Enzymatic in situ production of modified alpha- 1,4-glucans and products obtained, enzymes and modified alpha- 1,4-glucans

Abstract

The present disclosure relates, in part, to addition of glucosyl- or glucano-transferase type enzymes for producing and / or modifying alpha-glucan type structures in dough such as bread dough. Such enzymes encompass, for example, (i) dextrin dextranases, (ii) glucosyltransferases, and (iii) glucosyl-, maltosyl-, maltotetrasyl-, or glucano-transferases, where these enzymes can transfer glucose to / from starch and starch hydrolysate substrates (e.g., dextrin, amylodextrin, and / or maltodextrin) for production and / or modification of alpha-glucan type polymers in bread dough. Further disclosed are methods of preparing a baked food product by baking a farinaceous dough, comprising incorporating into the dough one or more of the foregoing enzymes – e.g., a glucosyl- or glucano-transferase type enzyme – wherein the enzyme can transfer a glucose-based moiety from a polysaccharide or oligosaccharide substrate to the non-reducing end of an oligosaccharide acceptor, thereby improving bread volume and / or dough stability. Further disclosed are modified alpha-glucans for use as food ingredients in general.

Description

[0001] TITLE ALPHA-GLUCAN, AND PRODUCTION THEREOF, FOR IMPROVED FOOD INGREDIENTS AND FOOD PRODUCTS This application claims the benefit of International Application Nos. PCT / CN2024 / 113940 (filed August 22, 2024) and PCT / CN2025 / 099358 (filed June 5, 2025), both of which prior applications are incorporated herein by reference in their entirety. FIELD The present disclosure is in the field of enzymes, food products and grain processing. For example, the disclosure pertains to food products and food dough comprising flour and alpha-glucan, and methods of producing these food products. REFERENCE TO SEQUENCE LISTING SUBMITTED ELECTRONICALLY The official copy of the sequence listing is submitted electronically via EFS-Web as a file named IFF10096WOPCT3_SequenceListing.xml created on August 20, 2025 and having a size of about 307 kilobytes, and is filed concurrently with the specification. The sequence listing contained in this file is part of the specification and is incorporated herein by reference in its entirety. BACKGROUND Several additives may be used in bread baking to improve the texture of bakery products. These include chemicals, sugars, enzymes, or combinations of these. Well-known additives include: milk powder, gluten, emulsifiers (mono- or di-glycerides, sugar esters, lecithin, etc.), granulated fat, oxidants (ascorbic acid or potassium bromate), cysteine, sugars and salts. Advances in biotechnology now offer additional enzymes to the baking industry. Since enzymes are produced from natural ingredients, these catalysts will find greater acceptance by consumers because of demand for products without chemicals. Some families of enzymes have been shown to act as dough and / or bread improvers in situ, by being able to modify one or more major dough components. For instance, enzymes active on starch (e.g., alpha-amylase, branching and debranching enzyme, maltogenic amylase, beta-amylase, amyloglucosidase) have been shown to act as anti-staling agents. Despite this progress, additional enzyme solutions are sought after for improving dough-based food products. Addressing this and other needs, novel glucosyl- and glucano-transferase type enzymes are disclosed herein to be useful for improving bread volume and dough stability by effecting in situ production and / or modification of alpha-glucan through activity on starch, dextrin and other alpha-1,4-glucan substrates during dough preparation. SUMMARY In one embodiment, the present disclosure concerns a method of producing a food dough, wherein the method comprises: mixing at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6- alpha-glucanotransferase, thereby producing a food dough, optionally wherein: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks the enzyme, (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks the enzyme, and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks the enzyme. In another embodiment, the present disclosure concerns a food dough or food product produced by a method herein. In another embodiment, the present disclosure concerns a food dough comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, optionally wherein: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks the enzyme, (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks the enzyme, and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks the enzyme. In another embodiment, the present disclosure concerns a food product comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, optionally wherein the food product has a water-binding capacity that is increased as compared to the water-binding capacity of a control food product that lacks the enzyme. In another embodiment, the present disclosure concerns an enzyme selected from a dextrin dextranase or a 4,6-alpha-glucanotransferase, wherein the enzyme comprises an amino acid sequence that is at least about 90% identical to SEQ ID NO:1 (optionally to SEQ ID NO:28), 2 (optionally to SEQ ID NO:29), 3 (optionally to SEQ ID NO:30), 4 (optionally to SEQ ID NO:31), 5 (optionally to SEQ ID NO:32), 6 (optionally to SEQ ID NO:33), 7 (optionally to SEQ ID NO:34), 8 (optionally to SEQ ID NO:35), 9 (optionally to SEQ ID NO:36), 10 (optionally to SEQ ID NO:37), 11 (optionally to SEQ ID NO:38), 12 (optionally to SEQ ID NO:39), 13 (optionally to SEQ ID NO:40), 14 (optionally to SEQ ID NO:41), 15 (optionally to SEQ ID NO:42), 16 (optionally to SEQ ID NO:43), 17 (optionally to SEQ ID NO:44), 18 (optionally to SEQ ID NO:45), 19 (optionally to SEQ ID NO:46), 20 (optionally to SEQ ID NO:47), 21 (optionally to SEQ ID NO:48), 22 (optionally to SEQ ID NO:49), 23 (optionally to SEQ ID NO:50), 24 (optionally to SEQ ID NO:51), 25 (optionally to SEQ ID NO:52), 26 (optionally to SEQ ID NO:53), 27 (optionally to SEQ ID NO:54), 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148. In another embodiment, the present disclosure concerns a modified 4,6-alpha- glucanotransferase enzyme, wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22 (or at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23, or at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83, 84, or 85), wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% identical to SEQ ID NO:22 (or SEQ ID NO:23, 83, 84, or 85), optionally wherein the modified 4,6-alpha-glucanotransferase enzyme can produce a modified alpha-glucan at a yield that is higher than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. In another embodiment, the present disclosure concerns a polynucleotide comprising a nucleotide sequence encoding an enzyme herein, optionally wherein one or more regulatory sequences are operably linked to the nucleotide sequence, and preferably wherein the one or more regulatory sequences include a promoter sequence. In another embodiment, the present disclosure concerns a food ingredient comprising a modified alpha-glucan, or a food product comprising the food ingredient, wherein the modified alpha-glucan is produced by providing a composition comprising at least (i) water, (ii) an alpha-1,4-glucan substrate, and (iii) an enzyme herein selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase. BRIEF DESCRIPTION OF THE SEQUENCES Table 1. Summary of Protein and Nucleic Acid SEQ ID Numbers BRIEF DESCRIPTION OF THE DRAWINGS FIG.1 depicts HPLC-42A chromatograms of maltoheptaose (DP7) incubated without enzyme (labeled as substrate only) for different incubation durations on the left, and chromatograms of substrate treated with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.2 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:1 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:1 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.3 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:2 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:2 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.4 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:3 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:3 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.5 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:4 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:4 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.6 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:5 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:5 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.7 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:6 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:6 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.8 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:7 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:7 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.9 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:8 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:8 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.10 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:9 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:9 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.11 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:10 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:10 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.12 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:11 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:11 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.13 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:12 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:12 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.14 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:13 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:13 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.15 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:14 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:14 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.16 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:15 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:15 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.17 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:16 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:16 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.18 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:17 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:17 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.19 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:18 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:18 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.20 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:19 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:19 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.21 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:20 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:20 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.22 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:21 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:21 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.23 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:22 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:22 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.24 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:23 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:23 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.25 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:24 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:24 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.26 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:25 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:25 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.27 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:26 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:26 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.28 depicts HPLC-42A chromatograms of maltoheptaose (DP7) reacted with the enzyme of SEQ ID NO:27 for different incubation durations on the left, and chromatograms of the products of SEQ ID NO:27 and DP7 after treatment with three different types of alpha- glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.29 depicts an HPLC-42A chromatogram of amylose incubated without enzyme (labeled as substrate only) for 24 hours on the left, and chromatograms of substrate treated for 24 hours with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.30 depicts HPLC-42A chromatograms of amylose only (no enzyme) or amylose incubated with the enzyme of SEQ ID NO:2 for 24 hours on the left, and the chromatograms of the products of SEQ ID NO:2 and amylose after treatment with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.31 depicts HPLC-42A chromatograms of amylose only (no enzyme) or amylose incubated with the enzyme of SEQ ID NO:14 for 24 hours on the left, and the chromatograms of the products of SEQ ID NO:14 and amylose after treatment with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.32 depicts HPLC-42A chromatograms of amylose only (no enzyme) or amylose incubated with the enzyme of SEQ ID NO:22 for 24 hours on the left, and the chromatograms of the products of SEQ ID NO:22 and amylose after treatment with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.33 depicts HPLC-42A chromatograms of amylose only (no enzyme) or amylose incubated with the enzyme of SEQ ID NO:26 for 24 hours on the left, and the chromatograms of the products of SEQ ID NO:26 and amylose after treatment with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.34 depicts HPLC-42A chromatograms of amylose only (no enzyme) or amylose incubated with the enzyme of SEQ ID NO:27 for 24 hours on the left, and the chromatograms of the products of SEQ ID NO:27 and amylose after treatment with three different types of alpha-glucan hydrolyzing enzymes on the right, using water as the mobile phase and RI detection. FIG.35 depicts flour slurry viscosity (cP) as determined by Gilson Viscoman of a 30% flour slurry containing acetate buffer pH 5.2 at 30 °C with various amounts of starch- acting GTF-C enzyme (LEI2176, SEQ ID NO:27) as described in legends and analyzed over 160 minutes. FIG.36 depicts specific volume of unshocked (dark gray) and shocked (light gray) breads (4 unshocked rolls and 4 shocked rolls) determined three times based on the dough weight A) and bread weight B) using Enovera 3001 with addition of starch-acting GTF-like enzymes. Enovera 3001 was tested alone without starch-acting GTF-like enzymes and together with the following individually: 0.55% GH31 (CRC31440, SEQ ID NO:12), 0.27% GtfB (CRC31302, SEQ ID NO:14) and 0.27% GtfD (CRC29205, SEQ ID NO:22) given as % of amount flour (Bakers percentage). FIG.37 depicts representative1H-spectra of sample 5_AMY_2h_Liq_1ml showing assignment of H-1 peaks with different linkage types as marked in the figure (alpha-1,6, alpha-1,3, alpha-1,4 and alpha-1,2). FIG.38 depicts Brabender farinograph dough analysis (Brabender ICC_BIPEA_50) with 50 g Reform Wheat flour (Valsemøllen, Esbjerg Denmark, 12.5% protein) at 30 ^C including as indicated, Blank 1 and 2 (no ingredient addition), DATEM diacetyl tartaric acid ester of mono- / di-glycerides (PANODAN® A2020 supplied by IFF Brabrand Denmark), PowerFRESH 8100 (G4- forming amylase product by IFF, Denmark) and purified starch- acting GTF-like enzyme samples: DDase CRC29225v1 (SEQ ID NO:1), GTF-C CRC28250 (SEQ ID NO:26), and DDase CRC29218 (SEQ ID NO:2) were added at 0.32%, 0.36%, 0.27% and 0.5% respectively, of the flour (Bakers percentage). FIG.39 depicts specific volume of unshocked (dark gray) and shocked (light gray) breads (4 unshocked rolls and 4 shocked rolls) determined three times based on the dough weight using Enovera 3001 with addition of starch-acting GTF-like enzymes. Enovera 3001 was tested alone without starch-acting GTF-like enzymes and together with the following individually: 0.14%, 0.29% and 0.58% DDase (CRC29225-00001, SEQ ID NO:1), 0.3% DDase (CRC29234-WT, SEQ ID NO:6), 0.47% DDase (CRC29233-WT, SEQ ID NO:5) and 1.24% GtfC (CRC28250-WT, SEQ ID NO:26) given as % of amount flour (Bakers percentage). FIG.40 depicts specific volume of unshocked (dark gray) and shocked (light gray) breads (4 unshocked rolls and 4 shocked rolls) determined three times based on the final bread weight using Enovera 3001 with addition of starch-acting GTF-like enzymes. Enovera 3001 was tested alone without starch-acting GTF-like enzymes and together with the following individually: 0.14%, 0.29% and 0.58% DDase (CRC29225-v1, SEQ ID NO:1), 0.3% DDase (CRC29234-WT, SEQ ID