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WO 2017/091533 Al 1 June 20 17 (0 1.06.20 17) W P O P C T (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 2017/091533 Al 1 June 20 17 (0 1.06.20 17) W P O P C T (51) International Patent Classification: Plaza 721/2340, 974 Centre Road, PO Box 291 5 Wilming A23L 33/10 (201 6.01) CI2N 9/10 (2006.01) ton, Delaware 19805 (US). A61K 31/716 (2006.01) C08L 5/00 (2006.01) (81) Designated States (unless otherwise indicated, for every C 37/00 (2006.01) C08L 5/02 (2006.01) kind of national protection available): AE, AG, AL, AM, C12P 19/04 (2006.01) A23L 33/135 (2016.01) AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, CUP 19/08 (2006.01) A23L 33/21 (201 6.01) BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, CUP 19/16 (2006.01) A61K 8/73 (2006.01) DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, CUP 19/18 (2006.01) HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, (21) International Application Number: KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, PCT/US2016/063233 MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (22) International Filing Date: SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, 22 November 2016 (22.1 1.2016) TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (25) Filing Language: English ZW. (26) Publication Language: English ( ) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (30) Priority Data: GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, PCT/CN2015/095687 TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, 26 November 2015 (26. 11.2015) CN TJ, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, PCT/CN2016/085547 13 June 2016 (13.06.2016) CN DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, (71) Applicant: E. I. DU PONT DE NEMOURS AND COM¬ LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, PANY [US/US]; Chestnut Run Plaza, 974 Centre Road, P. SM, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, O. Box 2915, Wilmington, Delaware 19805 (US). GW, KM, ML, MR, NE, SN, TD, TG). (72) Inventors: CHENG, Qiong; 4 Collins Drive, Wilmington, Published: Delaware 19803 (US). DICOSIMO, Robert; 1607 Mas — with international search report (Art. 21(3)) ters Way, Chadds Ford, Pennsylvania 193 17-9720 (US). — before the expiration of the time limit for amending the PRASAD, Jahnavi Chandra; 2124 Haven Road, Apt F, claims and to be republished in the event of receipt of Wilmington, Delaware 19809 (US). ZHANG, Zhenghong; amendments (Rule 48.2(h)) Room 2702, Building 13, Lane 655, Chengyin Road, Baoshan District, Shanghai 200444 (CN). — with sequence listing part of description (Rule 5.2(a)) (74) Agent: CHESIRE, Dennis; E. I. du Pont de Nemours and Company, Legal Patent Records Center, Chestnut Run © - © (54) Title: POLYPEPTIDES CAPABLE OF PRODUCING GLUCANS HAVING ALPHA- 1,2 BRANCHES AND USE OF THE SAME (57) Abstract: Disclosed herein are proteins capable of forming glucans having alpha- 1,2 linkages/branches, reactions and methods for producing such glucan, compositions comprising such glucan, and various applications thereof. POLYPEPTIDES CAPABLE OF PRODUCING GLUCANS HAVING ALPHA- 1,2 BRANCHES AND USE OF THE SAME This application claims the benefit of International Application Nos. PCT/CN20 15/095687 (filed November 26, 2015) and PCT/CN2016/085547 (filed June 13, 2016), both of which are incorporated herein by reference in their entireties. FIELD OF INVENTION The disclosure relates to, for example, proteins that are capable of forming glucan having alpha- 1,2 linkages, reactions and methods for producing such glucan, compositions comprising this glucan, and various applications of using this glucan. REFERENCE TO SEQUENCE LISTING SUBMITTED ELECTRONICALLY The official copy of the sequence listing is submitted electronically via EFS-Web as an ASCII formatted sequence listing with a file named 20161 122_CL6550WOPCT3_SequenceListingExtraLinesRemoved.txt created on November 21, 2016 and having a size of 413 kilobytes and is filed concurrently with the specification. The sequence listing contained in this ASCII-formatted document is part of the specification and is herein incorporated by reference in its entirety. BACKGROUND The enzymatic addition of alpha- 1,2 branching to dextrans has been reported. A glucosyltransferase (DsrE) from Leuconostoc mesenteroides NRRL B-1299 has a second catalytic domain ("CD2") capable of adding alpha-1,2 branching to dextrans (U.S. Patent Nos. 7439049 and 5141858; U.S. Patent Appl. Publ. No. 2009-0123448; Bozonnet et al., J. Bacteriol. 