Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application

REFERENCES

• Puls, J., Chemistry and biochemistry of hemicelluloses: relationship between hemicellulose structure and enzymes required for hydrolysis, Macromol. Symp. 120, 183, 1997.
   Google Scholar
• Bissoon, S., Christov, L., and Singh, S., Bleach boosting effects of purified xylanase from Thermomyces lamiginosus SSBP on bagasse pulp. Process Biochem. 37, 567, 2002.
   Web of Science ®Google Scholar
• Shoham, Y., Schwartz, Z., Khasin, A., Gat, O., Zosim, Z., and Rosenberg, E. Delignification of wood pulp by a thermostable xylanase from Bacillus stearothermophilus strain T-6. Biodegradation. 3, 207–218, 1992.
   Google Scholar
• Viikari, L., Ranua, M., Kantelinen, A., Sundiquist, J., and Linko, M., Bleaching with enzymes. Biotechnology in the pulp and paper industry. Proc.3rd Int. Con., Stockholm, 1986, 67.
   Google Scholar
• Wong, K.K.Y., Tan, L. U. L., and Saddler, J. N., Multiplicity of β-l,4-xylanase in microorganisms: Functions and applications. Microbiol. Rev. 52, 305, 1988.
   PubMedGoogle Scholar
• Biely, P., Microbial xylanolytic systems. Trends Biotechnol. 3, 286, 1985.
   Web of Science ®Google Scholar
• Kulkami N., Shendye A., and Rao, M., Molecular and biotechnological aspects of xylanases, FEMS Microbiol. Rev. 23, 411, 1999.
   PubMed Web of Science ®Google Scholar
• Jeffries T W. Biochemistry and genetics of microbial xylanases. Curr. Opin. Biotechnol. 7, 337, 1996b.
   PubMed Web of Science ®Google Scholar
• Dervilly, G., Thibault, J.-F., and Saulnier, L., Experimental evidence for a semi-flexible conformation for arabinoxylans. Carbohydrate Res. 330, 365, 2001.
   PubMed Web of Science ®Google Scholar
• Dervilly, G., Leclercq, C, Zimmerman, D., Roue, C., Thibault, J.-F. and Saulnier, L., Isolation and characterization of high molecular mass water-soluble arabinoxylans from barley malt. Carbohydrate Polymers, 47, 143, 2002.
   Web of Science ®Google Scholar
• Teleman, A., Tenkanen, M., Jacobs, A., and Dahlman, O., Characterization of O-acetyl-(4-O-methylglucurono) xylan isolated from birch and beech. Carbohydrate Res. 337, 373, 2002.
   PubMed Web of Science ®Google Scholar
• Jeffries T. W., Biochemistry and genetics of microbial xylanases. Online publication URL: http://calvinbiotech.wisc.edu/iefFries/xvlanase#review/Indexof/ieffries/xylanasereview. 1996a.
   Google Scholar
• Poutanen, K., Ratto, M., Puls, J., and Viikari, L., Evaluation of different microbial xylanolytic systems, J. Biotechnol. 6, 49, 1987.
   Web of Science ®Google Scholar
• Kang, S. W., Kim, S.–W., and Lee, J. –S., Production of cellulase and xylanase in a bubble column using immobilized Aspergillus niger KKS, Appl. Biochem. Biotech. 53, 101, 1995.
   PubMed Web of Science ®Google Scholar
• Bi, R, Sun, X., and Ren, S., The study on xylanase fermentation by Aspergillus niger sp., Ind. Microbiol. 30, 53, 2000.
   Google Scholar
• Singh S., Pillay, B., Dilsook, V., and Prior, B.A., Production and properties of hemicellulases by a Thermomyces lamiginosus strain, J. Appl. Microbiol. 88, 975, 2000.
   PubMed Web of Science ®Google Scholar
• Copa-Patino, J.L., Kim, Y.G., and Broda, P., Production and initial characterisation of the xylan-degrading system of Phanerochaete chrysosporium, Appl. Microbiol. Biotechnol. 40, 69 1993.
   Web of Science ®Google Scholar
• Tenuissen, M. J., de Kort, G. V. M., Op den Camp, H. J.M., and Huis in t Veld, J. H. J., Production of cellulolytic and xylanolytic enzymes during growth of the anaerobic fungus Piromyces sp. on different substrates, J. Gen. Microbiol. 138, 1657, 1992.
   PubMedGoogle Scholar
• Steiner, W., Lafferty, R M., Gomes, I., and Esterbauer, H., Studies on a wild strain of Schizophyllum commune: cellulase and xylanase production and formation of the extracellular polysaccharide Schizophyllan, Biotechnol. Bioeng. 30, 169, 1987.
   PubMed Web of Science ®Google Scholar
• Tuohy, M., Coughlan, T. L., and Coughlan, M. P., Solid-state versus liquid cultivation of Talaromyces emersonii on straw and pulps: enzyme productivity, in Advances in Biological Treatment of Lignocellulosic Materials, Coughlan, M. P. and Amaral Collaco, M. T., Eds., Elsevier Applied Science, London 1990, 153.