NO:6), 0.47% DDase (CRC29233-WT, SEQ ID NO:5) and 1.24% GTF-C (CRC28250-WT, SEQ ID NO:26) given as % of amount flour (Bakers percentage). FIG.41 depicts specific volume of unshocked (dark gray) and shocked (light gray) breads (4 unshocked rolls and 4 shocked rolls) determined three times based on the dough weight (top) and bread weight (bottom) using Enovera 3001 with addition of the starch-acting GTF-like enzyme DDase (CRC29218, SEQ ID NO:2). Enovera 3001 was tested alone without starch-acting GTF-like enzymes and together with 1.33% DDase (CRC29218, SEQ ID NO:2) given as % of amount flour (Bakers percentage). FIG.42 depicts HPLC-SB806M analyses of products produced by GtfD CRC29205- WT (SEQ ID NO:22) and its variant, CRC29205-00002 (SEQ ID NO:86), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using water as the mobile phase and RI detection. FIG.43 depicts HPLC-SB806M analyses of products produced by GtfD CRC29211- WT (SEQ ID NO:82) and its variant, CRC29211-00001 (SEQ ID NO:88), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (0.5 mL / min) and RI detection. FIG.44 depicts HPLC-SB806M analyses of products produced by GtfD CRC29210- WT (SEQ ID NO:23) and its variant, CRC29210-00001 (SEQ ID NO:87), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (0.5 mL / min) and RI detection. Relative to SEQ ID NO:23, SEQ ID NO:87 has a Q543I substitution. FIG.45 depicts HPLC-SB806M analyses of products produced by GtfD CRC34732- WT (SEQ ID NO:83) and its variant, CRC34732-00001 (SEQ ID NO:89), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (0.5 mL / min) and RI detection. Relative to SEQ ID NO:83, SEQ ID NO:89 has a Q487I substitution. FIG.46 depicts HPLC-SB806M analyses of products produced by GtfD CRC34742- WT (SEQ ID NO:84) and its variant, CRC34742-00001 (SEQ ID NO:90), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (0.5 mL / min) and RI detection. Relative to SEQ ID NO:84, SEQ ID NO:90 has a Q487I substitution. FIG.47 depicts HPLC-SB806M analyses of products produced by GtfD CRC34743- WT (SEQ ID NO:85) and its variant, CRC34743-00001 (SEQ ID NO:91), individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (0.5 mL / min) and RI detection. Relative to SEQ ID NO:85, SEQ ID NO:91 has a Q487I substitution. FIG.48 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00002 (SEQ ID NO:86), CRC29205-00006 (SEQ ID NO:92), CRC29205-00007 (SEQ ID NO:93) and CRC29205-WT (SEQ ID NO:22) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. Relative to SEQ ID NO:22, SEQ ID NO:86 has a Q487I substitution. FIG.49 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00008 (SEQ ID NO:94), CRC29205-00009 (SEQ ID NO:95), CRC29205-00010 (SEQ ID NO:96) and CRC29205-00011 (SEQ ID NO:97) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.50 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00012 (SEQ ID NO:98), CRC29205-00013 (SEQ ID NO:99), CRC29205-00014 (SEQ ID NO:100) and CRC29205-00015 (SEQ ID NO:101) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.51 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00016 (SEQ ID NO:102), CRC29205-00017 (SEQ ID NO:103) and CRC29205- 00018 (SEQ ID NO:104) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.52 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00019 (SEQ ID NO:105) and CRC29205-00020 (SEQ ID NO:106) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.53 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00021 (SEQ ID NO:107), CRC29205-00022 (SEQ ID NO:108) and CRC29205- 00023 (SEQ ID NO:109) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.54 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00024 (SEQ ID NO:110), CRC29205-00025 (SEQ ID NO:111) and CRC29205- 00026 (SEQ ID NO:112) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.55 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00027 (SEQ ID NO:113), CRC29205-00028 (SEQ ID NO:114) and CRC29205- 00029 (SEQ ID NO:115) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.56 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00030 (SEQ ID NO:116), CRC29205-00031 (SEQ ID NO:117) and CRC29205- 00032 (SEQ ID NO:118) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.57 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00033 (SEQ ID NO:119), CRC29205-00034 (SEQ ID NO:120) and CRC29205- 00035 (SEQ ID NO:121) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.58 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00036 (SEQ ID NO:122), CRC29205-00037 (SEQ ID NO:123) and CRC29205- 00038 (SEQ ID NO:124) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.59 depicts HPLC-SB803 analyses of products produced by GtfD enzymes CRC29205-00039 (SEQ ID NO:125), CRC29205-00040 (SEQ ID NO:126) and CRC29205- 00041 (SEQ ID NO:127) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.60 depicts HPLC-SB803 analyses of products produced by DDase CRC29233 (SEQ ID NO:32) and its variants, CRC29233-v2 (SEQ ID NO:146) and CRC29233-v3 (SEQ ID NO:128) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.61 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v4 (SEQ ID NO:129), CRC29233-v7 (SEQ ID NO:130) and CRC29233-v9 (SEQ ID NO:131) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.62 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v10 (SEQ ID NO:132), CRC29233-v11 (SEQ ID NO:133) and CRC29233-v17 (SEQ ID NO:134) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.63 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v18 (SEQ ID NO:135), CRC29233-v19 (SEQ ID NO:136) and CRC29233-v20 (SEQ ID NO:137) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.64 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v21 (SEQ ID NO:138), CRC29233-v22 (SEQ ID NO:139) and CRC29233-v23 (SEQ ID NO:140) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.65 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v24 (SEQ ID NO:147), CRC29233-v25 (SEQ ID NO:148) and CRC29233-v26 (SEQ ID NO:141) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. FIG.66 depicts HPLC-SB803 analyses of products produced by DDase CRC29233- v27 (SEQ ID NO:142), CRC29233-v28 (SEQ ID NO:143), CRC29233-v30 (SEQ ID NO:144) and CRC29233-v31 (SEQ ID NO:145) individually acting on 6.5% (w / v) maltodextrin (DE4-7) as substrate, using 10 mM NaCl as the mobile phase (1 mL / min) and RI detection. DETAILED DESCRIPTION The present disclosure regards, for example, dough preparation methods using starch- acting glucanotransferase type enzymes for converting dextrin and damaged starch, for example, of flour into various alpha-glucan type structures in bread dough. This process encompasses generation of alpha-glucan compounds with various glycosidic linkages such as alpha-1,6, alpha-1,3 and / or alpha-1,2. Alpha-glucans herein can be generated enzymatically using different glucanotransferase type enzymes such as dextrin dextranase, glucosyltransferase, or glucosyl-, maltosyl-, or maltotetrasyl-glucanotransferase. The present disclosure also regards exogenous starch-acting glucanotransferase type enzymes that can modify bread volume, viscosity of flour slurries, and dough stability. Damaged starch is a parameter for assessing the quality of flour used in breads, cookies and other baked products. It refers to the portion of kernel starch that has been physically broken or fragmented during wheat milling. The amount of damaged starch in flour is a function of kernel hardness and milling intensity. Furthermore, in milling wheat flour, starch granules contained in the wheat flour are crushed, resulting in production of damaged starch and a decrease in gluten activity. This results in significant loss of workability and texture during the production of the yeast- fermented food. The content of damaged starch as percent of total starch in soft wheat flour and hard wheat flour (HRS and HRW) is, respectively, about 1-4% and 6-12%. Damaged starch can absorb more water, but it does not retain it well. Damaged starch is very hygroscopic and absorbs water quickly. However, during the mixing phase, the granules tend to release that water again. Thus, if water continues to escape from the damaged starch granules once the protein is fully hydrated, it will separate from the dough and cause stickiness. In another aspect of the present disclosure, a method of preparing a baked product is presented in which a dough as described herein is baked. In another aspect, a baked product is presented. Optionally, a baked product herein has at least one improved property such as improved crumb pore size, improved uniformity of gas bubbles, no separation between crust and crumb, increased volume, increased shock stability, increased crust crispiness and improved oven spring. Optionally, the improved property is increased crust crispiness. Optionally, an improved property herein is improved when compared to a baked product prepared from a dough that does not comprise a glucosyl- or glucanotransferase type enzyme of the present disclosure, but typically is otherwise of the same composition (e.g., same ingredients, except for one or more of the foregoing enzymes). In another aspect, a baked product is provided that comprises an enzyme as described herein, or that is prepared from a dough that comprises an enzyme as described herein. In another aspect of the present disclosure, in situ production of alpha-glucan during dough preparation and / or modification of damaged starch increases the specific %-mol. content of alpha-1,6-, alpha-1,3-, and / or alpha-1,2-linkages of the modified alpha-glucan and / or modified starch as compared to what is observed in dough prepared in a manner without in situ enzyme treatment. The disclosures of all cited patent and non-patent literature are incorporated herein by reference in their entirety. Unless otherwise disclosed, the terms “a”, “an” and “the” as used herein are intended to encompass one or more (i.e., at least one) of a referenced feature. Where present, all ranges are inclusive and combinable, except as otherwise noted. For example, when a range of “1 to 5” (i.e., 1-5) is recited, the recited range should be construed as including ranges “1 to 4”, “1 to 3”, “1-2”, “1-2 & 4-5”, “1-3 & 5”, and the like. The numerical values of the various ranges in the present disclosure, unless expressly indicated otherwise, are stated as approximations as though the minimum and maximum values within the stated ranges were both proceeded by the word “about”. In this manner, slight variations above and below the stated ranges can typically be used to achieve substantially the same results as values within the ranges. Also, the disclosure of these ranges is intended as a continuous range including each and every value between the minimum and maximum values. It is intended that every maximum numerical limitation given throughout this specification includes every lower numerical limitation, as if such lower numerical limitations were expressly written herein. Every minimum numerical limitation given throughout this specification will include every higher numerical limitation, as if such higher numerical limitations were expressly written herein. Every numerical range given throughout this specification will include every narrower numerical range that falls within such broader numerical range, as if such narrower numerical ranges were all expressly written herein. It is to be appreciated that certain features of the present disclosure, which are, for clarity, described above and below in the context of aspects / embodiments, may also be provided in combination in a single element. Conversely, various features of the disclosure that are, for brevity, described in the context of a single aspect / embodiment, can also be provided separately or in any sub-combination. A “glucan” herein is a type of polysaccharide that is a polymer of glucose (polyglucose). A glucan can be comprised of, for example, about, or at least about, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% by weight glucose monomeric units. Examples of glucans herein are alpha-glucan and beta-glucan. The terms “alpha-glucan”, “alpha-glucan polymer” and the like are used interchangeably herein. An alpha-glucan is a polymer comprising glucose monomeric units linked together by alpha-glycosidic linkages. In typical embodiments, an alpha-glucan herein comprises at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% alpha-glycosidic linkages. Examples of alpha-glucan polymers herein include alpha-1,4-glucan and alpha-1,4-glucan that further comprises alpha-1,6, alpha-1,3, and / or alpha-1,2 glycosidic linkages. The term “saccharide” and other like terms herein refer to monosaccharides and / or disaccharides / oligosaccharides, unless otherwise noted. A “disaccharide” herein refers to a carbohydrate having two monosaccharides joined by a glycosidic linkage. An “oligosaccharide” herein can refer to a carbohydrate having 3 to 15 monosaccharides, for example, joined by glycosidic linkages; an example is a gluco-oligosaccharide which is comprised of glucose residues. An oligosaccharide can also be referred to as an “oligomer” (e.g., gluco-oligomer). Monosaccharides (e.g., glucose and / or fructose) comprised within disaccharides / oligosaccharides can be referred to as “monomeric units”, “monosaccharide units”, or other like terms. The terms “sugar” or “sugars”, unless used to specifically refer to sucrose only, typically refer to any monosaccharide (e.g., fructose, glucose, and / or galactose) and / or disaccharide (e.g., sucrose, leucrose, and / or lactose; and / or optionally DP2 gluco- oligosaccharide). Sugars herein typically are water-soluble. The terms “alpha-1,4-glucan”, “poly alpha-1,4-glucan”, “alpha-1,4-glucan polymer” and the like are used interchangeably herein. Alpha-1,4-glucan is an alpha-glucan comprising glucose monomeric units linked together by glycosidic linkages, wherein at least about 50% of the glycosidic linkages are alpha-1,4. Other linkages (if present, and in some aspects, as present following enzymatic treatment herein) in alpha-1,4-glucan herein typically are alpha-1,6, alpha-1,2 and / or alpha-1,3. Examples of alpha-1,4-glucan herein include starch, which itself typically comprises at least amylose and amylopectin. Amylose typically comprises linear alpha-1,4-glucan (i.e., ~100% alpha-1,4 linkages), whereas amylopectin is a branched polymer comprising alpha-1,4-glucan iteratively branched from alpha-1,4-glucan via alpha-1,6 branch points (i.e., alpha-1,4-1,6-glucan). The term “modified alpha-glucan” herein typically refers to alpha-glucan that has been modified, or newly synthesized, by an enzyme in a dough production method of the disclosure. Examples of modified alpha-glucan include modified alpha-1,4-glucan (e.g., modified starch, modified dextrin, modified amylodextrin, and / or modified maltodextrin) and modified gluco-oligosaccharides (GlcOS). Except as noted otherwise, modified alpha-glucan herein encompasses all of the modified alpha-glucans (pre-existing alpha-glucan that has now been enzymatically altered to have a different molecular weight and / or linkage profile, for example) and / or newly synthesized alpha-glucans of an enzyme-treated food dough herein. The percent branching in an alpha-glucan herein refers to that percentage of all the linkages in the alpha-glucan that represent branch points. For example, the percent of alpha- 1,6 branching in an alpha-glucan herein refers to that percentage of all the linkages in the glucan that represent alpha-1,6 branch points. Except as otherwise noted, linkage percentages disclosed herein are based on the total linkages of a glucan, or the portion of a glucan for which a disclosure specifically regards. The terms “linkage”, “glycosidic linkage”, “glycosidic bond” and the like refer to the covalent bonds connecting the sugar monomers within a saccharide compound (oligosaccharides and / or polysaccharides). Examples of glycosidic linkages include 1,6- alpha-D-glycosidic linkages (herein also referred to as “alpha-1,6” linkages), 1,3-alpha-D- glycosidic linkages (herein also referred to as “alpha-1,3” linkages), 1,4-alpha-D-glycosidic linkages (herein also referred to as “alpha-1,4” linkages), and 1,2-alpha-D-glycosidic linkages (herein also referred to as “alpha-1,2” linkages). The glycosidic linkages of a glucan polymer herein can also be referred to as “glucosidic linkages”. Herein, “alpha-D-glucose” is referred to as “glucose”. The glycosidic linkage profile of an alpha-glucan herein can be determined using any method known in the art. For example, a linkage profile can be determined using methods using nuclear magnetic resonance (NMR) spectroscopy (e.g.,13C NMR or1H NMR). These and other methods that can be used are disclosed in, for example, Food Carbohydrates: Chemistry, Physical Properties, and Applications (S. W. Cui, Ed., Chapter 3, S. W. Cui, Structural Analysis of Polysaccharides, Taylor & Francis Group LLC, Boca Raton, FL, 2005), which is incorporated herein by reference. The “molecular weight” of an alpha-glucan herein can be represented as weight- average molecular weight (Mw) or number-average molecular weight (Mn), the units of which are in Daltons (Da) or grams / mole. In some aspects, molecular weight can be represented as DPw (weight average degree of polymerization) or DPn (number average degree of polymerization). DPw and DPn are calculated from the corresponding Mw or Mn, respectively, by dividing by the molar mass of one monomer unit M1. In the case of glucan polymer, M1= 162.14. In some aspects, molecular weight can sometimes be provided as “DP” (degree of polymerization), which simply refers to the number of glucoses comprised within the alpha-glucan on an individual molecule basis. Various means are known in the art for calculating these various molecular weight measurements such as with high-pressure liquid chromatography (HPLC), size exclusion chromatography (SEC), or gel permeation chromatography (GPC). The terms “dextrin dextranase” (DDase), “dextrin dextranase enzyme” and the like are used interchangeably herein. The activity of a DDase typically is of EC (Enzyme Commission) no.2.4.1.2. In general, a DDase catalyzes the transfer of a non-reducing end glucosyl residue of an alpha-1,4-linked donor substrate (e.g., an alpha-1,4-glucan herein such as starch, dextrin, amylodextrin, or maltodextrin) to a non-reducing end of a growing alpha- 1,6-glucan acceptor molecule. The terms “4,6-alpha-glucanotransferase” (4,6-alpha-GT), “4,6-alpha- glucanotransferase enzyme” and the like are used interchangeably herein. The activity of a 4,6-alpha-GT typically is of EC no. EC 2.4.1.