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Fungal Xylanase Xylanase Aus Pilz Xylanase Fongiques

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Fungal Xylanase Xylanase Aus Pilz Xylanase Fongiques (19) TZZ _¥¥¥_T (11) EP 2 183 363 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.: of the grant of the patent: C12N 9/24 (2006.01) C12P 7/10 (2006.01) 08.06.2016 Bulletin 2016/23 C12P 19/14 (2006.01) C11D 3/386 (2006.01) (21) Application number: 08797046.3 (86) International application number: PCT/US2008/071982 (22) Date of filing: 01.08.2008 (87) International publication number: WO 2009/018537 (05.02.2009 Gazette 2009/06) (54) FUNGAL XYLANASE XYLANASE AUS PILZ XYLANASE FONGIQUES (84) Designated Contracting States: (56) References cited: AT BE BG CH CY CZ DE DK EE ES FI FR GB GR WO-A1-98/15633 WO-A2-00/20555 HR HU IE IS IT LI LT LU LV MC MT NL NO PL PT WO-A2-01/79507 WO-A2-2008/008070 RO SE SI SK TR US-A1- 2004 002 136 US-A1- 2006 053 514 US-A1- 2006 134 747 US-A1- 2006 218 671 (30) Priority: 02.08.2007 US 833133 US-A1- 2007 077 630 (43) Date of publication of application: • GUSAKOV ALEXANDER V ET AL: "Purification, 12.05.2010 Bulletin 2010/19 cloning and characterisation of two forms of thermostable and highly active (73) Proprietor: Danisco US Inc. cellobiohydrolase I (Cel7A) produced by the Palo Alto, CA 94304 (US) industrial strain of Chrysosporium lucknowense" ENZYME AND MICROBIAL (72) Inventors: TECHNOLOGY, vol. 36, no. 1, 6 January 2005 • GUSAKOV, Alexander, Vasilievich (2005-01-06), pages 57-69, XP002608583 ISSN: Moscow 115054 (RU) 0141-0229 • PUNT, Peter, J. • GUSAKOV ALEXANDER V ET AL: "Design of NL-3994 XT Houten (NL) highly efficient cellulase mixtures for enzymatic • VERDOES, Jan, Cornelis hydrolysis of cellulose" BIOTECHNOLOGY AND deceased (NL) BIOENGINEERING, WILEY & SONS, HOBOKEN, • SINITSYN, Arkady, Panteleimonovich NJ, US LNKD- DOI:10.1002/BIT.21329, vol. 97, no. Moscow 119590 (RU) 5, 1 August 2007 (2007-08-01) , pages 1028-1038, • VLASENKO, Elena XP002565359 ISSN: 0006-3592 [retrieved on Davis, CA 95616 (US) 2007-01-12] • HINZ, Sandra Wihelmina, Agnes • DATABASE UniProt [Online] 1 May 1997 NL-6708 SN Wageningen (NL) (1997-05-01), Iikura et al.: "Cloning of a Gene • GOSINK, Mark Encoding a Putative Xylanase with a Wellington, FL 33414 (US) Cellulose-Binding Domain from Humicola • JIANG, Zhijie grisea" XP002608584 retrieved from EBI West Palm Beach, FL 33401 (US) Database accession no. P79046 • DATABASE UniProt [Online] 21 March 1996 (74) Representative: Nederlandsch Octrooibureau (1996-03-21), Birren et al.: "Annotation of the P.O. Box 29720 Chaetomium globosum CBS 148.51 genome" 2502 LS The Hague (NL) XP002608585 retrieved from EBI Database accession no. Q2HIC4 Note: Within nine months of the publication of the mention of the grant of the European patent in the European Patent Bulletin, any person may give notice to the European Patent Office of opposition to that patent, in accordance with the Implementing Regulations. Notice of opposition shall not be deemed to have been filed until the opposition fee has been paid. (Art. 99(1) European Patent Convention). EP 2 183 363 B1 Printed by Jouve, 75001 PARIS (FR) (Cont. next page) EP 2 183 363 B1 • DATABASE Geneseq [Online] 19 February 1997 • USTINOV B B ET AL: "Comparison of properties (1997-02-19), Ikura et al.: "Cloning of a Gene and mode of action of six secreted xylanases Encoding a Putative Xylanase with a from Chrysosporium lucknowense" ENZYME Cellulose-Binding Domain from Humicola AND MICROBIAL TECHNOLOGY, STONEHAM, grisea" XP002608586 retrieved from EBI MA, US LNKD- Database accession no. AB001030 DOI:10.1016/J.ENZMICTEC.2008.01.017, vol. 43, • DATABASE Geneseq [Online] 18 October 2007 no. 1, 7 July 2008 (2008-07-07), pages 56-65, (2007-10-18), "Acremonium thermophilum XP022683403 ISSN: 0141-0229 [retrieved on XYN60/Xyn10A gene." XP002608587 retrieved 2008-02-07] from EBI accession no. GSN:AGD76041 • HINZ SANDRA W A ET AL: "Hemicellulase Database accession no. AGD76041 production in Chrysosporium lucknowense C1" • MARKOV A V ET AL: "Properties of JOURNAL OF CEREAL SCIENCE, ACADEMIC hemicellulases of the enzyme complex from PRESS LTD, XX LNKD- Trichoderma longibrachiatum" APPLIED DOI:10.1016/J.JCS.2009.07.005, vol. 50, no. 3, 1 BIOCHEMISTRYAND MICROBIOLOGY, KLUWER November 2009 (2009-11-01), pages 318-323, ACADEMIC PUBLISHERS-PLENUM XP002593773 ISSN: 0733-5210 [retrieved on PUBLISHERS, NE LNKD- 2009-08-20] DOI:10.1134/S000368380606007X, vol. 42, no. 6, 1 December 2006 (2006-12-01), pages 573-583, XP019432666 ISSN: 1608-3024 2 EP 2 183 363 B1 Description FIELD OF THE INVENTION 5 [0001] This invention relates to novel enzymes and novel methods for producing the same. More specifically this invention relates to enzymes produced by fungi. The invention also relates to a method to convert lignocellulosic biomass to fermentable sugars with enzymes that degrade the lignocellulosic material and novel combinations of enzymes, including those that provide a synergistic release of sugars from plant biomass. The invention also relates to methods to use the novel enzymes and compositions of such enzymes in a variety of other processes, including washing of 10 clothing, detergent processes, deinking