   Google Scholar
• Gomes, J., Purkarthofer, H., Hayn, M., Kapplmuller, J., Sinner, M., and Steiner, W., Production of a high level of cellulase-free xylanase by the thermophilic fungus Thermomyces lanuginosus in laboratory and pilot scales using lignocellulosic materials, Appl. Microbiol. Biotechnol. 39, 700, 1993.
   Web of Science ®Google Scholar
• Gamerith, G., Groicher, R, Zeilinger, S., Herzog, P., and Kubicek, C. P., Cellulase poor xylanase produced by Trichoderma reesei RUT C-30 on hemicellulose substrates, Appl. Microbiol. Biotechnol. 38, 315, 1992.
   Web of Science ®Google Scholar
• Bailey, M.J., Buchert, J., and Viikari, L., Effect of pH on production of xylanase by Trichoderma reesei on xylan and cellulose-based media. . ippl. Microbiol. Biotechnol. 40, 224, 1993.
   Web of Science ®Google Scholar
• Gomes, I., Gomes, J., Steiner, W., and Esterbauer, H., Production of cellulase and xylanase by a wild strain of Trichoderma viride, Appl. Microbiol. Biotechnol. 36, 701, 1992.
   Web of Science ®Google Scholar
• Subramaniyan, S., Studies on the Production of Bacterial Xylanases. Ph.D. Thesis, Cochin University of Science and Technology, Kerala, India, 2000.
   Google Scholar
• Ratto, M., Poutanen, K., and Viikari, L., Production of xylanolytic enzymes by an alkalitolerant Bacillus circulons strain, Appl. Microbiol. Biotechnol. 37, 470, 1992.
   Web of Science ®Google Scholar
• Khasin, A., Alchanati, I., and Shoham, Y., Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6, Appl. Environ. Microbiol. 59, 1725, 1993.
   PubMed Web of Science ®Google Scholar
• Lundgren, K.R, Bergkvist, L., Hogman, S., Joves, H., Eriksson, G., Bartfai, T., Laan, J. V. D., Rosenberg, E. and Shoham, Y., TCF Mill Trial on softwood pulp with Korsnas thermostable and alkaline stable xylanase T6, FEMS Microbiol. Rev. 13, 365, 1994.
   Web of Science ®Google Scholar
• Balakrishnan, H., Dutta-Choudhury, M., Srinivasan, M.C., and Rele, M.V., Cellulasefree xylanase production from an alkalophilic Bacillus sp.. World. J. Microbiol. Biotechnol. 8, 627, 1992.
   PubMed Web of Science ®Google Scholar
• Paul, J. and Varma, AK., Characterisation of cellulose and hemicellulose degrading Bacillus sp. from termite infested soil, Curr. Sci. 64, 262, 1993.
   Web of Science ®Google Scholar
• Balakrishnan, H., Srinivasan, M. C., Rele, M. V., Chaundhari, K., and Chandwadkar, A. J., Effect of synthetic zeolites on xylanase production from an alkalophilic Bacillus sp., Curr. Sci. 79, 95, 2000.
   Web of Science ®Google Scholar
• Dhillon, A., Gupta, J. K., Jauhari, B. M., and Khanna, S., A cellulase-poor, thermostable, alkalitolerant xylanase produced by Bacillus circulons AB 16 grown on rice straw and its application in biobleaching of eucalyptus pulp. Bioresource Technol. 73, 273, 2000.
   Web of Science ®Google Scholar
• Emanuilova, E. I., Dimitrov, P. L., Mandeva, R D., Kambourova, M. S., and Engibarov, S. A., Extracellular xylanase production by 2 thermophilic alkali-tolerant Bacillus strains in batch and continuous cultures, Z. Naturforsch. C., 55, 66, 2000.
   PubMedGoogle Scholar
• Rani, D. S. and Nand, K., Production of thermostable cellulase-free xylanase by Clostridium absonum CFR - 702, Process Biochem. 36, 355, 2000.
   Web of Science ®Google Scholar
• Dahlberg, L., Holst, O., and Kristjansson, J. K., Thermostable xylanolytic enzymes from Rhodothermus marinus grown on xylan, Appl. Microbiol. Biotechnol. 40, 63, 1993.
   Web of Science ®Google Scholar
• Hreggvidsson, G.O., Kaiste, E., Holst, O., Eggertsson, G., Palsdottir, A, and Kristjansson, J. K., An extremely thermostable cellulase from the thermophilic eubacterium Rhodothermus marinus, Appl. Environ. Microbiol. 62, 3047, 1996.
   Web of Science ®Google Scholar
• Maheswari, M. U. and Chandra, T. S., Production and potential applications of a xylanase from a new strain of Streptomyces cuspidosporus, World J. Microbiol. Biotechnol. 16, 257, 2000.
   Web of Science ®Google Scholar
• Grabski, A.C. and Jeffries T.W., Production, purification and characterization of β-(1-4)-Endoxylanase of Streptomvces roseiscleroticus, Appl. Environ. Microbiol. 57, 987, 1991.