-. In general, a 4,6-alpha-GT can use alpha-1,4- glucan herein (e.g., starch, dextrin, amylodextrin, and / or MOS) as a glucose source to perform alpha-1,6 transglucosylation to produce an alpha-glucan product with at least one additional alpha-1,6 linkage (as compared to pre-transglucosylation). In some aspects, a 4,6- alpha-GT can produce a linear alpha-glucan product with high amount of alpha-1,6 linkages (e.g., >80% or >90% alpha-1,6 linkages). In some other aspects, a 4,6-alpha-GT can produce a branched alpha-glucan, where the product typically has a lower amount of alpha-1,6 linkages (e.g., <50%, <40%, or <30% alpha-1,6 linkages). A 4,6-alpha-GT can also, in some aspects, introduce alpha-1,3 linkages to alpha-glucan products. Although 4,6-alpha-GT enzymes belong to the glycoside hydrolase family 70 (GH70), they do not employ sucrose as a substrate. GtfB, GtfC, and GtfD glucanotransferases are examples of 4,6-alpha-GT enzymes herein. The terms “GtfB enzyme” “GtfB-type alpha-glucosyltransferase”, “GtfB 4,6-alpha- glucanotransferase” and the like are used interchangeably herein. A GtfB enzyme can transfer a non-reducing end glucose from alpha-1,4-glucan herein to the non-reducing end of an acceptor such as MOS via an alpha-1,6 linkage to produce linear malto- / isomalto- oligosaccharide product (e.g., alpha-glucan with a span of one or more alpha-1,6-linked glucose units linked to a span of one or more alpha-1,4-linked glucose units). A GtfB in some aspects can also modify products to have one or more alpha-1,3 linkages. The terms “GtfC enzyme” “GtfC-type alpha-glucosyltransferase”, “GtfC 4,6-alpha- glucanotransferase” and the like are used interchangeably herein. A GtfC enzyme can transfer non-reducing end glucose units from alpha-1,4-glucan herein (e.g., amylose) to the non-reducing end of an acceptor such as MOS to produce linear alpha-glucan product having a span of alternating alpha-1,6 and alpha-1,4 linkages (e.g., where this span is linked to a span of one or more consecutive alpha-1,4-linked glucose units). The terms “GtfD enzyme” “GtfD-type alpha-glucosyltransferase”, “GtfD 4,6-alpha- glucanotransferase” and the like are used interchangeably herein. A GtfD enzyme can transfer non-reducing end glucose units from alpha-1,4-glucan herein (e.g., amylose) to the non-reducing end of an acceptor such as MOS to produce branched alpha-glucan product having one or more spans of alternating alpha-1,6 and alpha-1,4 linkages (e.g., where such a span in at least one instance is linked to a span of one or more consecutive alpha-1,4-linked glucose units). A GtfD in some aspects can also modify products to have one or more alpha- 1,3 linkages. The term “in situ” as used herein characterizes an enzyme reaction(s) that occurs inside a food dough or precursor thereof (e.g., incompletely mixed dough) and thereby produces an enzymatic product within the food dough itself (or precursor). Typically, an enzyme used for an in situ reaction herein is added to the food dough or precursor thereof as an exogenous ingredient, for example as a purified or otherwise isolated enzyme. Enzymatic product(s) produced in situ in a food dough or precursor thereof typically persist through downstream food dough / precursor processing (e.g., baking), and thus can exist in a food product made using the enzymatically treated food dough / precursor. The terms “percent by volume”, “volume percent”, “vol %”, “v / v %” and the like are used interchangeably herein. The percent by volume of a solute in a solution can be determined using the formula: [(volume of solute) / (volume of solution)] x 100%. The terms “percent by weight”, “weight percentage (wt%)”, “weight-weight percentage (% w / w)” and the like are used interchangeably herein. Percent by weight refers to the percentage of a material on a mass basis as it is comprised in a composition, mixture, or solution. The terms “weight / volume percent”, “w / v%” and the like are used interchangeably herein. Weight / volume percent can be calculated as: ((mass [g] of material) / (total volume [mL] of the material plus the liquid in which the material is placed)) x 100%. The material can be insoluble in the liquid (i.e., be a solid phase in a liquid phase, such as with a dispersion), or soluble in the liquid (i.e., be a solute dissolved in the liquid). The terms “ingestible product” and “ingestible composition” are used interchangeably herein, and refer to any substance that, either alone or together with another substance, may be taken orally (i.e., by mouth), whether intended for consumption or not. Thus, an ingestible product includes food / beverage products. “Food / beverage products” refer to any edible product intended for consumption (e.g., for nutritional purposes) by humans or animals, including solids, semi-solids, or liquids. A “food” herein can optionally be referred to as a “foodstuff”, “food product”, or other like term, for example. Herein, unless otherwise disclosed, a beverage or other ingestible liquid is an example of a food product. While the present disclosure generally regards food and food precursors that are by definition intended for ingestion or eventual ingestion (food precursor first made into food before being eaten), the disclosure likewise regards other ingestible products (e.g., supplement, nutraceutical, pharmaceutical product) comprising in situ-produced enzymatic product herein. A food precursor herein can be (i) a food as it exists before one or more processing steps (e.g., fermentation, aging, cooling / freezing, heating, baking, mixing) that render it to be a food product intended for direct consumption, and / or (ii) an ingredient for use in preparing a food product, for example. In some aspects, a food precursor can characterize a food product or ingredient as it exists before treatment with one or more enzymes in a method herein. “Flour” and like terms herein refer to powder made by grinding (milling) grains / cereals, roots / tubers, beans / legumes, or nuts / seeds, for example. Typically, the material that is ground into flour is entered into the grinding process in raw, dried form. A flour herein that is made from grain can optionally be referred to as a “grain flour”. “Meal” and other like terms herein refer to a substance that is similar to flour, but with a grain or particle size that is larger / coarser. A meal is not ground / milled as finely as flour. A meal herein that is made from grain can optionally be referred to as a “grain meal”. Flour and meal are generally used as ingredients in various food products. Flour and meal produced from a grain can optionally be characterized as grain derivatives herein. “Dough”, “food dough” and like terms herein typically refer to a mixture comprising at least (i) flour and / or meal and (ii) a water-comprising liquid (e.g., water and / or milk), and typically is in a suitable form (stiff / firm) for kneading or rolling. A dough can optionally be referred to with reference to the grain, grain derivative, or other material from which it was derived (e.g., wheat dough, wheat flour dough, corn flour dough, cornmeal dough). Since dough typically is not eaten as a food prior to further processing (e.g., baking), dough can optionally be characterized as a “food precursor”. A “baked food” (and like terms) herein refers to a food that has been baked during its preparation. Baking herein typically refers to a process of applying dry heat to a food / food precursor (e.g., dough) for a period of time during preparation of the food. In general, baking is conducted in an enclosed (typically confined) space such as within an oven. Bread is an example of a food for which its preparation process typically comprises baking. An “extruded food” (and like terms) herein refers to a food that has been extruded during its preparation. Food extrusion is a process by which a mix of ingredients (e.g., dough) is forced through an opening in a perforated device (e.g., plate or die), which typically is specifically designed for the food being extruded. After this step, an extruded food typically is then cut to a particular size. The terms “dietary fiber”, “glucan fiber” and the like herein refer to an alpha-glucan that is indigestible and / or that does not increase blood-glucose levels when enterally administered to a mammal. In general, a dietary fiber herein is not significantly hydrolyzed by endogenous enzymes in the upper gastrointestinal tract of mammals such as humans. Isomalto-oligosaccharides (IMOs) are generally characterized as being a form of dietary fiber. “Gluten” herein refers to a group of proteins, termed prolamins and glutelins, which occur with starch in the endosperm of cereal grains. Gluten has been previously described by Wieser (2007, Food Microbiol.200724:115-119), for example, which is incorporated herein by reference. The term “starch” herein refers to a material, derived from plants, typically comprising (i) amylose and amylopectin, or (ii) mostly amylopectin. For instance, starch can contain (i) about 20 to 25 wt% amylose and about 75 to 80 wt% amylopectin, or (ii) over about 99 wt% (e.g., ≥ ~99.5 or ~99.9 wt%) amylopectin or about 100 wt% amylopectin. Starch typically can be prepared from a plant source such as grains, cereal, grasses, or tubers / roots, and in some aspects from wheat, barley, corn, rye, rice, sorghum, bran, cassava, millet, milo, potato, sweet potato, or tapioca. The term “starch” can include granular starch, which refers to raw (i.e., uncooked) starch (e.g., starch that has not been subject to gelatinization). Starch in some aspects can be from a waxy crop (waxy grain) such as waxy corn, which starch typically is comprised mostly of amylopectin (as above). “Fermentation” and like terms herein as applied to food product / precursor refer to the conversion of carbohydrates in a food product / precursor into alcohol(s) and / or acid(s) through the action of one or more microorganisms (e.g., bacteria, yeast). A composition herein that is “dry” or “dried” typically has less than 5, 4, 3, 2, 1, 0.5, or 0.1 wt% water comprised therein. The terms “aqueous liquid”, “aqueous fluid”, “aqueous conditions”, “aqueous setting”, “aqueous system” and the like as used herein can refer to water or an aqueous solution. An “aqueous solution” herein can comprise one or more dissolved salts, where the maximal total salt concentration can be about 3.5 wt% in some embodiments. Although aqueous liquids herein typically comprise water as the only solvent in the liquid, an aqueous liquid can optionally comprise one or more other solvents (e.g., polar organic solvent) that are miscible in water. Thus, an aqueous solution can comprise a solvent having at least about 10 wt% water. An “aqueous composition” herein has a liquid component that comprises about, or at least about, 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, 99, or 100 wt% water, for example. Examples of aqueous compositions include mixtures, solutions, dispersions (e.g., suspensions, colloidal dispersions) and emulsions, for example. An alpha-glucan herein that is “insoluble”, “aqueous-insoluble”, “water-insoluble” (and like terms) herein does not dissolve (or does not appreciably dissolve) in water or other aqueous conditions, optionally where the aqueous conditions are at a pH of 4-9 (e.g., pH 6-8) and / or a temperature of about 1 to 130 °C (e.g., 20-25 °C). In some aspects, less than 1.0 gram (e.g., no detectable amount) of an aqueous-insoluble alpha-glucan dissolves in 1000 milliliters of such aqueous conditions (e.g., water at 23 °C). In contrast, an alpha-glucan that is “soluble”, “aqueous-soluble”, “water-soluble” and the like appreciably dissolves under the above aqueous conditions. As used herein, the term “polypeptide” is defined as a chain of amino acid residues, usually having a defined sequence. As used herein the term polypeptide is interchangeable with the terms “peptides” and “proteins”. Typical amino acids contained in polypeptides herein include (respective three- and one-letter codes shown parenthetically): alanine (Ala, A), arginine (Arg, R), asparagine (Asn, N), aspartic acid (Asp, D), cysteine (Cys, C), glutamic acid (Glu, E), glutamine (Gln, Q), glycine (Gly, G), histidine (His, H), isoleucine (Ile, I), leucine (Leu, L), lysine (Lys, K), methionine (Met, M), phenylalanine (Phe, F), proline (Pro, P), serine (Ser, S), threonine (Thr, T), tryptophan (Trp, W), tyrosine (Tyr, Y), valine (Val, V). The terms “sequence identity”, “identity” and the like as used herein with respect to polypeptide sequences refer to amino acid residues in two sequences that are the same when aligned for maximum correspondence over a specified comparison window. Thus, “percentage of sequence identity”, “percent identity” and the like refer to the value determined by comparing two optimally aligned sequences over a comparison window, wherein the portion of the polypeptide sequence in the comparison window may comprise additions or deletions (i.e., gaps) as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. The percentage is calculated by determining the number of positions at which the identical amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison and multiplying the results by 100 to yield the percentage of sequence identity. Percent identity can be readily determined by any known method, including but not limited to those described in: 1) Computational Molecular Biology (Lesk, A.M., Ed.) Oxford University: NY (1988); 2) Biocomputing: Informatics and Genome Projects (Smith, D.W., Ed.) Academic: NY (1993); 3) Computer Analysis of Sequence Data, Part I (Griffin, A.M., and Griffin, H.G., Eds.) Humana: NJ (1994); 4) Sequence Analysis in Molecular Biology (von Heinje, G., Ed.) Academic (1987); and 5) Sequence Analysis Primer (Gribskov, M. and Devereux, J., Eds.) Stockton: NY (1991), all of which are incorporated herein by reference. Preferred methods for determining percent identity are designed to give the best match between the sequences tested. Methods of determining identity and similarity are codified in publicly available computer programs, for example. Sequence alignments and percent identity calculations can be performed using the MEGALIGN program of the LASERGENE bioinformatics computing suite (DNASTAR Inc., Madison, WI), for example. Multiple alignment of sequences can be performed, for example, using the Clustal method of alignment which encompasses several varieties of the algorithm including the Clustal V method of alignment (described by Higgins and Sharp, CABIOS.5:151-153 (1989); Higgins, D.G. et al., Comput. Appl. Biosci., 8:189-191 (1992)) and found in the MEGALIGN v8.0 program of the LASERGENE bioinformatics computing suite (DNASTAR Inc.). For multiple alignments, the default values can correspond to GAP PENALTY=10 and GAP LENGTH PENALTY=10. Default parameters for pairwise alignments and calculation of percent identity of protein sequences using the Clustal method can be KTUPLE=1, GAP PENALTY=3, WINDOW=5 and DIAGONALS SAVED=5. For nucleic acids, these parameters can be KTUPLE=2, GAP PENALTY=5, WINDOW=4 and DIAGONALS SAVED=4. Additionally, the Clustal W method of alignment can be used (described by Higgins and Sharp, CABIOS.5:151-153 (1989); Higgins, D.G. et al., Comput. Appl. Biosci. 