184:5753-5761, 2002). U.S. Patent Appl. Pub. No. 2010-0284972 describes methods and compositions for improving the health of a subject by administering compositions comprising alpha-1,2-branched alpha-1,6 dextrans. Sarbini et al. (Appl. Environ. Microbiol. 77:5307-5315, 2011) describes in vitro fermentation of dextran and alpha-1,2-branched dextrans by human fecal microbiota. Brison et al. (J. Biol. Chem. 287:7915-7924, 2012) describes a truncated form of the DsrE glucosyltransferase from Leuconostoc mesenteroides NRRL B-1299 (a glucan binding domain [GBD] coupled to the second catalytic domain, CD2 [i.e., GBD-CD2]) that is capable of adding alpha-1,2 branching to dextrans. Despite these reports, there remains a need to identify further enzymes that are capable of producing glucans having alpha-1,2 linkages. SUMMARY In one aspect, the present disclosure regards a reaction composition comprising at east water, sucrose, an aipha-glucan substrate, and a polypeptide that is capable of forming at least one a!pha-1,2 branch frora the alpha-glucan substrate, wherein the polypeptide comprises an ammo acid sequence tha is at least 90% identical to: (i) the mature form of a sequence selected from the group consisting of SEQ ID NOs:4, , 2, 3, 5, , 7, 8, 9, 10, 11, 12, and 13; (ii) SEQ ID NO: or a sub-sequence within any one of SEQ ID NOs:4, 2, 3, 5, 6, 7, 8, 9, 10, , 12, or 13 that aligns with SEQ ID NO:27; and/or (iii) a sequence selected from the group consisting of SEQ ID N()s:4, , 2, 3, 5, 6, 7, 8, 9, 10, 11, 12, and 13. The present disclosure also concerns a method of producing a glucan composition that comprises alpha-1,2 linkages, the method comprising: (a) providing at least the following reaction components: water, sucrose, an alpha- glucan substrate, and a polypeptide that is capable of forming at least one alpha-1,2 branch from the alpha-glucan substrate, wherein the polypeptide comprises an amino acid sequence that is at least 90% identical to: (i) the mature form of a sequence selected frora the group consisting of SEQ ID N()s:4, , 2, 3, 5, 6, 7, 8, 9, 0, , 2, and 3; ( i) SEQ ID NO:27 or a sub-sequence within any one of SEQ ID NOs:4, 2, 3, 5, 6, 7, 8, 9, 10, , 12, or 13 that aligns with SEQ ID NO:27; and/or (in) a sequence selected frora the group consisting of SEQ ID NOs:4, 1, 2, 3, 5, 6, 7, 8, 9, 10, , 12, and 13; (b) combining the reaction components under suitable conditions whereby the polypeptide catalyzes the synthesis of at least one alpha-1,2 branch frora the alpha- glucan substrate, thereby forming a glucan composition comprising alpha-1,2 linkages; and (c) optionally isolating the glucan composition comprising alpha-1,2 linkages. The present disclosure also concerns a composition that comprises a glucan composition comprising one or more alpha-1,2 linkages produced by a method or reaction as described herein, preferably wherein the composition is in the form of a food product, pharmaceutical product, personal care product, household care product, or industrial product, optionally wherein the composition comprises about 0.01 to 99 wt% (dry solids basis) of the glucan composition. The present disclosure also concerns a method comprising enterally administering a substance to a mammal, wherein the substance comprises a glucan composition comprising alpha- 1,2 linkages, wherein the administering results in less or slower blood glucose elevation in the mammal as compared to a mamma! that is enteraily administered a substance that lacks the glucan composition but instead contains a same amount of a readily digestible glucose-containing carbohydrate, wherein the glucan composition is produced by a method or reaction as described herein, optionally wherein the mammal is a human, and optionally wherein the readily digestible glucose-containing carbohydrate is sucrose, free glucose, or starch. The present disclosure also concerns a method of producing a food or beverage, the method comprising incorporating a glucan composition comprising alpha- 1,2 linkages into the food or beverage, wherein the glycemic index of the resulting food or beverage is not increased, or only marginally increased, compared to a food or beverage that lacks the glucan composition, and wherein the glucan composition is produced by a method or reaction as described herein. BRIEF DESCRIPTION OF THE BIOLOGICAL SEQUENCES The identification (gi) and accession numbers provided below are from GENEBANK (available at National Center for Biotechnology Information [NCBI] website). SEQ ID NO:l is the amino acid sequence of full length GTFJ18 (old gi: 356644413, new gi: 504090610, Acc.
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