   PubMed Web of Science ®Google Scholar
• Techapun, C., Sinsuwongwat, S., Poosaran, N., Watanabe, M., and Sasaki, K., Production of a cellulase-free xylanase from agricultural waste materials by thermotolerant Streptomyces sp. Biotechnol. Letts. 23, 1685, 2001.
   Web of Science ®Google Scholar
• Beg, Q. K., Bhushan, B., Kapoor, M., and Hoondal, G. S., Production and characterization of thermostable xylanase and pectinase from Streptomyces sp. QG-11-3, J. Ind. Microbiol. Biotechnol. 24, 396, 2000.
   Web of Science ®Google Scholar
• Kohli, U., Nigam, P., Singh, D., and Chaudhary, K., Thermostable, alkalophilic and cellulase-free xylanase production by Thermoactinomyces thalophilus subgroup C, Enzyme Microbial Technol., 28, 606, 2001.
   PubMed Web of Science ®Google Scholar
• Cleemput, G., Hessing, M., van Oort, M., Deconynck, M., and Delcour, J. A., Purification and characterization of β-D-xylosidase and an endo-xylanase from wheat flour, PlantPhysiol. 113, 377, 1997.
   Web of Science ®Google Scholar
• Yamura, I., Koga, T., Matsumoto, T., and Kato, T., Purification and some properties of Endo-1, 4-β-d-xylanse from a fresh water mollusc, Pomacea insularus (de Ordigny), Biosc. Biotech. Biochem. 61, 615, 1997.
   PubMed Web of Science ®Google Scholar
• Lebeda, A., Luhová, L., Sedlá, M., and Jan, D., The role of enzymes in plant-fungal pathogens interactions, Zeitschrift fur Pflanzenkrankheiten und Pflanzenschutz, 108, 89, 2001.
   Google Scholar
• La-Grange, D. C., Claeyssens, M., Pretorius, I. S., and van-Zyl, W. H., Coexpression of the Bacillus pumilus beta-xylosidase (xynB) gene with the Trichodenna reesei beta-xylanase-2 (xyn2) gene in the yeast Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 54, 195, 2000.
   PubMed Web of Science ®Google Scholar
• Poutanen, K. Characterisation of xylanolytic enzymes for potential applications. Ph.D. Thesis, Technical Research Centre of Finland, Publications, 47, Espoo, 1988.
   Google Scholar
• Gomes, J., Gomes, I., Terler, K., Gubala, N., Ditzelmuller, G., and Steiner, W., Optimisation of culture medium and conditions for α-l-arabinofuranosidase production by the extreme thermophilic eubacterium Rhodothermus marinus, Enzyme Microb. Technol. 27, 414, 2000.
   PubMed Web of Science ®Google Scholar
• Morales, P. Sendra, J. M., and Perez-Gonzalez, J. A., Purification and characterisation of an arabinofuranosidase from Bacillus polymyxa expressed in Bacillus subtilis, Appl. Microbiol. Biotechnol. 44, 112, 1995.
   PubMed Web of Science ®Google Scholar
• Hazlewood, G. P. and Gilbert, H. J., Molecular biology of hemicellulases, in Hemicelluloses and Hemicellulases, Coughlan, M. P. and Hazlewood, G. P., Eds., Portland Press, London 1993. 103.
   Google Scholar
• Esteban, R;, Villanueva, I.R, and Villa, T.G., β-d-Xylanases of Bacillus circulons WL-12, Can. J. Microbiol. 28, 733, 1982.
   Google Scholar
• Fuchs, Y., Saxena, A., Gamble, H.R, and Anderson, J.D., Ethylene biosynthesis inducing protein from celluly sin in an endoxylanase. Plant Physiol. 89, 138, 1989.
   PubMed Web of Science ®Google Scholar
• Lotan, T. and Fluhr, R, Xylanase, a novel elicitor of pathogenesis related proteins in tobacco, uses a non-ethylene pathway for induction, Plant Physiol. 93, 811, 1990.
   PubMed Web of Science ®Google Scholar
• Dean, J. F. D. and Anderson, J. D., Ethylene biosynthesis inducing xylanase II: Purification and physical characterization of the enzyme produced by Trichoderma viridae, Plant Physiol. 95, 316, 1991.
   PubMed Web of Science ®Google Scholar
• Dean, J.F.D., Gross, K.C., and Anderson, J.D., Ethylene biosynthesis inducing xylanase III: Product characterization. Plant Physiol. 96, 571, 1991.
   PubMed Web of Science ®Google Scholar
• Subramaniyan, S., Sandhia, G. S., and Prema, P., Control of xylanase production with out protease activity in Bacillus sp. by the selected nitrogen source, Biotechnol. Lett. 23, 369, 2001.
   Web of Science ®Google Scholar
• Luthi, E., Jasmat, N.B., and Bergquist P.L., Xylanase from the extremely thermophilic bacterium Caldocellum saccharolyticum: overexpression of the gene in Escherichia coli and characterization of the gene product, Appl. Environ. Microbiol. 36, 2677, 1990.
