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WO 2018/057420 Al 29 March 2018 (29.03.2018) W!P O PCT

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WO 2018/057420 Al 29 March 2018 (29.03.2018) W!P O PCT (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2018/057420 Al 29 March 2018 (29.03.2018) W!P O PCT (51) International Patent Classification: Chestnut Run Plaza 721/2340, 974 Centre Road, PO Box A23K 20/189 (2016.01) A23K 50/10 (2016.01) 2915, Wilmington, Delaware 19805 (US). A23K 10/14 {2016.01) (81) Designated States (unless otherwise indicated, for every (21) International Application Number: kind of national protection available): AE, AG, AL, AM, PCT/US2017/051758 AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, (22) International Filing Date: DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, 15 September 2017 (15.09.2017) HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, (25) Filing Language: English KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (26) Publication Langi English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (30) Priority Data: SC, SD, SE, SG, SK, SL, SM, ST, SV, SY,TH, TJ, TM, TN, 62/398,741 23 September 2016 (23.09.2016) US TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (71) Applicant: DUPONT NUTRITION BIOSCIENCES (84) Designated States (unless otherwise indicated, for every APS [DK/DK]; Langebrogade 1, DK-141 1 Copenhagen K kind of regional protection available): ARIPO (BW, GH, (DK). GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (71) Applicant (for SC only): E. I. DU PONT DE NEMOURS TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, AND COMPANY [US/US]; Chestnut Run Plaza, 974 Cen EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, tre Road, P. O. Box 2915, Wilmington, Delaware 19805 MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, (US). TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, (72) Inventors: YU, Shukun; GUNNAR HEJDEMANS GATA KM, ML, MR, NE, SN, TD, TG). 29, S-212 40 Malmo (SE). KRAGH, Karsten Matthias; Madsbjergparken 21, DK-8270 Hoejbjerg (DK). LI, Went- Published: ing; 92B HIGH STREET, Marlborough Wiltshire SN8 1HD — with international search report (Art. 21(3)) (GB). (74) Agent: CHRISTENBURY, Lynne M.; E.I. du Pont de Nemours and Company, Legal Patent Records Center, (54) Title: USE OF LOW PH ACTIVE ALPHA- 1,4/1 ,6-GLYCOSIDE HYDROLASES AS A FEED ADDITIVE FOR RUMINANTS TO ENHANCE STARCH DIGESTION 60 50 □ Glucose (Gl) ■ Maltose (G2) 40 5 30 20 10 AkAA 20µ Ι Pepsin 50µ Ι Α Ι<ΑΑ 20µ Ι + Pepsin Α Ρ 0µ Ι AkAA 20µ Ι + AFP o 50µ Ι 50µ Ι Figure 1. Release of glucose and maltose from corn flour by AkAA alpha-amylase in the presence © of pepsin and AFP proteases at pH3.2. 00 (57) Abstract: Disclosed are uses at least one alpha- 1,4/ 1,6-glycoside hydrolase (GLCH) as a feed additive for a ruminant wherein said hydrolase: (a) has at least 20% activity at pH less than or equal to 3 in the presence of pepsin as compared to activity of the hydrolase o at pH 6 in the presence of pepsin, (b) said hydrolase is active in at least two of three digestive chambers of a ruminant comprising a rumen, an abomasum and a small intestine and (c) the hydrolase works with pancreatic amylase to increase glucose yield. USE OF LOW PH ACTIVE ALPHA-1 ,4/1 ,6-GLYCOSIDE HYDROLASES AS A FEED ADDITIVE FOR RUMINANTS TO ENHANCE STARCH DIGESTION FIELD The field relates to animal nutrition and, in particular, to the use of low pH active alpha-1 ,4/1 ,6 glycoside hydrolases (GLCH) such as alpha-amylases, glucoamylases and alpha-glucosidases as a feed additive for ruminants to enhance starch digestion. BACKGROUND Ruminants have the unique ability to convert roughage into protein and energy through their microbial/enzyme digestive systems. Accordingly, ruminants play an important role in the earth's ecology and in the food chain. The primary difference between ruminants and nonruminants is that ruminants' stomachs have four compartments: the rumen, reticulum, omasum, and abomasum. In the first two chambers, the rumen and the reticulum, the food is mixed with saliva and separates into layers of solid and liquid material. Solids clump together to form the cud or bolus. The cud is then regurgitated and chewed to completely mix it with saliva and to break down the particle size. Fiber, especially cellulose and hemicellulose, is primarily broken down in these chambers by microbes (mostly bacteria, as well as some protozoa, fungi and yeast) into the three major volatile fatty acids (VFAs): acetic acid, propionic acid, and butyric acid. Protein and nonstructural carbohydrate (pectin, sugars, and starches) are also fermented. Though the rumen and reticulum have