compounds on enzyme activity. Thermal denaturation of one isolated enzyme was evaluated. The crude extract from R. emersonii was applied to breakdown pretreated sugarcane bagasse, by quantifying the release of xylose and glucose. The optimum pH value for the cr

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35

Barabote, Ravi D., Juanito V. Parales, Ying-Yi Guo, John M. Labavitch, Rebecca E. Parales, and Alison M. Berry. "Xyn10A, a Thermostable Endoxylanase from Acidothermus cellulolyticus 11B." Applied and Environmental Microbiology 76, no. 21 (2010): 7363–66. http://dx.doi.org/10.1128/aem.01326-10.

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ABSTRACT We cloned and purified the major family 10 xylanase (Xyn10A) from Acidothermus cellulolyticus 11B. Xyn10A was active on oat spelt and birchwood xylans between 60°C and 100°C and between pH 4 and pH 8. The optimal activity was at 90°C and pH 6; specific activity and Km for oat spelt xylan were 350 μmol xylose produced min−1 mg of protein−1 and 0.53 mg ml−1, respectively. Based on xylan cleavage patterns, Xyn10A is an endoxylanase, and its half-life at 90°C was approximately 1.5 h in the presence of xylan.

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Simkhada, Jaya Ram, Hah Young Yoo, Don Hee Park, et al. "An ammonium sulfate sensitive endoxylanase produced by Streptomyces." Bioprocess and Biosystems Engineering 36, no. 6 (2013): 819–25. http://dx.doi.org/10.1007/s00449-013-0908-4.

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37

Dornez, Emmie, Kurt Gebruers, Iris J. Joye, et al. "Effects of fungicide treatment, N-fertilisation and harvest date on arabinoxylan, endoxylanase activity and endoxylanase inhibitor levels in wheat kernels." Journal of Cereal Science 47, no. 2 (2008): 190–200. http://dx.doi.org/10.1016/j.jcs.2007.03.009.

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RODRIGUES, M. A. M., J. W. CONE, C. A. SEQUEIRA, and A. MASCARENHAS-FERREIRA. "Effect of the addition of cell wall degrading enzymes on fermentation kinetics of perennial ryegrass silage." Journal of Agricultural Science 136, no. 4 (2001): 443–49. http://dx.doi.org/10.1017/s0021859601008954.

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Two studies were undertaken to evaluate the effects of cellulase and endoxylanase enzymes on the chemical composition and the fermentation characteristics of grass silage, using the gas production technique. Perennial ryegrass was ensiled in 1 litre glass containers for 90 days with cellulase (0·2 g/kg grass on fresh weight basis) and endoxylanase in the concentrations of 0·05 g/kg grass (Endox 0·05) and 0·2 g/kg grass (Endox 0·2). Subsequently, dried samples, ground through a 1 mm screen, were used in chemical analysis and gas production measurements. In Expt 1, the enzyme treatment significa

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Najjarzadeh, Nasim, Leonidas Matsakas, Ulrika Rova, and Paul Christakopoulos. "Effect of Oligosaccharide Degree of Polymerization on the Induction of Xylan-Degrading Enzymes by Fusarium oxysporum f. sp. Lycopersici." Molecules 25, no. 24 (2020): 5849. http://dx.doi.org/10.3390/molecules25245849.

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Xylan is one of the most abundant carbohydrates on Earth. Complete degradation of xylan is achieved by the collaborative action of endo-β-1,4-xylanases and β-d-xylosidases and a number of accessories enzymes. In filamentous fungi, the xylanolytic system is controlled through induction and repression. However, the exact mechanism remains unclear. Substrates containing xylan promote the induction of xylanases, which release xylooligosaccharides. These, in turn, induce expression of xylanase-encoding genes. Here, we aimed to determine which xylan degradation products acted as inducers, and whethe

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Kim, Yeon-Hee, Sun-Yeon Heo, Mi-Jin Kim, Jae-Hyung Lee, Young-Man Kim, and Soo-Wan Nam. "Optimal Production of Xylooligosaccharide by Using Recombinant Endoxylanase from Bacillus subtilis." Journal of Life Science 18, no. 1 (2008): 52–57. http://dx.doi.org/10.5352/jls.2008.18.1.052.

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Monti, Rubens, Héctor Francisco Terenzi, and João Atílio Jorge. "Purification and properties of an extracellular xylanase from the thermophilic fungus Humicola grisea var. thermoidea." Canadian Journal of Microbiology 37, no. 9 (1991): 675–81. http://dx.doi.org/10.1139/m91-115.