   Google Scholar
• Mathrani, LM, and Ahring, B.K., Thermophilic and alkalophilic xylanases from several Diclyoglomus isolates, Appl. Microbiol. Biotechnol. 38, 23, 1992.
   Web of Science ®Google Scholar
• Subramaniyan, S. and Prema, P., Cellulase-free xylanases from Bacillus and other microorganisms, FEMS Microbiol. Lett. 183, 1, 2000.
   PubMed Web of Science ®Google Scholar
• Salles, B. C., Cunha, R. B., Fontes, W., Sousa, M. V., and Filho, E. X. F. Purification and characterization of a new xylanase from Acrophialophora nainiana, J. Biotechnol., 81, 199, 2000.
   PubMed Web of Science ®Google Scholar
• Kormelink, F. J. M., Leeuwen, M. G. F. S. -L., Wood, T.M., and Voragen, A.G.J., Purification and characterisation of three endo (1,4)-β-xylanases and one β-xylosidase from Aspergillus awamori, J. Biotechnol. 27, 249, 1993.
   Web of Science ®Google Scholar
• Femadez-Espinar M.T., Pinaga, F., deGraaff, L., Visser, J., Ramon, D., and Valles, S., Purification, characterisation and regulation of the synthesis of an Aspergillus nidulans acidic xylanase, Appl. Microbiol. Biotechnol. 42, 555, 1994.
   Web of Science ®Google Scholar
• Kimura, I., Sasahara, H., and Tajima, S., Purification and characterization of two xylanases and an arabinofuranosidase from Aspergillus sojae, J. Ferm. Bioeng. 80, 334, 1995.
   Google Scholar
• Li, X. L., Zhang, Z., Dean, I. F. D., Eriksson, KL., and Ljungdahl, L. G., Purification and characterisation of a new xylanase (APX-II) from the fungus Aureobasidium pullulons Y-2311-1, Appl. Environ. Microbiol., 59, 3212, 1993.
   PubMed Web of Science ®Google Scholar
• Vadi, R M., Strohfus, B. R. H., and West, T.P., Characterisation of a xylanase from Aureobasidium pullulons, Microbios 85, 179, 1996.
   Google Scholar
• Kang, M.K, Maeng, P.J., and Rhee, Y.H., Purification and characterization of two xylanases from alkalophilic Cephalosporium sp. Strain RYM-202, Appl. Environ. Microbiol. 62, 3480, 1996.
   PubMed Web of Science ®Google Scholar
• Braun, E.J. and Rodrigues C.A., Purification and properties of an endoxylanase from a com stalk rot strain of Erwinia chrysanthemi, Phytopathology 83, 332, 1993.
   Web of Science ®Google Scholar
• Dusterhoft, E. M., Linssen, V. A. J. M., Voragen, A.G.J., and Beldman, G., Purification characterization and properties of two xylanases from Humicola insolens. Enzyme Microb Technol. 20, 437, 1997.
   Web of Science ®Google Scholar
• Belancic, A., Scarpa, J., Peirano, A., Diaz, R, Steiner, J., and Eyzaguirre, J., Pencillium purpurogenum produces several xylanases: purification and properties of two of the enzymes, J. Biotechnol. 41, 71, 1995.
   PubMed Web of Science ®Google Scholar
• Chen, C., Chen, J.-L., and Lin, T.-Y., Purification and characterization of a xylanase from Trichoderma longibrachiatam for xylooligosaccliaridc production Enzyme Microb. Technol. 21, 91, 1997.
   Google Scholar
• Ujiie, M., Roy, C., and Yaguchi, M., Low molecular weight xylanase from Trichoderma viride, Appl. Environ. Microbiol. 57, 1860, 1991.
   PubMed Web of Science ®Google Scholar
• Tan, L.U.L., Wong, KKY., Yu, E.KC., and Saddler, J.N., Purification and characterisation of two D-Xylanases from Trichoderma harzianum, Enzyme and Microb. Technol. 7, 425, 1985.
   Web of Science ®Google Scholar
• Kubata, K.B., Horitsu, H., Kawai, K, Takamizawa, K, and Suzuki, T., Xylanasel of Aeromonas caviae ME-I isolated from the intestine of a herbivorous insect (Samia cvnthia pryeri), Biosci. Biotech. Biochem. 56, 1463, 1992.
   PubMed Web of Science ®Google Scholar
• Breccia, J. D., Sineriz, F., Baigori, M. D., Castro, G. R, and Hatti-Kaul, R, Purification and characterization of a thermostable xylanase from Bacillus amyloliquefaciens, Enzyme Microb. Technol. 22, 42, 1998.
   Web of Science ®Google Scholar
• Akiba, T. and Horikoshi, K, Xylanases of alkalophilic thermophilic Bacillus, Methods in Enzymol. 160, 655, 1988.
   Web of Science ®Google Scholar
• Nakamura, S., Wakabayashi, K, Nakai, R, Aono, R, and Horikoshi, K, Purification and some properties of an alkaline xylanase from alkalophilic Bacillus sp. strain 41 M-1, Appl. Environ. Microbiol. 59, 2311, 1993.