8:189-191(1992); Thompson, J.D. et al, Nucleic Acids Research, 22 (22): 4673-4680, 1994) and found in the MEGALIGN v8.0 program of the LASERGENE bioinformatics computing suite (DNASTAR Inc.). Default parameters for multiple alignment (protein / nucleic acid) can be: GAP PENALTY=10 / 15, GAP LENGTH PENALTY=0.2 / 6.66, Delay Divergent Seqs(%)=30 / 30, DNA Transition Weight=0.5, Protein Weight Matrix=Gonnet Series, DNA Weight Matrix=IUB. Various polypeptide amino acid sequences are disclosed herein as features of certain embodiments. Variants of these sequences that are at least about 70-85%, 85-90%, or 90%- 95% identical to the sequences disclosed herein can be used or referenced. Alternatively, a variant amino acid sequence can have at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identity with a sequence disclosed herein. A variant amino acid sequence herein has the same function / activity of the disclosed sequence, or at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% of the function / activity of the disclosed sequence. Any polypeptide amino acid sequence disclosed herein not beginning with a methionine or valine can typically further comprise at least a start-methionine or start-valine at the N-terminus of the amino acid sequence. In contrast, any polypeptide amino acid sequence disclosed herein beginning with a methionine or valine can optionally lack such a methionine or valine residue. In some aspects, any polypeptide amino acid sequence disclosed herein beginning with a methionine or valine can instead have, respectively, a valine or methionine as the first amino acid residue. The terms “corresponds with”, “aligns with”, and the like can be used interchangeably herein. Some aspects herein relate to a non-native / modified 4,6-alpha-glucanotransferase enzyme comprising an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22. An amino acid position of a 4,6-alpha- glucanotransferase or subsequence thereof (can refer to such an amino acid position or sequence as a “query” position or sequence) can be characterized to correspond with amino acid residue Gln-487 of SEQ ID NO:22 (can refer to such an amino acid position or sequence as a “subject” position or sequence) if (1) the query sequence can be aligned with the subject sequence (e.g., where an alignment indicates that the query sequence and the subject sequence [or a subsequence of the subject sequence] are at least about 30%, 40%, 50%, 60%, 70%, 80%, or 90% identical), and (2) if the query amino acid position directly aligns with (directly lines up against) the subject amino acid position Gln-487 in the alignment of (1). In general, one can align a query amino acid sequence with a subject sequence (SEQ ID NO:22 or a subsequence of SEQ ID NO:22) using any alignment algorithm, tool and / or software described disclosed herein (e.g., BLASTP, ClustalW, ClustalV, Clustal-Omega, EMBOSS) to determine percent identity. Just for further example, one can align a query sequence with a subject sequence herein using the Needleman-Wunsch algorithm (Needleman and Wunsch, J. Mol. Biol.48:443-453, 1970) as implemented in the Needle program of the European Molecular Biology Open Software Suite (EMBOSS [e.g., version 5.0.0 or later], Rice et al., Trends Genet.16:276-277, 2000). The parameters of such an EMBOSS alignment can comprise, for example: gap open penalty of 10, gap extension penalty of 0.5, EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The numbering of particular amino acid residues of SEQ ID NO:22 herein (e.g., Gln- 487) is with respect to the full-length amino acid sequence of SEQ ID NO:22. Unless otherwise disclosed, substitutions herein are in correspondence to the full-length amino acid sequence of SEQ ID NO:22 as reference sequence. A “non-native 4,6-alpha-glucanotransferase enzyme” herein (“mutant”, “variant”, “modified” and like terms can likewise be used to describe such an enzyme) has at least one amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22 (SEQ ID NOs:86 and 92-127 are examples of such non-native enzymes). Such at least one amino acid substitution typically is in place of the amino acid residue(s) that normally (natively) occurs at the same position in the native counterpart (parent) of the non- native enzyme (i.e., although SEQ ID NO:22 is used as a reference for position, an amino acid substitution herein is with respect to the native counterpart of a non-native enzyme) (considered another way, when aligning the sequence of a non-native enzyme with SEQ ID NO:22, determining whether a substitution exists at a particular position does not depend in- and-of-itself on the respective amino acid residue in SEQ ID NO:22, but rather depends on what amino acid exists at the subject position within the native counterpart of the non-native enzyme). The amino acid normally occurring at the relevant site in the native counterpart enzyme often (but not always) is the same as (or conserved with) the particular amino acid residue of SEQ ID NO:22 for which the alignment is made. A non-native 4,6-alpha- glucanotransferase enzyme optionally can have other amino acid changes (mutations, deletions, and / or insertions) relative to its native counterpart sequence. The term “isolated” means a substance (or process) in a form or environment that does not occur in nature. A non-limiting example of an isolated substance herein includes any non-naturally occurring substance such as a food product or food precursor (as well as enzymatic reactions / processes used to prepare these materials). It is believed that the embodiments disclosed herein are synthetic / man-made (could not have been made except for human intervention / involvement), and / or have properties that are not naturally occurring. The term “increased” as used herein can refer to a quantity or activity that is at least about 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 50%, 100%, or 200% more than the quantity or activity for which the increased quantity or activity is being compared. The terms “increased”, “elevated”, “enhanced”, “greater than”, “improved” and the like are used interchangeably herein. Some aspects of the present disclosure concern a method / process of producing a food dough (flour dough or flour slurry) (a flour slurry is an example of a dough precursor or dough ingredient herein). Such a method can comprise mixing at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) one or more enzymes selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, thereby producing a food dough. Optionally, a food dough produced by this method can be characterized by one or more of the following features: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks the enzyme, (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks the enzyme, and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks the enzyme. A “control food dough” (or “corresponding food dough” and like terms) herein can be, for example, a food dough that is produced the same way, or substantially the same way, as the first food dough (food dough of the present disclosure can optionally also be referred to as “first food dough”, which can be instructive for comparison purposes), with the exception that the enzyme(s) is / are not included / added during production of the control food dough. A “control food product” (and like terms) is similarly distinguished from a food product made from a first food dough. The foregoing method can optionally be characterized herein as a dough production method or process. A dough production method herein comprises addition of one or more dextrin dextranase and / or 4,6-alpha-glucanotransferase enzymes, which processing can optionally lead to one or more enhancements of the dough product, such as increased dough strength (e.g., increased dough shock stability and / or increased dough viscosity) and / or water-binding capacity. Increased dough strength can be taken advantage of by, for example, (i) reducing the amount of gluten and / or related proteins that otherwise would be necessary as a dough component / ingredient to achieve a level of dough strength, and / or (ii) achieving greater volumes of baked products made using dough herein. A food dough production method as presently disclosed comprises provision of flour and / or meal. In some aspects, only flour or only meal is the flour / meal ingredient (one or more other ingredients that are not flour or meal can optionally also be present), while in other aspects there can be a mix of flour and meal. For example, flour and meal ingredients can comprise at least about 50, 60, 70, 80, 90, 95, 98, or 99 wt% flour, and less than about 50, 40, 30, 20, 10, 5, 2, or 1 wt% meal, or vice versa. There can be one, two, three, or more different types of flour and / or meal, for example, in the flour / meal component of food dough herein. Flour and / or meal herein can be that of a grain / cereal, root / tuber, bean / legume, or nut / seed in some aspects. Meal can be bolted or unbolted in some aspects. Suitable examples of a grain / cereal for making a flour and / or meal herein include grain of wheat (e.g., Triticum aestivum, T. compactum, T. sphaerococcum), Hordeum vulgare (barley), Avena sativa (oat), Secale cereale (rye), Triticosecale spp. (triticale), Zea mays (maize / corn), sorghum, millet (e.g., Digitaria, Echinochloa, Eleusine, Panicum, Setaria, Pennisetum), Phalaris canariensis (canary seed), rice (e.g., Oryza species such as O. sativa, Zizania), Eragrostis abyssinica (teff), and Coix lacryma-jobi (Job's tears), amaranth, buckwheat (e.g., Fagopyrum, Eriogonum) and quinoa. A grain can be dehulled or hulled. Examples of wheat varieties herein include winter and spring wheat, hard and soft wheat, and red wheat and white wheat; some particular wheat varieties are winter wheat (e.g., hard red winter, soft red winter), spring wheat (e.g., hard red spring), durum (e.g., for making semolina), hard white wheat, and soft white wheat. Soft wheat flour herein can contain about 5-9 wt% gluten (or total protein), whereas hard wheat flour can contain about 11-15 wt% gluten (or total protein), for example. Examples of corn varieties herein include dent corn, flour corn, sweet corn, flint corn, heirloom corn, and waxy corn. Examples of rice varieties herein include long grain rice, medium grain rice, short grain rice, sticky rice, basmati rice, jasmine rice, wild rice, Manmibyeo, Jinsumi, Seolgaeng, Hanareumbyeo, Chenmaai, and Goamibyeo. Examples of barley varieties herein include malting barley, Lacey, and Taylor. Flour made with grain can be whole grain flour in some aspects, which includes the germ and bran of the grain. Suitable examples of roots and tubers for making a flour and / or meal herein include arrowroot, cassava / yucca / manioc / tapioca (e.g., sweet or bitter), potatoes, sweet potatoes, yams, taro root, carrot, beetroot, parsnip, ginger, lotus root and turmeric. Potatoes can be starchy potatoes (e.g., Russet, Idaho, Yukon gold) or waxy potatoes (e.g., red, blue, fingerling), for example. Other vegetables that are fruit (e.g., squash, pumpkins, tomatoes) or leaves (e.g., kale, spinach) of plants can be used to make flour or meal in some aspects. Suitable examples of beans and legumes for making a flour and / or meal herein include chickpeas, soybeans, mung beans, peas (yellow or green), black gram (urad dal), fava beans and lentils, while suitable examples of nuts and seeds include almonds, coconuts, Brazil nuts, cashews, pistachios, macadamias, peanuts, pecans, walnuts, hazelnuts, pine nuts, flaxseeds, sunflower seeds, chia seeds, pumpkin seeds, hemp seeds, and tiger nuts. Flour made from wheat in some aspects herein can be in the form of whole wheat flour (includes the germ and bran), graham flour, cake flour, pastry flour, all-purpose (plain) flour, atta flour, or maida flour. Corn flour herein typically is made of finely ground cornmeal. Cornmeal in some aspects can be unprocessed or further processed (e.g., leached with lye to make corn masa). In some aspects, the gluten content of a flour (e.g., wheat flour) is about, or less than about, 12%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 0.5%, 0.1%, 0.01%, 0.001%, 0% (or otherwise undetectable), 0.001-0.01%, 0.001-0.1%, 4-6%, 4-8%, 4-9%, 5-9%, 6-8%, or 6-10% by weight. Typically, a flour or dough herein comprises alpha-1,4-glucan such as in the form of starch, amongst other species of alpha-1,4-glucan (e.g., dextrin, amylodextrin, maltodextrin, malto-oligosaccharides). Such starch-containing flour or dough can thus optionally be characterized as being farinaceous. A dextrin dextranase and / or a 4,6-alpha-glucanotransferase of the present disclosure, such as one used in a food dough production method herein, can be a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase, for example. In some aspects, a dextrin dextranase and / or 4,6-alpha-glucanotransferase can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148 and have dextrin dextranase and / or 4,6-alpha- glucanotransferase activity (e.g., GtfB, GtfC, GtfD, or GH31 enzyme activity), as appropriate (yet, in some aspects, the amino acid sequence is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, or 99.5% identical to one of the foregoing sequences [SEQ ID NOs], but is not 100% identical; this aspect can be applied to all other particular SEQ ID NO lists herein, as appropriate). Respective examples (for SEQ ID NOs:1-27) of such a dextrin dextranase and / or 4,6-alpha- glucanotransferase can comprise, or consist of, an amino acid sequence that is about, or at least about, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, or 54. In some aspects, a dextrin dextranase and / or 4,6- alpha-glucanotransferase can comprise, or consist of, an amino acid sequence that is about, or at least about, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:1, 2, 5, 6, 12, 14, 16, 22, 26, or 27. In some aspects, a dextrin dextranase can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, and have dextrin dextranase activity. In some aspects, a GtfB enzyme can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:14, 15, 16, 17, 18, 19, or 20, and have GtfB enzyme activity. In some aspects, a GtfC enzyme can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:21, 26, or 27, and have GtfC enzyme activity. In some aspects, a GtfD enzyme can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:22, 23, 24, 25, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, or 127, and have GtfD enzyme activity. In some aspects, a GH31 enzyme can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:12 or 13, and have GH31 enzyme activity. In some aspects, a dextrin dextranase and / or 4,6-alpha-glucanotransferase, such as any of the foregoing enzymes, can be one that is encoded by a polynucleotide sequence comprising, or consisting of, a nucleotide sequence that is 100% identical to, or that is at least 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to, SEQ ID NO:55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, or 81. Given that certain amino acids share similar structural and / or charge features with each other (i.e., conserved), one or more amino acids of a dextrin dextranase or 4,6-alpha- glucanotransferase sequence herein (and / or other types of polypeptides herein) can optionally be substituted with a conserved amino acid residue (“conservative amino acid substitution”) as follows: 1. The following small aliphatic, nonpolar or slightly polar residues can substitute for each other: Ala (A), Ser (S), Thr (T), Pro (P), Gly (G); 2. The following polar, negatively charged residues and their amides can substitute for each other: Asp (D), Asn (N), Glu (E), Gln (Q); 3. The following polar, positively charged residues can substitute for each other: His (H), Arg (R), Lys (K); 4. The following aliphatic, nonpolar residues can substitute for each other: Ala (A), Leu (L), Ile (I), Val (V), Cys (C), Met (M); and / or 5. The following large aromatic residues can substitute for each other: Phe (F), Tyr (Y), Trp (W). In some aspects, a dextrin dextranase or 4,6-alpha-glucanotransferase enzyme can be any as disclosed herein and include 1-300 (or any integer there between [e.g., 10, 15, 20, 25, 30, 35, 40, 45, or 50]) residues on the N-terminus and / or C-terminus. Such additional residues can be from a corresponding wild type sequence from which the GTF enzyme is derivable, or can be a heterologous sequence such as an epitope tag (at either N- or C- terminus) or a heterologous signal peptide (at N-terminus), for example. A dextrin dextranase or 4,6-alpha-glucanotransferase enzyme as used in a method herein typically lacks an N-terminal signal peptide; such an enzyme can optionally be characterized as being mature if its signal peptide was removed