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(12) Patent Application Publication (10) Pub. No.: US 2015/0132824 A1 Segura Et Al

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(12) Patent Application Publication (10) Pub. No.: US 2015/0132824 A1 Segura Et Al US 2015O132824A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0132824 A1 Segura et al. (43) Pub. Date: May 14, 2015 (54) POLYPEPTIDES HAVING XANTHAN (30) Foreign Application Priority Data DEGRADING ACTIVITY AND POLYNUCLEOTDESENCODING SAME May 7, 2012 (EP) .................................. 12167O23.6 Jan. 10, 2013 (EP) .................................. 13150833.5 (71) Applicant: Novozymes A/S, Bagsvaerd (DK) (72) Inventors: Dorotea Raventos Segura, Rungsted Publication Classification (DK); Peter Fischer Halin, Holte (DK); Anders Viksoe-Nielsen, Slangerup (51) Int. C. (DK); Lars Anderson, Malmoe (SE): CI2N 9/42 (2006.01) Martin Simon Borchert, Hilleroed (DK); Leigh Murphy, Roskilde (DK); CID 3/386 (2006.01) Astrid Boisen, Soeborg (DK); Lorena C09K8/08 (2006.01) G. Palmén, Malmoe (SE); Kenneth CI2N 9/88 (2006.01) Jensen, Oelsted (DK); Carsten (52) U.S. C. Sjoeholm, Virum (DK); Tine Hoff, CPC ................ CI2N 9/2437 (2013.01); C12N 9/88 Holte (DK); Charlotte Blom, Lynge (2013.01): CII D3/38645 (2013.01): CIID (DK) 3/386.36 (2013.01); C09K8/08 (2013.01); C12Y 302/01004 (2013.01); C12Y402/02012 (21) Appl. No.: 14/395,165 (2013.01) (22) PCT Fled: May 7, 2013 (57) ABSTRACT (86) PCT NO.: PCT/EP2013/059472 S371 (c)(1), The present invention relates to isolated polypeptides having (2) Date: Oct. 17, 2014 Xanthan degrading activity, catalytic domains and polynucle otides encoding the polypeptides and catalytic domains. The Related U.S. Application Data invention also relates to nucleic acid constructs, vectors, and (60) Provisional application No. 61/644,033, filed on May host cells comprising the polynucleotides as well as methods 8, 2012, provisional application No. 61/754,663, filed of producing and using the polypeptides and catalytic on Jan. 21, 2013. domains. GH 9 gene fragment Wector fragment Signal peptide Terminator Wector fragment B. subtilis chromosomal region for integration triple promter CAT B. subtilis chromosomal region for integratic | C59AC GH9 Construct 12721 bp Patent Application Publication May 14, 2015 US 201S/O132824 A1 / ?0n.u?SUOD6H5)DV6GO FIGURE 1 US 2015/O 132824 A1 May 14, 2015 POLYPEPTIDES HAVING XANTHAN sequence identity to SEQID NO: 14 has been published by T. DEGRADING ACTIVITY AND Morohoshi et al. (2011).J. Bacteriol. 193(8), 2072-2073. POLYNUCLEOTDESENCODING SAME 0009. In recent years xanthan gum has been use as an ingredient in many consumer products including foods (e.g. REFERENCE TO ASEQUENCE LISTING as thickening agent in Salat dressings and dairy products) and cosmetics (e.g. as Stabilizer and thickener in toothpaste and 0001. This application contains a Sequence Listing in make-up to prevent ingredients from separating) and cosmet computer readable form, which is incorporated herein by ics (such as Sun creams). Further Xanthan gum has found use reference. in the oil industry as well as an additive to regulate the vis cosity of drilling fluids etc. The widespread use of Xanthan BACKGROUND OF THE INVENTION gum has led to a desire to degrade solutions or gels of Xanthan 0002 1. Field of the Invention gum thereby allowing easier removal of the byproducts. It has 0003. The present invention relates to polypeptides having been suggested to add a Xanthan lyase to a detergent compo Xanthan degrading activity, in particular Xanthan lyase activ sition in order to remove Xanthan gum containing stains, e.g. ity and to GH9 endoglucanases having activity on Xanthan in EP0896998A, but this publication does not contain any gum pretreated with Xanthan lyase, catalytic domains, and experimental data demonstrating any effect thereof. polynucleotides encoding the polypeptides and catalytic 0010. The invention provides new and improved enzymes domains. The invention also relates to nucleic acid constructs, for the degradation of Xanthan gum and the use of Such vectors, and host cells comprising the polynucleotides as well enzymes for cleaning purposes, such as the removal of Xan as methods of producing and using the polypeptides and than gum stains, and in the drilling and oil industries. catalytic domains. The invention further relates to composi tions comprising GH9 endoglucanases and/or Xanthan lyases SUMMARY OF THE INVENTION for use in detergents and in the drilling and oil industries. 