   PubMed Web of Science ®Google Scholar
• Nakamura, S., Nakai, R, Wakabayashi, K, Ishiguro, Y., Aono, R, and Horikoshi, K, Thermophilic alkaline xylanase from newly isolated alkaliphilic and thermophilic Bacillus sp. Strain TAR-1, Biosci. Biotech. Biochem. 58, 78, 1994.
   PubMed Web of Science ®Google Scholar
• Ratanakhanokchai, K., Kyu, K. L., and Tanticharoen, M., Purification and properties of a xylan-binding endoxylanase from alkalophilic Bacillus sp. Strain K-1, Appl. Environ. Microbiol. 65, 694, 1999.
   PubMed Web of Science ®Google Scholar
• Keskar, S.S., Srinivasan, M.C., and Deshpande, V.V., Chemical modification of a xylanase from thennotolerant Streptomvces: evidence for essential tryptophan and cystein residues at the active site, Biochem. J. 261, 49, 1989.
   PubMed Web of Science ®Google Scholar
• Nakanishi, K, Marui, M., and Yasui, T., Comparison of xylan and methyl β-xyloside induced xylanases from Streptomvces sp. J. Ferm. Bioeng. 74, 392, 1992.
   Google Scholar
• Bergquist, P., Gibbs, M. D., Morris, D. D., Thompson, D. R, Uhl, A. M., and Daniel, R M., Hyperthermophilic xylanases. Method. Enzymol., Vol. 330, 301, 2001.
   PubMed Web of Science ®Google Scholar
• Sunna, A., Puls, J., and Antranikian, G., Purification and characterization of two thermo-stable endo-1,4-β-d-xylanases from Thermotoga thermarum, Biotechnol. Appl. Biochem, 24, 177, 1996.
   Web of Science ®Google Scholar
• Subramaniyan, S., Prema, P., and Ramakrishna, S. V., Isolation and screening for alkaline thermostable xylanases,. J Basic Microbiol. 37, 431, 1997.
   Web of Science ®Google Scholar
• Subramaniyan, S. and Prema, P., Optimisation of cultural parameters for the synthesis of endoxylanases from Bacillus SSP-34, J. Sci. Ind. Res. 611, 1998.
   Google Scholar
• Gilbert, H.J. and Hazelwood, G.P., Bacterial ccllulascs and xylanases. J. Gen. Microbiol. 139, 187, 1993.
   Google Scholar
• Sapag, A., Wouters, J., Lambert, C., Ioannes, P., Eyzaguirre, J., and Depiereux, E., The endoxylanases from family 11 : computer analysis of protein sequences reveals important structural and phylogenetic relationships, J. Biotechnol. (in press), 2002.
   PubMed Web of Science ®Google Scholar
• Kuno, A., Kaneko, S., Ohtsuki, H., Ito, S., Fujimoto Z., Mizuno, H., Hasegawa T., Taira K., Kusakabe, I., and Hayashi, K., Novel sugarbinding specificity of the type XIII xylan-binding domain of a family F/10 xylanase from Streptomyces olivaceoviridis E-86, FEBS Lett. 482, 231, 2000.
   PubMed Web of Science ®Google Scholar
• Biely, P., Markovik, O., and Mislovicova, D., Sensitive detection of endo-l,4,-β-glucanases and endo-l,4-β-xylanases in gels. Anal. Biochem. 144, 147, 1985.
   PubMed Web of Science ®Google Scholar
• Biely, P., Vrsanska, M., Tenkanen, M., and Kluepfel, D. Endo-β-xylanases families: differences in catalytic properties, J. Biotechnol. 57, 151, 1997.
   PubMed Web of Science ®Google Scholar
• Elegir., G. Szakacs, G., and Jeffries, T.W., Purification, characterization and substrate specificitys of multiple xylanases from Streptomyces sp. strain B-12-2, Appl. Environ. Microbiol. 60, 2609, 1994.
   PubMed Web of Science ®Google Scholar
• Dobozi, M. S., Szakacs, G., and Bruschi, C. V., Xylanase activity of Phanerchaete chrysosporiunu Appl. Environ. Microbiol. 58, 3466, 1992.
   Google Scholar
• Tsujibo, H., Ohtsuki, T., Iio, T., Yamazaki, I., Miyamoto, K., Sugiyama, M., and Inamori, Y., Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterases from Streptomyces OPC-520, Appl. Environ. Microbiol. 63, 661, 1997.
   PubMed Web of Science ®Google Scholar
• Leathers, T. D., Amino acid composition and partial sequence of xylanase from Aureobasidium, Biotechnol. Lett. 10, 775, 1988.
   Web of Science ®Google Scholar
• Li, X.-L. and Ljungdahl, L.G., Cloning, sequencing and regulation of a xylanase gene from the fungus Aureobasidium pullulons Y-2311-1, Appl. Environ. Microbiol. 60, 3160, 1994.
   PubMed Web of Science ®Google Scholar
• Leathers, T. D., Purification and properties of xylanase from Aureobasidiunu J. Ind. Microbiol. 4, 341, 1989.