during a secretion process. In some aspects, a dextrin dextranase or 4,6-alpha-glucanotransferase enzyme can be derived / obtained from, or is derivable / obtainable from, a microbe such as a species of bacteria. Examples of such bacteria include species of Mesobacillus (e.g., M. subterraneus), Pseudoclostridium (e.g., P. thermosuccinogenes), Bacillus, Paenibacillus (e.g., P. sp.81-11, P. sp. Soil750), Listeria (e.g., L. seeligeri), Jannaschia (e.g., J. sp. S6380), Acetobacteraceae, Oscillospiraceae (e.g., O. bacterium), Lawsonibacter (e.g., L. sp. NSJ-51), Leifsonia (e.g., L. shinshuensis such as sp. DSM 15165), Microaerobacter (e.g., M. geothermalis), Cohnella (e.g., C. zeiphila), Exiguobacterium (e.g., E. acetylicum), Limosilactobacillus (e.g., L. reuteri), Streptococcus (e.g., S. thermophilus), Clostridium (e.g., C. oryzae), Gammaproteobacteria (e.g., G. bacterium), Actinospica (e.g., A. durhamensis), Microbacterium, Acidobacteria (e.g., A. bacterium such as sp. AB60), Caballeronia (e.g., C. arationis), and / or Paraburkholderia (e.g., P. sp. HD33-4). In some aspects, a dextrin dextranase or 4,6-alpha-glucanotransferase enzyme is metagenomic in origin (e.g., the enzyme represents a metagenomic composite and / or is obtained / obtainable from a metagenomic source). In some aspects, a 4,6-alpha-glucanotransferase enzyme (e.g., a GtfD enzyme or DDase enzyme) has been modified such that the enzyme has enhanced performance (e.g., enhanced yield of producing a modified alpha-glucan as presently disclosed). Such a modification can be, for example, by having one, two, or more amino acid substitutions as compared to a corresponding parent / control GtfD or DDase 4,6-alpha-glucanotransferase enzyme (e.g., a wild type mature 4,6-alpha-glucanotransferase enzyme or active subsequence thereof). In some aspects, an increase in yield of a modified alpha-glucan can be by about, or at least about, 10%, 25%, 50%, 100%, 150%, or 200%, for example, as compared to the yield of the modified alpha-glucan by a parent / control 4,6-alpha-glucanotransferase enzyme that has not been modified (typically, a parent / control 4,6-alpha-glucanotransferase enzyme only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position[s]), typically under the same enzyme reaction conditions (e.g., as presently disclosed). Yield can be based on actual yield (e.g., product weight or moles), or based on percent yield (i.e., actual yield / theoretical yield x 100%), for instance. In some aspects, a modified 4,6-alpha-glucanotransferase enzyme comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22, such that the modified enzyme has an increased modified alpha-glucan yield as compared to a parent / control enzyme that only differs from the modified 4,6-alpha- glucanotransferase enzyme at the substitution position. Such a substitution can be with an amino acid residue that is not conserved with Gln (glutamine), for example. In some aspects, an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22 can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]). A modified 4,6-alpha-glucanotransferase enzyme herein can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:22 (but not be 100% identical to SEQ ID NO:22). For example, a modified 4,6-alpha- glucanotransferase enzyme herein can (i) comprise an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22 (e.g., the substitution can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue [or can be with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]]), and (ii) comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:22 (but not be 100% identical to SEQ ID NO:22). Examples of such a modified 4,6-alpha-glucanotransferase enzyme herein include SEQ ID NO:86, which has an Ile residue at amino acid position 487, and SEQ ID NOs:87, 88, 89, 90 and 91. In some aspects, a modified 4,6-alpha-glucanotransferase enzyme comprises an amino acid substitution at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23, such that the modified enzyme has an increased modified alpha-glucan yield as compared to a parent / control enzyme that only differs from the modified 4,6-alpha- glucanotransferase enzyme at the substitution position. Such a substitution can be with an amino acid residue that is not conserved with Gln (glutamine), for example. In some aspects, an amino acid substitution at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23 can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]). A modified 4,6-alpha-glucanotransferase enzyme herein can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:23 (but not be 100% identical to SEQ ID NO:23). For example, a modified 4,6-alpha- glucanotransferase enzyme herein can (i) comprise an amino acid substitution at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23 (e.g., the substitution can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue [or can be with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]]), and (ii) comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:23 (but not be 100% identical to SEQ ID NO:23). An example of such a modified 4,6-alpha-glucanotransferase enzyme herein includes SEQ ID NO:87, which has an Ile residue at amino acid position 543. In some aspects, a modified 4,6-alpha-glucanotransferase enzyme comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83, such that the modified enzyme has an increased modified alpha-glucan yield as compared to a parent / control enzyme that only differs from the modified 4,6-alpha- glucanotransferase enzyme at the substitution position. Such a substitution can be with an amino acid residue that is not conserved with Gln (glutamine), for example. In some aspects, an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83 can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]). A modified 4,6-alpha-glucanotransferase enzyme herein can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:83 (but not be 100% identical to SEQ ID NO:83). For example, a modified 4,6-alpha- glucanotransferase enzyme herein can (i) comprise an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83 (e.g., the substitution can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue [or can be with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]]), and (ii) comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:83 (but not be 100% identical to SEQ ID NO:83). An example of such a modified 4,6-alpha-glucanotransferase enzyme herein includes SEQ ID NO:89, which has an Ile residue at amino acid position 487. In some aspects, a modified 4,6-alpha-glucanotransferase enzyme comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:84, such that the modified enzyme has an increased modified alpha-glucan yield as compared to a parent / control enzyme that only differs from the modified 4,6-alpha- glucanotransferase enzyme at the substitution position. Such a substitution can be with an amino acid residue that is not conserved with Gln (glutamine), for example. In some aspects, an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:84 can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]). A modified 4,6-alpha-glucanotransferase enzyme herein can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:84 (but not be 100% identical to SEQ ID NO:84). For example, a modified 4,6-alpha- glucanotransferase enzyme herein can (i) comprise an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:84 (e.g., the substitution can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue [or can be with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]]), and (ii) comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:84 (but not be 100% identical to SEQ ID NO:84). An example of such a modified 4,6-alpha-glucanotransferase enzyme herein includes SEQ ID NO:90, which has an Ile residue at amino acid position 487. In some aspects, a modified 4,6-alpha-glucanotransferase enzyme comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:85, such that the modified enzyme has an increased modified alpha-glucan yield as compared to a parent / control enzyme that only differs from the modified 4,6-alpha- glucanotransferase enzyme at the substitution position. Such a substitution can be with an amino acid residue that is not conserved with Gln (glutamine), for example. In some aspects, an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:85 can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]). A modified 4,6-alpha-glucanotransferase enzyme herein can comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:85 (but not be 100% identical to SEQ ID NO:85). For example, a modified 4,6-alpha- glucanotransferase enzyme herein can (i) comprise an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:85 (e.g., the substitution can be with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue [or can be with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]]), and (ii) comprise, or consist of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to SEQ ID NO:85 (but not be 100% identical to SEQ ID NO:85). An example of such a modified 4,6-alpha-glucanotransferase enzyme herein includes SEQ ID NO:91, which has an Ile residue at amino acid position 487. A dextrin dextranase or 4,6-alpha-glucanotransferase enzyme herein can be prepared by fermentation with an appropriately engineered microbial strain, for example. Recombinant enzyme production by fermentation can be done, for example, using microbial species such as E. coli, Bacillus strains (e.g., B. subtilis), Ralstonia eutropha, Pseudomonas fluorescens, Saccharomyces cerevisiae, Pichia pastoris, Hansenula polymorpha, and species of Aspergillus (e.g., A. awamori) and Trichoderma (e.g., T. reesei) (e.g., see Adrio and Demain, Biomolecules 4:117-139, 2014, which is incorporated herein by reference). A nucleotide sequence encoding a dextrin dextranase or 4,6-alpha-glucanotransferase amino acid sequence is typically linked to a heterologous promoter sequence to create an expression cassette for the enzyme, and / or is codon-optimized accordingly. Such an expression cassette can be incorporated in a suitable plasmid or integrated into the microbial host chromosome. The expression cassette can include a transcriptional terminator nucleotide sequence following the amino acid coding sequence. The expression cassette can also include, between the promoter sequence and enzyme amino acid coding sequence, a nucleotide sequence encoding a signal peptide (e.g., heterologous signal peptide) that is designed for direct secretion of the enzyme. At the end of fermentation, cells can be ruptured accordingly (generally when a signal peptide for secretion is not employed) and the enzyme can be isolated or purified using methods such as precipitation, filtration, and / or concentration. Alternatively, a lysate or extract comprising an enzyme can be used without further isolation or purification. If the GTF was secreted (i.e., it is present in the fermentation broth), it can optionally be used as isolated / purified from, or as comprised in, the fermentation broth. The activity of a dextrin dextranase or 4,6-alpha-glucanotransferase enzyme can be confirmed by biochemical assay, such as by following methodology described in the below Examples. A dextrin dextranase or 4,6-alpha-glucanotransferase enzyme (and / or any other enzyme as presently disclosed as useful in producing dough) for use in a dough production method herein is typically in purified form. A purified enzyme can be essentially free from insoluble and / or soluble components of an organism / cell used to produce the enzyme, and / or any medium that was used for cellular fermentation of the enzyme. In some aspects, a purified enzyme denotes an enzyme preparation that contains less than 10%, 8%, 6%, 5%, 4%, 3%, 2%, 1%, 0.5%, or 0.1% by weight of other material (e.g., polypeptide material) with which the enzyme is natively or recombinantly associated. In some aspects, an enzyme herein is not comprised in, or otherwise associated with (e.g., expressed by), a microbial (e.g., bacterial, yeast, fungal, algal) cell that might be present (e.g., endogenously or purposely added) in a food dough or food product / precursor herein; however, in some aspects any foregoing enzyme(s) is comprised in, or otherwise associated with (e.g., expressed by), a microbial (e.g., bacterial, yeast, fungal, algal) cell such as one that heterologously expresses the enzyme(s) (i.e., recombinant cells). Contacting a food product / precursor with a foregoing enzyme(s) herein typically is not performed in an oral cavity or other environment in which unpurified / non-isolated enzyme can possibly be present. It is contemplated that contacting one or more dextrin dextranase and / or 4,6-alpha- glucanotransferase enzymes of the present disclosure with flour and / or meal under aqueous conditions during the mixing step of a food dough production method results in production of modified alpha-glucan. It is contemplated that modified alpha-glucan herein accounts for at least part of, or all of, one or more of the dough enhancements disclosed herein achieved with enzyme treatment. Modified alpha-glucan herein can comprise, for example, alpha-1,4-glucan such as starch (which includes amylose and / or amylopectin, e.g.) and / or dextrin, amylodextrin, and / or maltodextrin that has / have been modified in some manner by enzyme treatment herein. The alpha-1,4-glucan can be as it is found in dough, for example, and / or as it can be provided as an exogenous ingredient (e.g., that has not yet been used in food production such as presently disclosed) (e.g., a starch hydrolysate). For instance, alpha-1,4-glucan herein can originate from the flour itself (typically), and / or be a separate ingredient included in a dough production method herein (or any other food production method). Examples of alpha-1,4- glucan modification include reduction of the molecular weight (reduced DPw) of the alpha- 1,4-glucan (e.g., removal of at least one glucose residue from the alpha-1,4-glucan) and / or addition of one or more glucose residues to the alpha-1,4-glucan (e.g., addition of one or more glucose residues via an alpha-1,6 and / or alpha-1,3 [and / or sometimes alpha-1,2 linkage]), either at a non-reducing end(s) of the alpha-1,4-glucan and / or via at least one branch linkage formation, where such addition can be by a single residue [e.g., a pendant glucose branch] or formation of at least one chain of two or more glucose residues [typically all linked by same linkage type]). Thus, in some aspects, the alpha-1,4 glycosidic linkage content of the alpha-1,4-glucan of the food dough can be reduced as compared to the alpha- 1,4 glycosidic linkage content of the alpha-1,4-glucan of a control food dough or of the flour / meal as it existed before mixing the flour / meal with an enzyme(s) herein; this likewise can apply to aspects in which alpha-1,4-glucan is an exogenous ingredient that has not yet been used in food production, for example. Typically, such a reduction in alpha-1,4 linkage content occurs in concert with an increase in alpha-1,6 and / or alpha-1,3 glycosidic linkage content (and / or sometimes alpha-1,2 glycosidic linkage content) in the alpha-1,4-glucan (as compared to the alpha-1,6 and / or alpha-1,3 glycosidic linkage content [and / or sometimes alpha-1,2 glycosidic linkage content] of the [i] alpha-1,4-glucan of a control food dough or of the flour / meal as it existed before mixing the flour / meal with an enzyme(s) herein, or [ii] a control alpha-1,4-glucan exogenous ingredient that has not been contacted with an enzyme(s) herein). Modified alpha-glucan herein can comprise, for example, gluco-oligosaccharides (GlcOS) that are newly synthesized by an enzyme treatment herein, and / or that are pre- existing GlcOS that have been increased in molecular weight by the enzyme treatment. Such an increase in molecular weight can be reflected by an increase in GlcOS DPw by at least 1, 2, 3, 4, 5, 6, 7, 8, or more, for example, as compared to the DPw of the GlcOS of a control dough or of the flour / meal as it existed before mixing the flour / meal with an enzyme(s) herein. GlcOS herein can have a DP or DPw of about, or at least about, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 20, 3-10, 3-15, 3-20, 5-10, 5-15, or 5-20, for example; such a DP or DPw can optionally characterize GlcOS of a dough before (e.g., MOS) or following (MOS [modified MOS] and / or IMOS) (depending on the context being referred to, accordingly) an enzymatic treatment. Prior to an enzyme treatment herein (i.e., not yet modified alpha-glucan herein), the glycosidic linkage content of GlcOS can be about 100% alpha-1,4, or at least about 95%, 96%, 97%, 98%, 99%, or 99.5% alpha-1,4 (i.e., pre-existing GlcOS can include malto-oligosaccharides [MOS]), for example. Following an enzyme treatment herein (i.e., now pertaining to modified