and biobleaching of paper and pulp, and treatment of waste streams. BACKGROUND OF THE INVENTION [0002] Large amounts of carbohydrates in plant biomass provide a plentiful source of potential energy in the form of 15 sugars (both five carbon and six carbon sugars) that can be utilized for numerous industrial and agricultural processes. However, the enormous energy potential of these carbohydrates is currently under-utilized because the sugars are locked in complex polymers, and hence are not readily accessible for fermentation. These complex polymers are often referred to collectively as lignocellulose. Sugars generated from degradation of plant biomass potentially respresent plentiful, economically competitive feedstocks for fermentation into chemicals, plastics, and fuels, including ethanol as 20 a substitute for petroleum. [0003] For example, distillers’ dried grains (DDG) are lignocellulosic byproducts of the corn dry milling process. Milled whole corn kernels are treated with amylases to liquefy the starch within the kernels and hydrolyze it to glucose. The glucose so produced is then fermented in a second step to ethanol. The residual solids after the ethanol fermentation and distillation are centrifuged and dried, and the resulting product is DDG, which is used as an animal feed stock. 25 Although DDG composition can vary, a typical composition for DDG is: 32% hemicellulose, 22% cellulose, 30% protein, 10% lipids, 4% residual starch, and 4% inorganics. In theory, the cellulose and hemicellulose fractions, comprising about 54% of the weight of the DDG, can be efficiently hydrolyzed to fermentable sugars by enzymes; however, it has been foundthat the carbohydrates comprisinglignocellulosic materialsin DDG aremore difficult to digest. To date, the efficiency of hydrolysis of these (hemi) cellulosic polymers by enzymes is much lower than the hydrolytic efficiency of starch, due 30 to the more complex and recalcitrant nature of these substrates. Accordingly, the cost of producing the requisite enzymes is higher than the cost of producing amylases for starch hydrolysis. [0004] Major polysaccharides comprising lignocellulosic materials include cellulose and hemicelluloses. The enzymatic hydrolysis of these polysaccharides to soluble sugars (and finally to monomers such as glucose, xylose and other hexoses and pentoses) is catalyzed by several enzymes acting in concert. For example, endo-1,4- β-glucanases (EGs) 35 and exo-cellobiohydrolases (CBHs) catalyze the hydrolysis of insoluble cellulose to cellooligosachharides (with cellobiose the main product), while β-glucosidases (BGLs) convert the oligosaccharides to glucose. Similarly, xylanases, together with other enzymes such as α-L-arabinofuranosidases, feruloyl and acetylxylan esterases and β-xylosidases, catalyze the hydrolysis of hemicelluloses. [0005] Regardless of the type of cellulosic feedstock, the cost and hydrolytic efficiency of enzymes are major factors 40 that restrict the widespread use of biomass bioconversion processes. The hydrolytic efficiency of a multi-enzyme complex in the process of lignocellulosic saccharification depends both on properties of the individual enzymes and the ratio of each enzyme within the complex. [0006] Enzymes useful for the hydrolysis of complex polysaccharides are also highly useful in a variety of industrial textile applications, as well as industrial paper and pulp applications, and in the treatment of waste streams. For example, 45 as an alternative to the use of pumice in the stone washing process, methods for treating cellulose-containing fabrics for clothing with hydrolytic enzymes, such as cellulases, are known to improve the softness or feel of such fabrics. Cellulases are also used in detergent compositions, either for the purpose of enhancing the cleaning ability of the composition or as a softening agent. Cellulases are also used in combination with polymeric agents in processes for providing a localized variation in the color density of fibers. Such enzymes can also be used for the saccharification of 50 lignocellulosic biomass in waste streams, such as municipal solid waste, for biobleaching of wood pulp, and for deinking of recycled print paper. As with the hydrolysis of these polysaccharides in lignocellulosic materials for use as feedstocks described above, the cost and hydrolytic efficiency of the enzymes are major factors that control the use of enzymes in these processes. [0007] Filamentous fungi are a source of cellulases and hemicellulases, as well as other enzymes useful in the enzy- 55 matic hydrolysis of major polysaccharides. In particular, strains of Trichoderma sp., such as T. viride, T. reesei and T. longibrachiatum, and Penicillium sp., and enzymes derived from these strains, have previously been used to hydrolyze crystalline cellulose. However, the costs associated with producing enzymes from these fungi, as well as the presence of additional, undesirable enzymes, remains a drawback. It is therefore desirable to produce inexpensive enzymes and 3 EP 2 183 363 B1 enzyme mixtures that efficiently degrade cellulose and hemicellulose for use in a variety of agricultural and industrial applications.
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