   Google Scholar
• Wong, K. K. Y. and Saddler. J. N., Trichoderma xylanases, their properties and application, Prog. Biotechnol. 7, 171, 1992.
   Google Scholar
• Bataillon, M., Nunes-Cardinali, A. P., Castillon, N., and Duchiron, F., Purification and characterization of a moderately thermostable xylanase from Bacillus sp. strain SPS-0, Enzyme Microb. Technol. 26, 187, 2000.
   PubMed Web of Science ®Google Scholar
• Takahashi, H., Nakai, R., and Nakamura, S., Purification and partial characterization of a basic xylanase produced by thennoalkaliphilic Bacillus sp. strain TAR-1, Biosci. Biotechnol. Biochem. 64, 887, 2000.
   PubMed Web of Science ®Google Scholar
• Kimura, T., Ito, J., Kawano, A., Makino, T., Kondo, H., Karita, S., Sakka, K., and Ohmiya, K., Purification, charcaterization and molecular cloning of acidophilic endo-1,4-β-D-xylanase from Pénicillium sp. 40, Biosci. Biotechnol. Biochem. 64, 1230, 2000.
   PubMed Web of Science ®Google Scholar
• Torronen, A., Harkki, A., and Rouvinen, J., Three dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: two conformational states in active state, EMBO J. B. 3, 2493, 1994.
   Google Scholar
• Wakarchuk, W. W. Campbell, RL. Sung, W.L., Davoodi, J., and Yaguchi, M., Mutational and crystallographic analyses of the active site residues of the Bacillus circulons xylanase, Prot. Sci. 3, 467, 1994.
   PubMed Web of Science ®Google Scholar
• Leggio, L. L. Jenkins, J., Harris, G.W., and Pickersgill, R W., X-ray crystallographic study of xylopentose binding to Pseudomonas fluorescens xylanase A, Proteins: Struct. Function and Genetics, 41, 362, 2000.
   Google Scholar
• Davoodi, J., Wakarchuk, W.W., Campbell, RL., Carey, P.R, and Surewiz, W.K., Abnormally high pKa of an active site glutamic acid residue in Bacillus circulons xylanase — the role of electrostatic interactions, Eur. J. Biochem. 232, 839, 1995.
   PubMedGoogle Scholar
• White, A., Whithers, S. G., Gilkes, N. R, and Rose, D. R, Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi, Biochemistry 33, 12546, 1994.
   PubMed Web of Science ®Google Scholar
• Meagher, M.M, Tao, B.Y., Chow, J. M., and Reilly, P.J., Kinetics and subsite mapping of β-d-xylobiose and d-xylose producing Aspergillus endoxylanase, Carbohydr. Res. 173, 273, 1988.
   PubMed Web of Science ®Google Scholar
• Bray, M. R and Clarke, A. J., Identification of an essential tyrosyl residue in the binding site of Schizophyllum commune xylanase-A, Biochemistry, 34, 2006, 1995.
   PubMed Web of Science ®Google Scholar
• Hachem, M. A., Karlsson, E. N., Bartonek-Roxa, E., Raghothama, S., Simpson, P. J., Gilbert, H. J., Williamson, M. P., and Holst, O., Carbohydrate-binding modules from a thermostable Rodothermus marinus xylanase: cloning, expression and binding studies, Biochem. J. 345, 53, 2000.
   PubMed Web of Science ®Google Scholar
• Dupont, C., Roberge, M., Shareck, F., Morosoli, R, and Kluepfel, D., Substrate-binding domains of glycanases from Streptomvces lividans: characterization of a new family of xylan-binding domains, Biochem. J. 330, 41, 1998.
   PubMed Web of Science ®Google Scholar
• Bolam, D. N., Xie, H., White, P., Simpson. P. J., Hancock, S. M., Williamson, M. P., and Gilbert, H. J., Evidence for synergy between family 2b carbohydrate binding molecules in Cellulomonas fimi xylanase 11A, Biochemistry, 34, 2468, 2001.
   Google Scholar
• Xu, G. Y., Ong, E., Gilkes, N. R, Kilburn, D. G., Muhandiram, D. R, Harris-Brandts, M., Carver, J. P., Kay, L. E., and Harvey, T. S., Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy, Biochemistry, 34, 6993, 1995.
   PubMed Web of Science ®Google Scholar
• Black, G.W., Rixon, J.E., Clarke, J.H., Hazlewood, G.P., Ferreira, L.M.A., Bolam. D.N., and Gilbert, H. J., Cellulase binding domains and linker sequences potenciate the activity of hemicellulases against complex substrates, J. Biotechnol. 57, 59, 1997.
   PubMedGoogle Scholar
• Clarke, A. J., Bray, M. R, and Strating, H., β-Glycanases and xylanases. Their mechanism of action in ACS Symposium Series No: 533, American Chemical Society, USA, 1993, 27.
   Google Scholar
• Wong, K K Y. and Maringer, U. Substrate hydrolysis by combinations Trichoderma xylanases. World J. Microbiol. Biotechnol. 15, 23, 1999.