0011. In one aspect the invention relates to an isolated 0004 2. Description of the Related Art GH9 endoglucanase having activity on Xanthan gum pre 0005 Xanthan gum is a polysaccharide derived from the treated with Xanthan lyase, selected from the group consisting bacterial coat of Xanthomonas campestris. It is produced by of: the fermentation of glucose, Sucrose, or lactose by the Xan 0012 (a) a polypeptide having at least 80%, e.g., at least thomonas Campestris bacterium. After a fermentation period, 81%, at least 82%, at least 83%, at least 84%, at least the polysaccharide is precipitated from a growth medium 85%, at least 86%, at least 87%, at least 88%, at least with isopropyl alcohol, dried, and ground into a fine powder. 89%, at least 90%, at least 91%, at least 92%, at least Later, it is added to a liquid medium to form the gum. 93%, at least 94%, at least 95%, at least 96%, at least 0006 Xanthan gum is a natural polysaccharide consisting 97%, at least 98%, at least 99%, or 100% sequence of different sugars which are connected by several different identity to the mature polypeptide of SEQID NO: 2; bonds, such as B-D-mannosyl-B-D-1,4-glucuronosyl bonds 0013 (b) a polypeptidehaving at least 80%, e.g., at least and B-D-glucosyl-B-D-1,4-glucosyl bonds. Xanthan gum is 81%, at least 82%, at least 83%, at least 84%, at least at least partly soluble in water and forms highly viscous 85%, at least 86%, at least 87%, at least 88%, at least Solutions or gels. 89%, at least 90%, at least 91%, at least 92%, at least 0007 Complete enzymatic degradation of Xanthan gum 93%, at least 94%, at least 95%, at least 96%, at least requires several enzymatic activities including Xanthan lyase 97%, at least 98%, at least 99%, or 100% sequence activity and endo-3-1,4-glucanase activity. Xanthan lyases identity to the mature polypeptide of SEQID NO: 10; are enzymes that cleave the B-D-mannosyl-B-D-1,4-glucu 0.014 (c) a polypeptide having at least 80%, e.g., at least ronosyl bond of xanthan and have been described in the 81%, at least 82%, at least 83%, at least 84%, at least literature. Xanthan degrading enzymes are known in the art 85%, at least 86%, at least 87%, at least 88%, at least e.g. have two Xanthan lyases been isolated from Paenibacillus 89%, at least 90%, at least 91%, at least 92%, at least alginolyticus XL-1 (e.g. Ruijssenaars et al. (1999) A pyru 93%, at least 94%, at least 95%, at least 96%, at least vated mannose-specific Xanthan lyase involved in Xanthan 97%, at least 98%, at least 99%, or 100% sequence degradation by Paenibacillus alginolyticus XL-1 , Appl. identity to the mature polypeptide of SEQID NO: 12: Environ. Microbiol. 65(6): 2446-2452, and Ruijssenaars et al. 0.015 (d) a polypeptidehaving at least 80%, e.g., at least (2000). A novel gene encoding xanthan lyase of Paenibacil 81%, at least 82%, at least 83%, at least 84%, at least lus alginolyticus strain XL-1 , Appl. Environ. Microbiol. 85%, at least 86%, at least 87%, at least 88%, at least 66(9): 3945-3950). 89%, at least 90%, at least 91%, at least 92%, at least 0008 Glycoside hydrolases are enzymes that catalyse the 93%, at least 94%, at least 95%, at least 96%, at least hydrolysis of the glycosyl bond to release Smaller Sugars. 97%, at least 98%, at least 99%, or 100% sequence There are over 100 classes of glycoside hydrolases which identity to the mature polypeptide of SEQID NO: 14: have been classified, see Henrissat et al. (1991) A classifica 0016 (e)a polypeptide having at least 80%, e.g., at least tion of glycosyl hydrolases based on amino-acid sequence 81%, at least 82%, at least 83%, at least 84%, at least similarities, J. Biochem. 280: 309-316 and the Uniprot web 85%, at least 86%, at least 87%, at least 88%, at least site at www.cazy.org. The glycoside hydrolase family 9 89%, at least 90%, at least 91%, at least 92%, at least (GH9) consists of over 70 different enzymes that are mostly 93%, at least 94%, at least 95%, at least 96%, at least endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1. 97%, at least 98%, at least 99%, or 100% sequence 91), B-glucosidases (EC 3.2.1.21) and exo-f-glucosamini identity to the mature polypeptide of SEQID NO: 48; dase (EC 3.2.1.165). A GH9 from Microbacterium testaceum 0017 (f) a polypeptidehaving at least 80%, e.g., at least StLB037 having 84.5% sequence identity to SEQID NO: 12, 81%, at least 82%, at least 83%, at least 84%, at least 79.1% sequence identity to SEQ ID NO: 10 and 74.0% 85%, at least 86%, at least 87%, at least 88%, at least US 2015/O 132824 A1 May 14, 2015 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence 97%, at least 98%, at least 99%, or 100% sequence identity to the mature polypeptide of SEQID NO: 134; identity to the mature polypeptide of SEQID NO. 52; 0027 (p)a polypeptidehaving at least 80%, e.g., at least 0018 (g) a polypeptidehaving at least 80%, e.g., at least 81%, at least 82%, at least 83%, at least 84%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%,
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