different names, they represent the same functional space as digesta and can move back and forth between them. Together, these chambers are called the reticulorumen. The degraded digesta, which is now in the lower liquid part of the reticulorumen, then passes into the next chamber, the omasum, where water and many of the inorganic mineral elements are absorbed into the blood stream. After this, the digesta is moved to the true stomach, the abomasum. The abomasum is the direct equivalent of the monogastric stomach, and digesta is digested here in much the same way. Digesta is finally moved into the small intestine, where the digestion and absorption of nutrients occurs. Microbes produced in the reticulorumen are also digested in the small intestine. Fermentation continues in the large intestine in the same way as in the reticulorumen. Enzymes for use as feed additives ruminants are mainly fibrolytic enzymes, such as cellulases, beta-glucanases and hemicellulases (Table 1 in Beauchemin et al., 2004. A rationale for the development of feed enzyme products for ruminants. Can. J . Anim. Sci. 84: 23-36). Reports on starch hydrolases for ruminant uses are limited. Starch hydrolases are grouped as endo- and exo-amylases. Endoamylases, also called alpha-amylases (E.C. 3.2.1 . 1 ) , are starch-degrading enzymes that catalyse the hydrolysis of internal alpha-1 ,4-O-glycosidic bonds in polysaccharides while retaining an alpha-anomeric configuration in the products. Most of the alpha-amylases need calcium ions (Ca2+) for their activity, structural integrity and stability. The alpha-amylase family, i.e., the clan GH-H of glycoside hydrolases is the largest family of glycoside hydrolases, transferases, and isomerases comprising nearly 30 different enzyme specificities. A large variety of enzymes are able to act on starch. These enzymes can be divided into four groups: endoamylases, exoamylases, debranching enzymes and transferases. Endoamylases cleave internal alpha-1 ,4 bonds resulting in alpha-anomeric products. Exoamylases cleave alpha-1 ,4 or alpha-1 ,6 bonds of the external glucose residues resulting in alpha- or beta-anomeric products. Debranching enzymes hydrolyze alpha-1 ,6 bonds exclusively leaving long linear polysaccharides. Transferases cleave alpha-1 ,4 glycosidic bond of the donor molecule and transfer part of the donor to a glycosidic acceptor forming a new glycosidic bond. Glycoside hydrolases have been divided into classes based on their mode of reaction and families based on their well-defined amino acid sequence similarities. Most of the starch converting enzymes belong to GH-1 3 family. The GH-1 3 family can be further classified based on a larger unit called clan, which is the three-dimensional structure of catalytic module. Among the fourteen clans (A-N) defined for glycosidases and transglycosidases, alpha-amylase family (GH-13) belongs to the eighth clan GH-H. Animals synthesize and secret digestive pancreatic alpha-amylase for starch hydrolysis. This alpha-amylase has an optimal pH around pH 6-7 and is active in the small intestine. The addition of microbial amylases to feed can further increase animals' starch digestion possibly due to the fact that the secreted pancreatic amylase is not enough and/or the feed passage in the digestive tract of the small intestine is quite fast so that the pancreatic amylase does not have enough time to thoroughly digest the starch, especially in the case of poultry. (Isaksen, M . F. Cowieson, A . J . Kragh, K . M . (201 0). Starch- and protein-degrading enzymes: biochemistry, enzymology and characteristics relevant to animal feed use. In: Enzymes in farm animal nutrition /edited by M.R. Bedford and G.G. Partridge. Pages 85-95). Thus, endoamylases have been one of the feed enzymes widely used in the feed industry. The most common used feed amylases are derived from Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and Aspergillus oryzae. These feed amylases have optimal activity in the pH range of pH4 to pH8. Most of them have considerable tolerance to pepsin. However, these feed enzymes appear not to have a raw starch binding domain (SBD) and may have limited capability to hydrolyze non-gelatinized raw starch. Pianchot et aL, (Extensive degradation of native starch granules by alpha- amylase from Aspergillus fumigatus, Journal of Cereal Science, Volume 2 1, Issue 2 , 1995, Pages 163-1 7 1) , reported the low efficiency of alpha-amylase from Bacillus sp. in degrading granular starch compared to pancreatic amylase. EFSA (Scientific Opinion on the safety and efficacy of Ronozyme RumiStar (alpha-amylase) as a feed additive for dairy cows.
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