   Web of Science ®Google Scholar
• Wang, P., Ali, S., Mason, J. C., Sims, P. F. G., and Broda, P., Xylanases from Streptomvces cyaneus, in Xylans and Xylanases, Visser, J., Kusters-van Someran, M. A., and Voragen, A. G. J. Eds., Elsevier Science Publishers, Amsterdam BV, 1992, 225.
   Google Scholar
• Zhao, Y., Chany H, C. J., Sims, P. F. G., and Sinnott, M L., Definition of the substrate specificity of the ‘ sensing’ xylanase of Streptomyces cyaneus using xylooligosaccharide and cellooligsaccharide glycosides of 3,4-dinitrophenol, J. Biotechnol. 57, 181, 1997.
   PubMed Web of Science ®Google Scholar
• Gomes, D.J., Gomes, J., and Steiner, W., Factors influencing the induction of endo-xylanase by Thermoascus aurantiacus. J. Biotechnol. 33, 87, 1994.
   Web of Science ®Google Scholar
• Rapp, P. and Wagner, F., Production and properties of xylan-degrading enzyme from Cellulomonas uda. Appl. Environ. Microbiol. 51, 746, 1986.
   PubMed Web of Science ®Google Scholar
• Conrad. D. and Nothen, W., Hydrolysis of xylodextrins (DP 2-6) by xylanolytic enzymes from Aspergillus niger. Proc. 3^rd Eur. Congr. Biotechnol. Vol. 2, 1984, 169.
   Google Scholar
• Rajaram, S. and Varma, A., Production and characterisation of xylanase from Bacillus thermoalkalophilus grown on agricultural wastes, Appl. Microbiol. Biotechnol. 34, 141, 1990.
   Web of Science ®Google Scholar
• Saier, M. H. and Fagan, M. J., Catabolic repression, in Encyclopaedia of Microbiology, Vol.1, Lederberg, J., Ed. Academic Press, San Diego, CA, 1992, 431.
   Google Scholar
• Moat, A. G. and Foster, J. W., Regulation of the prokaryotic gene expression, in Microbial physiology, Wiley-Liss, New York, 1995a, 152.
   Google Scholar
• Moat, A. G. and Foster, J. W., Carbohydrate metabolism and energy production, in Microbial physiology, Wiley-Liss, New York, 1995b, 305.
   Google Scholar
• Peij, N. N. M. E. van, Gielkens, M. M. C., Vries, R P. de. Visser, J and Graff, L. H. de., The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger, Appl. Environ. Microbiol. 64, 3615, 1998.
   PubMed Web of Science ®Google Scholar
• Qureshy, A. F., Khan, L. A., and Khanna S., Expression of Bacillus circulons Teri-42 xylanase gene in Bacillus subtilis, Enzyme-Microb. Technol. 27, 227–33, 2000.
   PubMed Web of Science ®Google Scholar
• Gupta, N., Reddy, V. S. Maiti, S., and Ghosh, A., Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus sp. strain NG27, Appl. Environ. Microbiol. 66, 2631, 2000.
   PubMed Web of Science ®Google Scholar
• Araki, T., Hashikawa, S., and Morishita, T., Cloning, sequencing, and expression in Escherichia coli of the new gene encoding β-1, 3-xylanase from a marine bacterium. Vibrio sp. strain XY-214, Appl. Environ. Microbiol. 66, 1741, 2000.
   PubMed Web of Science ®Google Scholar
• Lee, H J. Shin, D. J., Cho, N. C., Kim, H O., Shin, S. Y., Im, S. Y., Lee, H. B., Chun, S. B., and Bai, S., Cloning, expression and nucleotide sequences of two xylanase genes from Paenibacillus sp. Biotechnol. Lett. 22, 387, 2000.
   Web of Science ®Google Scholar
• Panbangred, W., Fukusaki, E., Epifanio, E. C., Shinmyo, A., and Okada, H., Expression of a xylanase gene of Bacillus pumilus in Escherichia coli and Bacillus subtilis, Appl. Microbiol. Biotechnol. 22, 259, 1985.
   Web of Science ®Google Scholar
• Honda, H. Kudo, T., Horikoshi, K, Molecular cloning and expression of the xylanase gene of alkalophilic Bacillus sp. strain C125 in Escherichia coli, J. Bacteriol. 161, 784, 1985.
   PubMed Web of Science ®Google Scholar
• Sung, W. L., Luk, C. K, Zahab, D. M., and Wakarchuk, W., Overexpression of the Bacillus subtilis and circulons xylanases in Escherichia coli, Prot. Expression Purifin. 4, 200, 1993.
   PubMed Web of Science ®Google Scholar
• Jung, K H. and Pack, M. Y., Expression of a Clostridium thermocell um xylanase gene in Bacillus subtilis. Biotech. Lett. 15, 115, 1993.
   Web of Science ®Google Scholar
• Gat, O., Lapidot, A., Alchanati, I., Regueros, C., and Shoham, Y., Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase. Appl. Environ. Microbiol. 60, 1889, 1994.