alpha-glucan herein), the GlcOS of a dough can have an increase in alpha-1,6 and / or alpha-1,3 glycosidic linkage content (and / or sometimes alpha-1,2 glycosidic linkage content) (as compared to the alpha-1,6 and / or alpha-1,3 glycosidic linkage content [and / or sometimes alpha-1,2 glycosidic linkage content] of the GlcOS of a control dough or of the flour / meal as it existed before mixing the flour / meal with an enzyme(s) herein). Addition of one or more glucose residues to GlcOS by an enzyme treatment in dough herein can be via alpha-1,6 and / or alpha-1,3 linkage (and / or sometimes alpha-1,2 linkage), either at a non-reducing end(s) of the GlcOS and / or via at least one branch linkage formation, where such addition can be by a single residue [e.g., a pendant glucose branch] or formation of at least one chain of two or more glucose residues [typically all linked by same linkage type]). Typically, at least some GlcOS comprised in modified alpha-glucan herein can optionally be characterized as MOS that has been extended and / or branched with one or more glucose residues linked to the MOS via alpha-1,6 and / or alpha-1,3 linkage (and / or sometimes alpha-1,2 linkage). In some aspects, at least some GlcOS comprised in modified alpha-glucan herein is newly synthesized by an enzyme treatment herein (e.g., GlcOS made completely de novo or from enzymatic extension of pre-existing DP1 or DP2 saccharides such as glucose and di-glucose). The glycosidic linkage content of newly synthesized GlcOS in some aspects can be about 100% alpha-1,6, or at least about 95%, 96%, 97%, 98%, 99%, or 99.5% alpha-1,6 (i.e., newly synthesized GlcOS can include isomalto-oligosaccharides [IMOS]). In some aspects, such as with particular flours, the GlcOS of a flour before treatment can include IMOS, and modified alpha-glucan made following an enzymatic treatment herein includes IMOS modified as above (extended and / or branched). In general, newly synthesized or modified GlcOS of modified alpha-glucan herein is produced from (at least in part) glucose residues that were originally a constituent of alpha-1,4-glucan of the flour or meal before enzymatic treatment in a dough production method of the disclosure. In some aspects of a food or food dough herein, at least 0.5% or 1% by weight of the dry weight of the food or food dough is modified alpha-glucan (e.g., including modified GlcOS and / or modified alpha-1,4-glucan [e.g., modified starch]) of the disclosure. In some aspects, this weight percentage is about, or at least about, 0.5%, 1%, 5%, 10%, 25%, 30%, 40%, 50%, 0.5-50%, 0.5-40%, 0.5-30%, 0.5-25%, 0.5-20%, 0.5-10%, 5-50%, 5-40%, 5-30%, 5-25%, 5-20%, or 5-10%. An aqueous composition used in a food dough production method herein typically is water, an aqueous solution, and / or an aqueous mixture. An example of an aqueous mixture herein is a dispersion such as a homogenized product (e.g., milk such as skim milk, low-fat milk, whole milk, or other dispersed dairy product). Further examples of an aqueous composition herein include whole eggs (comprise ~70-80 wt% water), egg whites (comprise ~85-90 wt% water), egg yolks (comprise ~45-50 wt% water), buttermilk, yogurt, sour cream, cottage cheese, soft cheese (e.g., ricotta), coconut milk, juice (e.g., fruit or vegetable juice), beer (e.g., ale, lager), cider, wine, liquor, or soda. One, two, three, four, or more of the foregoing aqueous ingredients can be in the aqueous composition component of a dough recipe herein. The content of flour and / or meal (or the total solids content) in a flour dough or flour slurry (or other dough precursor / ingredient) herein can be about, or at least about, 30, 35, 40, 45, 50, 55, 60, 30-60, 30-50, 30-40, 35-60, 35-50, 35-40, 40-60, 40-50, or 50-60 wt%, for example. Typically, the balance of the dough or slurry (in weight) can be of water. Optionally, the balance can be of water plus some amount of other food-suitable liquid where the water typically is over 80%, 90%, or 95% by weight of the total liquid, for example. Examples of a food-suitable liquid include oil (e.g., coconut oil, palm kernel oil, palm oil, cottonseed oil, wheat germ oil, soybean oil, olive oil, corn oil, sunflower oil, safflower oil, hemp oil, canola / rapeseed oil, vegetable oil, lecithin oil) and any other suitable liquid as presently disclosed. The content of at least one of a dextrin dextranase or 4,6-alpha-glucanotransferase in a food dough herein can be about, or at least about, 0.1, 0.15, 0.2, 0.25, 0.3, 0.4, 0.5, 0.75, 1, 1.25, 1.5, 1.75., 2, 2.5, 0.1-1, 0.1-0.75, 0.1-0.5, 0.1-0.3, 0.2-1, 0.2-0.75, 0.2-0.5, 0.2-0.3, 0.5- 2.5, 0.5-2, 0.5-1.5, 0.5-1, 1-2.5, 1-2, or 1-1.5 wt%, for example. In some aspects, a single dextrin dextranase or 4,6-alpha-glucanotransferase is used, whereas two, three, or more of such enzyme(s) can be used in other aspects. The foregoing enzyme contents can be with respect to one enzyme, or a combination of enzymes. The foregoing enzyme contents are typically with respect to active enzyme(s), but in some aspects can be with respect to total protein of isolated / purified enzyme(s). A dextrin dextranase or 4,6-alpha-glucanotransferase enzyme (and / or any other enzyme as presently disclosed as useful in producing dough) for use in a dough production method herein can be comprised in a sterile-filtered preparation, for example. In some aspects, an enzyme can be sterile-filtered inline while applying the enzyme to a food product / precursor herein. In some aspects, an enzyme can be added to a food product / precursor that has been pasteurized (after pasteurization), or alternatively an enzyme can be added before pasteurizing the food product / precursor. In some aspects, an enzyme can be added to a food product / precursor that has been fermented (after fermentation), or alternatively an enzyme can be added during or before fermenting the food product / precursor. An enzyme in some aspects can be comprised in a preparation that is substantially free of (e.g., <0.5, <0.1, <0.05 wt%) any other enzyme(s) such as a lipase, protease, amylase, mannanase, pectinase, cellulase, and / or p-nitrobenzylesterase; such a preparation typically has little or no detectable activity(ies) of such other enzyme(s). A food (e.g., bread) or food dough (e.g., bread dough) herein can optionally comprise other ingredients in addition to its water (for dough and food products comprising water), flour / meal and modified alpha-glucan components. For example, at least one component selected from lipids, emulsifiers, enzymes, salt, sugar (e.g., sucrose, fructose, dextrose), added protein source (e.g., whey protein, egg), added starch, added gluten, leavening agent (e.g., yeast, baking powder, baking soda), natural and / or artificial flavors / colors, aqueous liquid (e.g., water, milk), and artificial sweetener can be included. Examples of lipid ingredients include triglycerides and phospholipids, such as soybean oil, soybean lecithin, butter, lard, margarine, corn oil, peanut oil, canola oil, or olive oil. Examples of emulsifiers include monoglycerides, diglycerides and esters of these glycerides and acids such as monoglyceride lactate or monoglyceride diacetyltartrate. Examples of enzymes include proteolytic enzymes, amylolytic enzymes and hemicellulolytic enzymes (e.g., alpha-amylase, beta-amylase, endo-xylanase, protease). Additional examples of enzymes include lipase, alpha-amylase, xylanase, non-maltogenic exoamylase, glucoamylase, glucose oxidase, and hexose oxidase. Examples of other agents that can be included in a food or food dough herein include oxidizing agents, reducing agents, and water-binding components such as hydrocolloids (e.g., pectin, gelatin, carboxymethyl cellulose, carrageenan, guar, locust bean gum, alpha-1,3-glucan). Bread or bread dough in some aspects can comprise one or more ingredients as disclosed in any of U.S. Pat. Appl. Publ. Nos.2005 / 0013900, 2009 / 0297663, or 2018 / 030310, which are incorporated herein by reference. In addition to these references, a food, food dough, or precursor herein such as a bread, bread dough, or dough slurry can optionally comprise one or more ingredients according to any of U.S. Patent Nos.3889003, 3930055, 3987206, 4367241, 4645673, 4687673, 4849230, 5403610, 5409717, 7947319, 7815952, 9883679, or 8486469, all of which are incorporated herein by reference. A food dough production method herein comprises a step of mixing / blending / stirring at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) one or more enzymes selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, to produce a food dough. In some aspects, food dough production method can simply comprise providing a food dough comprising at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) one or more enzymes selected from a dextrin dextranase and / or a 4,6- alpha-glucanotransferase. Mixing herein typically produces a flour dough or slurry. The mixing step of a food dough production method herein can comprise, for example, addition of all of at least the recipe ingredients of (i) flour and / or meal, (ii) water or aqueous composition, and (iii) one or more enzymes selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase together into a mixing vessel, followed by mixing, or mixing two of the ingredients first (i and ii, i and iii, ii and iii) followed by admixture of the third remaining ingredient. One or more other ingredients (e.g., any as disclosed herein such as a leavening agent) can optionally be included in any of these mixing schemes. Mixing herein can be done manually or via automation. Mixing can optionally also be characterized herein as stirring, blending, or any other like term. In some aspects, a food dough or slurry produced herein is allowed to incubate for a time (e.g., ~0.5 hour to about, or at least about, 1, 2, 4, 6, 8, 10, or 12 hours) and / or temperature (e.g., ~5-50 °C, ~20-40 °C, ~30-40 °C, ~20-30 °C, ~20-25 °C, ~20 °C, ~25 °C, ~30 °C, ~35 °C, ~37 °C, or ~40 °C) allowing one or more of the ingredient dextrin dextranase and / or 4,6-alpha-glucanotransferase enzymes to produce modified alpha-glucan in the dough or slurry. It is contemplated that in situ modified alpha-glucan production can also occur while initially mixing and / or kneading a dough having all of at least ingredients (i), (ii) and (iii) (above). Yet, in some aspects, incubation of one or more dextrin dextranase and / or a 4,6-alpha- glucanotransferase enzymes (and / or any other enzyme as presently disclosed) in a flour dough or slurry can be for about, or at least about, 0.5, 1, 1.5, 2, 2.5, 3, 4, 5, 6, 7, 8, 9, 10, 12, 15, 18, 24, 30, 36, 42, 48, 72, 96, 0.5-3, 0.5-2.5, 0.5-2, 0.5-1.5, 1-3, 1-2.5, 1-2, 1-1.5, 1.5-3, or 1.5-2 hours, or for about, or at least about, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, or 60 days (or a range between any two of these hours and / or days), for example. The temperature for incubating one or more enzymes in a dough or slurry herein can be about 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 14, 16, 18, 20, 22, 24, 25, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 2-5, 2-10, 2-15, 2-20, 2-25, 2-30, 2-35, 2-40, 2-45, 2-50, 3-5, 3-10, 3-15, 3-20, 3-25, 3-30, 3-35, 3-40, 3-45, 3-50, 5-10, 5-15, 5-20, 5-25, 5-30, 5-35, 5-40, 5-45, 5-50, 15-20, 15-25, 15-30, 15-35, 15-40, 15-45, 15-50, 20-25, 20-30, 20-35, 20-40, 20-45, 20-50, 25-30, 25-35, 25-40, 25-45, 25-50, 30-35, 30-40, 30-45, or 30-50 °C, for example. In some aspects, one or more dextrin dextranase and / or a 4,6-alpha-glucanotransferase enzymes (and / or any other enzyme as presently disclosed) can be added during a food dough production method in dry form (e.g., powder, flakes, lyophilized enzyme preparation) or wet form, either of which enzyme form typically is added to a wet preparation. In some aspects, a flour can be combined with enzyme(s) under dry conditions (resulting combination is dry), after which time water or an aqueous composition is added. The water content of a food dough or slurry (or food product) herein can be about, or at least about, 10, 20, 30, 40, 50, 60, 70, 80, or 90 wt%, for example. The pH of a food dough or slurry herein, which is typically the pH for incubating one or more enzymes in the food dough or slurry, can be about 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, 8.5, 9.0, 5.0-9.0, 5.0-8.0, 5.5-9.0, 5.5-8.0, 6.0-9.0, or 6.0-8.0, for example. A dextrin dextranase and / or a 4,6-alpha-glucanotransferase enzymes (and / or any other enzyme as presently disclosed) herein can optionally be provided by introducing a recombinantly engineered cell (e.g., a microbial cell such as a bacterial or fungal / yeast cell) during food dough / slurry production, wherein the cell recombinantly (heterologously) expresses and secretes the enzyme(s) in the dough or slurry. Such a cell can be that of a microbe that is amenable to recombinant engineering and useful in food processing (e.g., fermentation), such as a microbial cell disclosed herein (as applicable). In some aspects, a recombinantly engineered cell that is provided in a flour dough or slurry herein can be inactive and / or non-viable in some manner, such as by having been killed (but preferably in a manner that otherwise retains cellular shape / structure). For example, a cell can be rendered inactive and / or non-viable by being irradiated or being treated with a sterilizing agent / chemical (e.g., ethylene oxide). Typically, the means for cell inactivation and / or killing preserves at least some of the three-dimensional shape / structure of the cell, and / or ensures that enzyme(s) that had been expressed by the cell remains active and typically remains associated with the inactive / non-viable cell (e.g., such as by being associated with a cellular membrane via an optional transmembrane domain or membrane-binding domain of the enzyme(s) [e.g., fused to the enzyme]). An inactive / non-viable cell typically is porous, and optionally can be immobilized on a support (e.g., an inert, water-insoluble material, such as of a particle or surface). A dough production method herein can further include, for example, a step of processing the food dough into a food product. Such aspects can therefore be characterized as a food production method, if desired. In some aspects, dough processing for food production can comprise at least baking, frying, boiling, steaming, drying, leavening, chilling, extruding, and / or flattening / rolling the food dough. Any of these processing steps can be performed as disclosed in any of U.S. Pat. Appl. Publ. Nos.2005 / 0013900, 2009 / 0297663, or 2018 / 030310, or U.S. Patent Nos.3889003, 3930055, 3987206, 4367241, 4645673, 4687673, 4849230, 5403610, 5409717, 7947319, 7815952, 9883679, or 8486469 (all of which are incorporated herein by reference), for example. Example conditions for making a bread product herein include letting a bread dough rise at a temperature of about 20 to 40 °C (e.g., for about 20 to 45 minutes), followed by baking at a temperature of about 350 to 425 °F (e.g., for a time of about 25 to 45 minutes). In some aspects, parameters for conducting dough rising and / or baking (as well as other steps such as mixing), and can be as disclosed in any of U.S. Patent Nos.4957040, 4538509, 5615605, 6035763, or 6113966, for example, which are all incorporated herein by reference. A food as presently disclosed, such as one made using a food dough herein, can be a baked food and / or extruded food, for instance. In some aspects, and optionally in addition to being baked and / or extruded, a food can have been fried, boiled, steamed, dried, leavened, chilled, and / or flattened / rolled during its production. Examples of a baked food herein include bread (e.g., buns, sourdough, rye, whole wheat, pita, flatbread, tortilla, cornbread, brioche, white, baguette, bagels, banana, ciabatta, brown, challah, focaccia, multigrain, bread sticks, soda bread, pumpernickel, potato bread, biscuits, English muffins, whole grain, matzo, lavash, croutons, pizza crust), cakes (e.g., carrot cake, red velvet, angle food, pound cake, chocolate, white, black forest, tiramisu, coffee cake, cheesecake, devil’s food, upside-down cake, Boston cream pie, Swiss roll, lemon cake, short cake, chiffon cake, butter cake, spice cake, rum cake, sponge cake, marble cake, coconut cake, pandan cake), muffins, brownies, scones, cookies, bars, custards, pies, crackers (e.g., saltines, oyster crackers, cream crackers, water biscuits, cheese crackers, graham crackers, digestive biscuits, RITZ style crackers), pretzels, pastries, pudding and tarts. A food herein such as bread can be leavened or unleavened. Examples of an extruded food herein include pasta (e.g., spaghetti, rotini, fusilli, penne, bucatini, macaroni / maccheroni, rigatoni, fettuccine, linguine, vermicelli, ziti, farfalle, gomiti / elbow, rotelle), cereal (e.g., direct expanded cereal, filled cereal, flakes, breakfast cereal), some bread products (e.g., croutons, bread sticks, flat breads), pre-made cookie- dough, dry and semi-moist pet food (e.g., kibbles), and snacks (e.g., cheese curls, filled pillow puffs, chips [e.g., corn chips, pita chips, processed potato chips, tortilla chips], snack sticks [e.g., vegetable sticks], puffed shaped products such as curls [e.g., cheese curls], balls, tubes, bananas, cups, bowls, disks, baby food puffs). Pasta herein can be extruded (e.g., see above) and / or flattened / rolled (e.g., lasagna), fresh or dried, long or short, minute / soup pasta (pastina), filled (e.g., tortellini, ravioli, agnolotti, tortelli), stretched (e.g., cencioni, corzetti, foglie d’ulivo, orecchiette), and / or egg pasta. Examples of a fried food herein include beignets, churros, fried dough (e.g., elephant ears), doughnuts, falafel, fritters, funnel cake, hushpuppies, jin deui, fish cakes, empaná, curry puffs, curry bread, croquettes, noodles (wheat, rice), frybread / popovers, haliva, kachori, luchi, ma hua, papadum, paratha, pastel, prawn cracker, puri, papri, samosa, shuangbaotai, fried bread sticks, pierogi, pancakes / hotcakes, naan, roti, chapati, waffles, and batter. A fried food herein can be prepared by cooking food in hot vegetable or animal oil / fat, and / or by heating on a pan / griddle or other vessel typically containing at least a small amount of (much less than used in a deep-frying process) vegetable or animal oil / fat on its cooking surface. A food dough herein can be that used to prepare any of the foregoing products, for example. Semolina flour dough optionally can be used to prepare pasta herein. A food dough, food product, or any other composition, such as any as presently disclosed, can comprise one or more dextrin dextranase and / or 4,6-alpha-glucanotransferase enzymes herein (e.g., protein / amino acid sequences), and / or optionally further one or more polynucleotides (nucleic acid sequences) encoding such one or more enzymes. In some aspects, a dextrin dextranase and / or 4,6-alpha-glucanotransferase enzyme in any of the foregoing materials has been inactivated, such as by heat-inactivation or another inactivation means. A food product or food dough as presently disclosed in some aspects (e.g., a bread or bread dough) can have the same or improved handling / machinability, shelf life, texture, moisture, shape, volume, cohesiveness, strength, viscosity, shock stability, crumb pore size, uniformity of gas bubbles, non-separation of crust and crumb, crust crispiness, oven spring, staling resistance, water-binding capacity and / or dietary fiber characteristics as compared to a control food product or control food dough. If improved, such improvement of one or more of these characteristics can be by about, or at least about, 1%, 2%, 5%, 7.5%, 10%, 12.5%, 15%, 20%, 25%, 30%, 1-30%, 1-25%, 1-20%, 1-15%, 5-30%, 5-25%, 5-20%, 5-15%, or 7.5- 12.5%, for example, as compared to a control food product or control food dough. In some aspects, the shape, cohesiveness, and / or strength of a bread or bread dough herein is / are retained while keeping the benefit of reduced gluten. In some aspects, a food dough has a shock stability that is increased as compared to the shock stability of a control food dough. Typically, shock stability of a dough is with regard to a dough that has risen (e.g., dough that has been leavened, such as by comprising an added yeast, and subjected to conditions suitable for allowing the dough to rise from such leavening) (e.g., a raised bread dough loaf / roll). Shock stability in some aspects can be assessed by dropping a risen bread dough at least one time over a distance of about, or at least about, 1.0, 1.5, 2.0, 2.2, 2.5, 1.0-2.5, 1.5-2.5, or 2.0-2.5 cm (i.e., a shocking step), and then optionally measuring the height and / or volume of the now-shocked bread dough. Such a shocking step in some aspects can simply be practiced by virtue of moving a risen bread dough from one place to another in a bread production facility (e.g., bakery, kitchen), where, during the course of such movement, there is ample vertical movement constituting dropping the raised bread dough by the foregoing distance. Dropping rate typically is about g (9.8 m / s2), for example. Shock stability in some additional or alternative aspects can be assessed by subjecting a risen bread dough to horizontal shaking movement at about 630-650 rpm (e.g., ~640 rpm) for about 45-75 seconds (e.g., ~60 seconds) (e.g., on a shaking table). In some aspects, height and / or volume assessments can be done with bread that has been baked using the shocked dough. In some aspects, the height or volume of a shocked risen bread dough (or bread baked therewith) is about, or at least about, 5%, 10%, 15%, 20%, 5-20%, 10- 20%, 15-20%, 5-15%, or 10-15% greater than it would be if the shocked risen bread dough (or shocked baked bread) did not comprise an enzyme as presently disclosed during the dough production method. Shock stability herein can be assessed using any suitable methodology, such as any procedure disclosed in the below Examples (e.g., Example 7 or 10, or with parameters within 5% or 10% of those disclosed in any of these Examples). Yet, in some aspects, increased volume can be with respect to unshocked risen dough (e.g., bread dough), or food product made therewith (e.g., baked bread). Volume herein can be in terms of specific volume (e.g., mL / g), for example, which can optionally be measured with a procedure disclosed in the below Examples (e.g., Example 7, or with parameters within 5% or 10% of those disclosed in this Example). In some aspects, a flour dough or slurry has a viscosity that is increased as compared to the viscosity of a control flour dough or control slurry. Such a viscosity increase can optionally manifest during the mixing step of a dough production method by the dough or slurry exhibiting a torque that is about, or at least about, 2%, 3%, 4%, 5%, 6%, 2-6%, 3-6%, or 4-6% greater than it would be if the dough / slurry did not comprise an enzyme as presently disclosed during the dough / slurry production method. Torque can be measured in Brabender units (BU), for example. Viscosity herein can be assessed using any suitable methodology, such as with a procedure disclosed in the below Examples (e.g., Example 6 or 8, or with parameters within 5% or 10% of those disclosed in any of these Examples). In some aspects, a food product or food dough herein has one or more of the following features as compared to a control food product or control food dough: (I) increased dietary fiber (e.g., increased soluble dietary fiber), (II) increased prebiotic activity, (III) reduced caloric density or reduced calories, and / or (IV) reduced glycemic index. Such beneficial feature(s) (i.e., nutritional / dietary benefit[s]) (which may further include increased satiety), which typically can be realized with ingestion of the food product / dough by a human or other mammal (e.g., primate, pet such as a cat or dog, or livestock such as a pig, cow, horse, goat, sheep), can be improved by at least about 10%, 25%, 50%, or 100%, for example, as compared to when using a control food product / dough product. A suitable control food product / dough typically is the same as the food product / dough, except that the control food product / dough can be one to which an enzyme of the present disclosure was not added. In some aspects, a modified alpha-glucan as presently disclosed can be used as an exogenous ingredient to provide one or more of the foregoing features to a food product or food dough, whereas in some aspects the in situ formation of a modified alpha-glucan provides one or more of the foregoing features to a food product or food dough. A modified alpha-glucan in either of these contexts can optionally be characterized as dietary fiber or soluble dietary fiber, if and as appropriate. Dietary fiber as provided by some aspects of a modified alpha-glucan herein can be of low / reduced digestibility, typically within the human stomach and / or small intestine. Low or reduced digestibility can be a digestibility of less than about 20%, 15%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% as measured by the Association of Analytical Communities (AOAC) method 2009.01 or as disclosed in U.S. Pat. Appl. Publ. No.2017 / 0218093, which are incorporated herein by reference. Modified alpha-glucan of the present disclosure in some alternative and / or additive aspects herein can be comprised in a food ingredient or a food product. Such a food ingredient or food product is not necessarily (but can be) a dough, bakery product, or similar food product / precursor as disclosed herein related to the dough / baking field. Examples of a food ingredient / product in which a modified alpha-glucan herein can be included / used are disclosed in U.S. Pat. Appl. Publ. Nos.2017 / 0198324, 2017 / 0218093, 2018 / 0282385, or 2024 / 0108021, or Int. Pat. Appl. Publ. Nos. WO2023055902, WO2024 / 086560, or WO2024 / 206631, which are incorporated herein by reference. Starch for preparing modified alpha-glucan herein, can be provided as disclosed in Int. Pat. Appl. Publ. No. WO2023 / 114814, for example, which is incorporated herein by reference. In some aspects, starch can be obtained from tubers, roots, stems, legumes, cereals, or whole grain, and / or can be obtained from corn, cobs, sugarcane, sugar beets, wheat, barley, rye, triticale, milo, sago, millet, cassava, tapioca, sorghum, rice, peas, bean, banana, or potatoes. In some aspects, starch can be obtained from a waxy crop such as waxy corn. Starch herein from a grain can be ground or whole, for example, and can optionally further include solids such as corn kernels, bran, and / or cobs. Starch herein can be a highly refined raw starch or feedstock from starch refinery processes. In some aspects, starch can be a crude starch from milled whole grain, which contains non-starch fractions (e.g., germ residues and fibers). Milling typically comprises either wet-milling or dry-milling / grinding. In wet-milling, whole grain is typically soaked in water or dilute acid to separate the grain into its component parts (e.g., starch, protein, germ, oil, kernel fibers). In dry-milling or grinding, whole kernels typically are ground into a fine powder and often processed without fractionating the grain into its component parts. In some aspects, oils and / or fiber from the kernels are recovered. Dry-ground grain thus typically comprises significant amounts of nonstarch carbohydrate compounds, in addition to starch. Starch in some aspects can be hydrolyzed to form a starch hydrolysate, which in turn can be used to prepare modified alpha-glucan herein. A starch hydrolysate can be prepared from any type of starch disclosed herein (e.g., corn starch, or starch from a waxy crop such as waxy corn), for example. Starch hydrolysate can be prepared as disclosed in Int. Pat. Appl. Publ. Nos. WO2001 / 064933 or WO2023 / 114814, for example, which are incorporated herein by reference. In some aspects, a starch hydrolysate for use in producing a modified alpha- glucan comprises (i) dextrin, amylodextrin, and / or maltodextrin, or (ii) dextrin (e.g., mostly dextrin such as ≥ 99 or 99.5 wt% dextrin, or dextrin as comprised in a waxy starch hydrolysate). Some embodiments herein concern a dextrin dextranase or a 4,6-alpha- glucanotransferase as presently disclosed, and compositions comprising one or more of such enzyme(s). In some aspects, a dextrin dextranase or 4,6-alpha-glucanotransferase comprises, or consists of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, and has dextrin dextranase and / or 4,6-alpha-glucanotransferase activity (e.g., GtfB, GtfC, GtfD, or GH31 enzyme activity), as appropriate. Such a composition typically is isolated herein and consequently non-naturally occurring. A 4,6-alpha-glucanotransferase enzyme (e.g., GtfD enzyme) can be a modified / variant enzyme as disclosed herein, for example. A dextrin dextranase or 4,6-alpha-glucanotransferase, and / or a nucleotide sequence encoding any of the enzymes, in some aspects can be one that does not naturally occur (its sequence is not 100% identical to a naturally occurring sequence). A composition comprising a dextrin dextranase or a 4,6-alpha-glucanotransferase in some aspects can optionally be characterized as a reaction composition, which initially comprises (in addition to one or more of the foregoing enzyme[s]) at least water and an alpha-1,4-glucan substrate. Such a substrate can be any alpha-1,4-glucan as disclosed herein, such as starch (which comprises amylose and / or amylopectin), dextrin, amylodextrin, maltodextrin, and / or MOS. Conditions and parameters for preparing and conducting a reaction composition (e.g., enzyme content, reaction solids and water content, reaction time duration, temperature) can be any of those as disclosed in a food dough production method, for example. A product of a reaction composition herein can be as disclosed herein for modified alpha-glucan, for example. Some embodiments disclosed herein concern a polynucleotide comprising a nucleotide sequence that encodes a dextrin dextranase or 4,6-alpha-glucanotransferase as presently disclosed (e.g., one that comprises, or consists of, an amino acid sequence that is about, or at least about, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 98.5%, 99%, 99.5%, or 100% identical to SEQ ID NO:1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148). In some aspects, such a polynucleotide sequence comprises, or consists of, a nucleotide sequence that is 100% identical to, or that is at least 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to, SEQ ID NO:55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, or 81. Optionally, one or more regulatory sequences are operably linked to the nucleotide sequence, and preferably a promoter sequence is included as a regulatory sequence. A polynucleotide comprising a nucleotide sequence encoding a dextrin dextranase or 4,6-alpha-glucanotransferase herein can be a vector or construct useful for transferring a nucleotide sequence into a cell, for example. Examples of a suitable vector / construct can be selected from a plasmid, yeast artificial chromosome (YAC), cosmid, phagemid, bacterial artificial chromosome (BAC), virus, or linear DNA (e.g., linear PCR product). A polynucleotide sequence in some aspects can be capable of existing transiently (i.e., not integrated into the genome) or stably (i.e., integrated into the genome) in a cell. A polynucleotide sequence in some aspects can comprise, or lack, one or more suitable marker sequences (e.g., selection or phenotype marker). A polynucleotide sequence in some aspects can comprise one or more regulatory sequences operably linked to the nucleotide sequence encoding a dextrin dextranase or 4,6- alpha-glucanotransferase. For example, a nucleotide sequence encoding a dextrin dextranase or 4,6-alpha-glucanotransferase may be in operable linkage with a promoter sequence (e.g., a heterologous promoter). A promoter sequence can be suitable for expression in a cell (e.g., bacterial cell such as E. coli or Bacillus; eukaryotic cell such as a fungus, yeast, insect, or mammalian cell) or in an in vitro protein expression system, for example. Examples of other suitable regulatory sequences include transcription terminator sequences. Some aspects herein are drawn to a cell comprising a polynucleotide sequence as presently disclosed; such a cell can be any type disclosed herein (e.g., bacterial cell such as E. coli or Bacillus; eukaryotic cell such as a fungus, yeast, insect, or mammalian cell). A cell can optionally express a dextrin dextranase or 4,6-alpha-glucanotransferase encoded by the polynucleotide sequence. In some aspects, the polynucleotide sequence exists transiently (i.e., not integrated into the genome) or stably (i.e., integrated into the genome) in the cell. Non-limiting examples of compositions / products and methods / processes disclosed herein include: 1. A method (process) of producing a food dough (flour dough or flour slurry), the method comprising: mixing at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase (e.g., the enzyme is an isolated enzyme [e.g., it is not endogenous to the flour or meal]), thereby producing a food dough, optionally wherein: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough) (optionally wherein the food dough has an increased shock stability as measured according to instant Example 7 or 10), (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough) (optionally wherein the food dough has an increased viscosity as measured with a farinograph, such as described in instant Example 8), and / or (c) the food dough has a water- binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough). 