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Humicola grisea var. thermoidea mycelium grown on xylan as the sole source of carbon produced at least two extracellular xylanases. The main xylanolytic component (form 2; 90% of recovered activity) was purified to homogeneity. The apparent molecular mass of the purified enzyme was estimated to be 23 000 and 25 550 Da by Bio-Gel P-60 filtration and urea–SDS–PAGE, respectively. The purified enzyme was a glycoprotein with 45% carbohydrate content and pH and temperature optima of 5.5 and 70 °C, respectively. The apparent Km and Vmax values determined with larch-wood xylan were 3.3 mg/mL and 229 μ

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Wu, Sheng-Cheng, Kyung-Sik Ham, Alan G. Darvill та Peter Albersheim. "Deletion of Two Endo-β-1,4-Xylanase Genes Reveals Additional Isozymes Secreted by the Rice Blast Fungus". Molecular Plant-Microbe Interactions® 10, № 6 (1997): 700–708. http://dx.doi.org/10.1094/mpmi.1997.10.6.700.

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Fungal pathogens secrete hydrolases during infection of plant tissues capable of fragmenting the primary cell wall polysaccharides of the host. Magnaporthe grisea, the fungal pathogen that causes blast disease of graminaceous monocots, secretes two distinct endo-β-1,4-D-xylanases when grown on xylan-rich rice cell walls as the carbon source. We have previously reported the cloning of the genes encoding these two xylanases, XYL1 and XYL2 (formerly XYN22 and XYN33, respectively; see S.-C. Wu, S. Kauffmann, A. G. Darvill, and P. Albersheim, Mol. Plant-Microbe Interact. 8:506–514, 1995). We now pr

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Beliën, Tim, Steven Van Campenhout, Maarten Van Acker, and Guido Volckaert. "Cloning and characterization of two endoxylanases from the cereal phytopathogen Fusarium graminearum and their inhibition profile against endoxylanase inhibitors from wheat." Biochemical and Biophysical Research Communications 327, no. 2 (2005): 407–14. http://dx.doi.org/10.1016/j.bbrc.2004.12.036.

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Carmona, Eleonora Cano, Marcia Regina Brochetto-braga, Aline Aparecida Pizzirani-kleiner, and JoÃ£o Atilio Jorge. "Purification and biochemical characterization of an endoxylanase fromAspergillus versicolor." FEMS Microbiology Letters 166, no. 2 (1998): 311–15. http://dx.doi.org/10.1111/j.1574-6968.1998.tb13906.x.

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Fuchs, Yoram, Abha Saxena, H. Ray Gamble, and James D. Anderson. "Ethylene Biosynthesis-Inducing Protein from Cellulysin Is an Endoxylanase." Plant Physiology 89, no. 1 (1989): 138–43. http://dx.doi.org/10.1104/pp.89.1.138.

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FernÃ¡ndez-Espinar, MarÃa Teresa, Francisco PiÃ±aga, Pascual Sanz, Daniel RamÃ³n, and Salvador VallÃ©s. "Purification and characterization of a neutral endoxylanase fromAspergillus nidulans." FEMS Microbiology Letters 113, no. 2 (1993): 223–28. http://dx.doi.org/10.1111/j.1574-6968.1993.tb06518.x.

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Kalogeris, E., P. Christakopoulos, M. Vršanská, D. Kekos, P. Biely, and B. J. Macris. "Catalytic properties of the endoxylanase I from Thermoascus aurantiacus." Journal of Molecular Catalysis B: Enzymatic 11, no. 4-6 (2001): 491–501. http://dx.doi.org/10.1016/s1381-1177(00)00178-8.

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López Lorenzo, M., V. A. Nierstrasz, and M. M. C. G. Warmoeskerken. "Endoxylanase action towards the improvement of recycled fibre properties." Cellulose 16, no. 1 (2008): 103–15. http://dx.doi.org/10.1007/s10570-008-9246-0.

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Varzakas, Theodoros, Dimitrios Arapoglou, and Cleanthes Israilides. "Kinetics of endoglucanase and endoxylanase uptake by soybean seeds." Journal of Bioscience and Bioengineering 101, no. 2 (2006): 111–19. http://dx.doi.org/10.1263/jbb.101.111.

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Manenoi, Ashariya, and Robert E. Paull. "Papaya fruit softening, endoxylanase gene expression, protein and activity." Physiologia Plantarum 131, no. 3 (2007): 470–80. http://dx.doi.org/10.1111/j.1399-3054.2007.00967.x.

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