   PubMed Web of Science ®Google Scholar
• Arhin, F. F., Shareck, F., Kluepfel, D., and Morosoli, R, Effects of disruption of xylanase encoding genes on the xylanolutic system of Streptomyces lividans, J. Bacteriol. 176, 4924, 1994.
   PubMed Web of Science ®Google Scholar
• Mazy-Servais, C., Moreau, A., Gerard, C., and Dusart, J., Cloning and nucleotide sequence of a xylanase-encoding gene from Streptomyces sp. strain EC3, DNA Sequence — The J. Sequen. Mapping, 6, 147, 1996.
   PubMed Web of Science ®Google Scholar
• Bron, S., Bolhuis, A., Tjalsma, H., Holsappel, S., Venema, G., and van Dijl, J. M., Protein secretion and possible roles for multiple signal peptidases for precursor processing in Bacilli, J. Biotechnol. 64, 3, 1998.
   PubMed Web of Science ®Google Scholar
• Ethier, J.–F., Harpin, S., Girard, C., Beaulie, C., Dery, C.V., and Brzezinski, R, Clonong of two xylanase genes from the newly isolated actinomycete Actinomadura sp. strain FC7 and characterization of the gene products. Can J. Microbiol. 40, 362, 1994.
   Web of Science ®Google Scholar
• Srivastava, P. and Mukherjee, K J., Cloning, characterization and expression of xylanase gene from Bacillus lyticus in Escherichia coli and Bacillus subtilis, Preparative Biochem. Biotechnol. 31, 389, 2001.
   PubMed Web of Science ®Google Scholar
• Harbak, L. and Thygesen, H. V., Safety evaluation of a xylanase expressed in Bacillus subtilis, Food and Chemical Toxicol., 40, 1, 2002.
   PubMed Web of Science ®Google Scholar
• Cho, K H., Jung, K H., and Pack, M. Y., Xylanase encoded by genetically engineered Clostridium thermocellum gene in Bacillus subtilis, Biotechnol. Lett. 17, 157, 1995.
   Web of Science ®Google Scholar
• Georis, J., Giannotta, F., Lamotte-Brasseur, J., Devreese, B. Beeumen, J. V., Granier, B., Frere, J., Sequence, overproduction and purification of the family 11 endo-β-1,4-xylanase encoded by the xyl1gcno. of Streptomyces sp. S38, Gene 237, 123, 1999.
   PubMed Web of Science ®Google Scholar
• Bernier, R., Jr., Rho, D., Arcand, Y., and Desrochers, M. X., Partial characterization of an Escherichia coli strain harboring a xylanase encoding plasmid. Biotech. Lett. 7, 797, 1985.
   Web of Science ®Google Scholar
• Karlsson, O., Pettersson, B., and Westermark, U. Linkages between residual lignin and carbohydrates in bisulphite (manefite) pulps, J. Pulp and Paper Science 27, 310. 2001.
   Google Scholar
• Iverson, T. and Wannstrom, S., Lignin-carbohydrate bonds in a residual lignin isolated from pine kraft pulp, Holzforschung 40, 19, 1986.
   Web of Science ®Google Scholar
• Madlala, A. M., Bissoon, S., Singh, S., and Christove, L., Xylanase induced reduction of chlorine dioxide consumption during elemental chlorine-free bleaching of different pulp types, Biotechnol Lett. 23, 345, 2001.
   Web of Science ®Google Scholar
• Loras, V., Bleaching of chemical pulps, in Pulp and Paper Chemistry and Chemical Technology, Casey, J.P., Ed. 3rd ed., Vol.1, John Wiley & Sons, New York, 1980, 663.
   Google Scholar
• Bajpai, P. and Bajpai, P. K., Development of a process for the production of dissolving pulp using xylanase enzyme, Appita J., 54, 381, 2001.
   Web of Science ®Google Scholar
• Pekarovicova, A., Kozankova, J., Mikutasova, M., Jankovic, P., and Pekarovic, J., SEM study of xylanase pretreated pulps, in Xylans and Xylanases, Visser, J., Kusters-van Someran, M. A., and Voragen, A. G. J. Eds., Elsevier Science Publishers, Amsterdam B.V. 1992, 559.
   Google Scholar
• Biely, P., Biotechnological potential and production of xylanolytic systems free of cellulases, ACS Symp. Ser. 460, 408, 1991.
   Google Scholar
• Malathi, V. and Devegowda, G., In vitro evaluation of nonstarch polysaccharide digestibility of feed ingredients by enzymes. Poultry Sci., 80, 302, 2001.
   PubMed Web of Science ®Google Scholar
• Lynd, L. R, Cushman, J. H., Nicholas, RJ., and Wyman, C. E., Fuel ethanol from cellulosic biomass. Science 251, 1318, 1991.
   PubMed Web of Science ®Google Scholar
• Ahring, B. K., Licht, D., Schimdt, A. S., Sommer, P., and Thomsen, A. B., Production of ethanol from wet oxidised wheat straw by Thermoanaerobacter mathranii, Bioresource Technol. 68, 3, 1999.
   Web of Science ®Google Scholar