2. The method of embodiment 1, wherein the enzyme is the dextrin dextranase. 3. The method of embodiment 1, wherein the enzyme is the 4,6-alpha- glucanotransferase. 4. The method of embodiment 3, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase (or is a GtfB, GtfC, or GtfD glucanotransferase). 5. The method of embodiment 1, 2, 3, or 4, wherein the enzyme comprises an amino acid sequence that is at least about 40%, 50%, 60%, 70%, 80%, or 90% (e.g., ≥ ~90% or 95%) identical to SEQ ID NO:1 (optionally to SEQ ID NO:28), 2 (optionally to SEQ ID NO:29), 3 (optionally to SEQ ID NO:30), 4 (optionally to SEQ ID NO:31), 5 (optionally to SEQ ID NO:32), 6 (optionally to SEQ ID NO:33), 7 (optionally to SEQ ID NO:34), 8 (optionally to SEQ ID NO:35), 9 (optionally to SEQ ID NO:36), 10 (optionally to SEQ ID NO:37), 11 (optionally to SEQ ID NO:38), 12 (optionally to SEQ ID NO:39), 13 (optionally to SEQ ID NO:40), 14 (optionally to SEQ ID NO:41), 15 (optionally to SEQ ID NO:42), 16 (optionally to SEQ ID NO:43), 17 (optionally to SEQ ID NO:44), 18 (optionally to SEQ ID NO:45), 19 (optionally to SEQ ID NO:46), 20 (optionally to SEQ ID NO:47), 21 (optionally to SEQ ID NO:48), 22 (optionally to SEQ ID NO:49), 23 (optionally to SEQ ID NO:50), 24 (optionally to SEQ ID NO:51), 25 (optionally to SEQ ID:52), 26 (optionally to SEQ ID:53), 27 (optionally to SEQ ID:54), 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6-alpha-glucanotransferase enzyme according to embodiment 38, 39, 39a, 39b, 39c, 39d, 39e, 39f, 39g, or 39h. 6. The method of embodiment 1, 2, 3, 4, or 5, wherein the flour is used in the method, optionally wherein the flour is wheat flour (e.g., soft wheat flour). 7. The method of embodiment 1, 2, 3, 4, 5, or 6, further comprising: processing the food dough into a food. 8. The method of embodiment 7, wherein the processing comprises at least baking, frying, boiling, drying, chilling, extruding, and / or flattening the food dough. 9. The method of embodiment 1, 2, 3, 4, 5, 6, 7, or 8, wherein the food dough comprises a leavening agent, optionally wherein the leavening agent is yeast. 10. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, or 9, wherein the food dough is a bread dough. 11. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10, further comprising allowing the food dough to rise, thereby providing risen food dough. 12. The method of embodiment 11, wherein the risen food dough is risen bread dough, optionally wherein the volume of the risen bread dough is at least 5% greater than it would be if the risen bread dough did not comprise the enzyme, wherein optionally the risen bread dough has not been shocked, or optionally the risen bread dough has been shocked. 13. The method of embodiment 11 or 12, further comprising dropping the risen bread dough (or risen food dough) at least one time over a distance of at least 1 cm, wherein, following the dropping, the volume of the risen bread dough (or risen food dough) is at least 2% greater than it would be if the risen bread dough (or risen food dough) did not comprise the enzyme (or wherein the method of embodiment 11 or 12 further comprises applying a shock stability test according to instant Example 7 or 10). 14. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13, wherein the mixing exhibits a torque that is at least 2% greater than it would be if the food dough did not comprise the enzyme (optionally wherein the torque is measured according to instant Example 6 or 8). 15. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, or 14, wherein the weight-average degree of polymerization (DPw) of gluco-oligosaccharides of the food dough is increased by at least 1 as compared to the DPw of gluco-oligosaccharides of the flour or meal before the mixing. 16. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15, wherein the alpha-1,4 glycosidic linkage content of the alpha-1,4-glucan (e.g., starch, amylose, amylopectin, dextrin, amylodextrin, and / or maltodextrin) of the food dough is reduced as compared to the alpha-1,4 glycosidic linkage content of the alpha-1,4-glucan of the flour or meal before the mixing, typically wherein the alpha-1,4-glucan of the food dough has an increased content of alpha-1,6 and / or alpha-1,3 glycosidic linkages (and / or sometimes alpha- 1,2 glycosidic linkages) as compared to the alpha-1,6 and / or alpha-1,3 glycosidic linkage content (and / or sometimes alpha-1,2 glycosidic linkage content) of the alpha-1,4-glucan of the flour or meal before the mixing (i.e., the alpha-1,4-glucan is now a modified alpha-glucan as presently disclosed). 17. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16, wherein the flour has a gluten content that is less than about 12 wt% (e.g., gluten-free). 18. The method of embodiment 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, or 17, further comprising adding at least one of a lipase, alpha-amylase, xylanase, non-maltogenic exoamylase, glucoamylase, glucose oxidase, or hexose oxidase during production of the food dough (e.g., such added enzyme can be added during the mixing step) (e.g., such added enzyme is an isolated enzyme [e.g., it is not endogenous to the flour or meal]) (e.g., the nonmaltogenic exoamylase is capable of hydrolyzing starch by cleaving off one or more linear malto-oligosaccharides from the starch). 19. A food dough produced by the method of embodiment 1, 2, 3, 4, 5, 6, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18. 20. A food product produced by the method of embodiment 7 or 8, and / or as produced using a food dough of embodiment 19 or 29 (e.g., a baked food such as baked bread). 21. A food dough comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, optionally wherein: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough) (optionally wherein the food dough has an increased shock stability according to instant Example 7 or 10), (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough) (optionally wherein the food dough has an increased viscosity as measured with a farinograph, such as described in instant Example 8), and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks the enzyme (e.g., the control food dough is produced the same way as the food dough, except that the enzyme is not included in producing the control food dough). 22. The food dough of embodiment 21, wherein the enzyme is the dextrin dextranase. 23. The food dough of embodiment 21, wherein the enzyme is the 4,6-alpha- glucanotransferase. 24. The food dough of embodiment 23, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase (or is a GtfB, GtfC, or GtfD glucanotransferase). 25. The food dough of embodiment 21, 22, 23, or 24, wherein the enzyme comprises an amino acid sequence that is at least 90% (e.g., ≥95%) identical to SEQ ID NO:1 (optionally to SEQ ID NO:28), 2 (optionally to SEQ ID NO:29), 3 (optionally to SEQ ID NO:30), 4 (optionally to SEQ ID NO:31), 5 (optionally to SEQ ID NO:32), 6 (optionally to SEQ ID NO:33), 7 (optionally to SEQ ID NO:34), 8 (optionally to SEQ ID NO:35), 9 (optionally to SEQ ID NO:36), 10 (optionally to SEQ ID NO:37), 11 (optionally to SEQ ID NO:38), 12 (optionally to SEQ ID NO:39), 13 (optionally to SEQ ID NO:40), 14 (optionally to SEQ ID NO:41), 15 (optionally to SEQ ID NO:42), 16 (optionally to SEQ ID NO:43), 17 (optionally to SEQ ID NO:44), 18 (optionally to SEQ ID NO:45), 19 (optionally to SEQ ID NO:46), 20 (optionally to SEQ ID NO:47), 21 (optionally to SEQ ID NO:48), 22 (optionally to SEQ ID NO:49), 23 (optionally to SEQ ID NO:50), 24 (optionally to SEQ ID NO:51), 25 (optionally to SEQ ID:52), 26 (optionally to SEQ ID:53), 27 (optionally to SEQ ID:54), 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6-alpha-glucanotransferase enzyme according to embodiment 38, 39, 39a, 39b, 39c, 39d, 39e, 39f, 39g, or 39h. 26. The food dough of embodiment 21, 22, 23, 24, or 25, wherein the food dough comprises the flour, optionally wherein the flour is wheat flour. 27. The food dough of embodiment 21, 22, 23, 24, 25, or 26, wherein the food dough comprises a leavening agent, optionally wherein the leavening agent is yeast. 28. The food dough of embodiment 21, 22, 23, 24, 25, 26, or 27, wherein the food dough is a bread dough. 29. The food dough of embodiment 21, 22, 23, 24, 25, 26, 27, or 28, wherein food dough is a risen food dough. 30. A food product (e.g., according to embodiment 20) comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, optionally wherein the food product has a water- binding capacity that is increased as compared to the water-binding capacity of a control food product that lacks the enzyme (e.g., the control food product is produced the same way as the food product, except that the enzyme is not included in producing the control food product). 31. The food product of embodiment 30, wherein the enzyme is the dextrin dextranase. 32. The food product of embodiment 30, wherein the enzyme is the 4,6-alpha- glucanotransferase. 33. The food product of embodiment 32, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase (or is a GtfB, GtfC, or GtfD glucanotransferase). 34. The food product of embodiment 30, 31, 32, or 33, wherein the food product is a baked food product. 35. The food product of embodiment 34, wherein the baked food product is bread. 36. The food product of embodiment 30, 31, 32, 33, 34, or 35, wherein, as compared to a control food product that lacks said enzyme, the food product has one or more of the following features: (I) increased dietary fiber (e.g., increased dietary soluble fiber), (II) increased prebiotic activity, (III) reduced caloric density or reduced calories, (IV) reduced glycemic index, and / or (V) reduced digestibility (typically by virtue of comprising increased dietary fiber herein). 37. An enzyme (isolated enzyme) selected from a dextrin dextranase or a 4,6-alpha- glucanotransferase, wherein the enzyme comprises an amino acid sequence that is at least about 90% (e.g., ≥95%) identical to SEQ ID NO:1 (optionally to SEQ ID NO:28), 2 (optionally to SEQ ID NO:29), 3 (optionally to SEQ ID NO:30), 4 (optionally to SEQ ID NO:31), 5 (optionally to SEQ ID NO:32), 6 (optionally to SEQ ID NO:33), 7 (optionally to SEQ ID NO:34), 8 (optionally to SEQ ID NO:35), 9 (optionally to SEQ ID NO:36), 10 (optionally to SEQ ID NO:37), 11 (optionally to SEQ ID NO:38), 12 (optionally to SEQ ID NO:39), 13 (optionally to SEQ ID NO:40), 14 (optionally to SEQ ID NO:41), 15 (optionally to SEQ ID NO:42), 16 (optionally to SEQ ID NO:43), 17 (optionally to SEQ ID NO:44), 18 (optionally to SEQ ID NO:45), 19 (optionally to SEQ ID NO:46), 20 (optionally to SEQ ID NO:47), 21 (optionally to SEQ ID NO:48), 22 (optionally to SEQ ID NO:49), 23 (optionally to SEQ ID NO:50), 24 (optionally to SEQ ID NO:51), 25 (optionally to SEQ ID:52), 26 (optionally to SEQ ID:53), 27 (optionally to SEQ ID:54), 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, optionally wherein the enzyme is comprised in an isolated composition (e.g., a food dough or food product, such as recited in any of the foregoing embodiments or as disclosed herein) comprising a modified alpha-glucan as presently disclosed. 38. A modified (non-native, variant) 4,6-alpha-glucanotransferase enzyme (e.g., GtfD glucanotransferase) (an isolated 4,6-alpha-glucanotransferase enzyme), wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22, wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% (e.g., ≥ about 50%, 60%, 70%, 80%, or 90%) identical to SEQ ID NO:22, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme produces (is capable of producing) a modified alpha-glucan (e.g., as recited in embodiment 16; and / or under suitable enzyme reaction conditions herein) at a yield that is higher (e.g., at least about 10%, 25%, 50%, 100%, 150%, or 200% higher) than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. 39. The modified 4,6-alpha-glucanotransferase enzyme of embodiment 38, wherein the amino acid substitution is with the Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue (or is with the Ile, Leu, Val, Gly, or Ala residue), optionally wherein the modified 4,6-alpha- glucanotransferase enzyme comprises (i) the amino acid sequence of SEQ ID NO:86, 87, 88, 89, 90, 91, 112, 114, 115, 117, 118, 121, 122, 123, or 124 (e.g., SEQ ID NO:86, 87, 89, 90, 91, 112, 114, 115, 117, 118, 121, 122, 123, or 124) (e.g., SEQ ID NO:86, 87, 89, 90, or 91) (e.g., SEQ ID NO:86), or (ii) an amino acid sequence that is at least about 40%, 50%, 60%, 70%, 80%, 90%, or 95% identical to the amino acid sequence of (i). 39a. A modified (non-native, variant) 4,6-alpha-glucanotransferase enzyme (e.g., GtfD glucanotransferase) (an isolated 4,6-alpha-glucanotransferase enzyme), wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23, wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% (e.g., ≥ about 50%, 60%, 70%, 80%, 90%, or 95%) identical to SEQ ID NO:23, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme produces (is capable of producing) a modified alpha-glucan (e.g., as recited in embodiment 16; and / or under suitable enzyme reaction conditions herein) at a yield that is higher (e.g., at least about 10%, 25%, 50%, 100%, 150%, or 200% higher) than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. 39b. The modified 4,6-alpha-glucanotransferase enzyme of embodiment 39a, wherein the amino acid substitution is with the Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue (or is with the Ile, Leu, Val, Gly, or Ala residue), optionally wherein the modified 4,6-alpha- glucanotransferase enzyme comprises the amino acid sequence of SEQ ID NO:87. 39c. A modified (non-native, variant) 4,6-alpha-glucanotransferase enzyme (e.g., GtfD glucanotransferase) (an isolated 4,6-alpha-glucanotransferase enzyme), wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83, wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% (e.g., ≥ about 50%, 60%, 70%, 80%, 90%, or 95%) identical to SEQ ID NO:83, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme produces (is capable of producing) a modified alpha-glucan (e.g., as recited in embodiment 16; and / or under suitable enzyme reaction conditions herein) at a yield that is higher (e.g., at least about 10%, 25%, 50%, 100%, 150%, or 200% higher) than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. 39d. The modified 4,6-alpha-glucanotransferase enzyme of embodiment 39c, wherein the amino acid substitution is with the Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue (or is with the Ile, Leu, Val, Gly, or Ala residue), optionally wherein the modified 4,6-alpha- glucanotransferase enzyme comprises the amino acid sequence of SEQ ID NO:89. 39e. A modified (non-native, variant) 4,6-alpha-glucanotransferase enzyme (e.g., GtfD glucanotransferase) (an isolated 4,6-alpha-glucanotransferase enzyme), wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:84, wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% (e.g., ≥ about 50%, 60%, 70%, 80%, 90%, or 95%) identical to SEQ ID NO:84, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme produces (is capable of producing) a modified alpha-glucan (e.g., as recited in embodiment 16; and / or under suitable enzyme reaction conditions herein) at a yield that is higher (e.g., at least about 10%, 25%, 50%, 100%, 150%, or 200% higher) than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. 39f. The modified 4,6-alpha-glucanotransferase enzyme of embodiment 39e, wherein the amino acid substitution is with the Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue (or is with the Ile, Leu, Val, Gly, or Ala residue), optionally wherein the modified 4,6-alpha- glucanotransferase enzyme comprises the amino acid sequence of SEQ ID NO:90. 39g. A modified (non-native, variant) 4,6-alpha-glucanotransferase enzyme (e.g., GtfD glucanotransferase) (an isolated 4,6-alpha-glucanotransferase enzyme), wherein the modified 4,6-alpha-glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:85, wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue (or is with an Ile, Leu, Val, Gly, or Ala residue [e.g., Ile residue]), and (ii) comprises an amino acid sequence that is at least about 40% (e.g., ≥ about 50%, 60%, 70%, 80%, 90%, or 95%) identical to SEQ ID NO:85, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme produces (is capable of producing) a modified alpha-glucan (e.g., as recited in embodiment 16; and / or under suitable enzyme reaction conditions herein) at a yield that is higher (e.g., at least about 10%, 25%, 50%, 100%, 150%, or 200% higher) than the yield of the modified alpha-glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position. 39h. The modified 4,6-alpha-glucanotransferase enzyme of embodiment 39g, wherein the amino acid substitution is with the Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue (or is with the Ile, Leu, Val, Gly, or Ala residue), optionally wherein the modified 4,6-alpha- glucanotransferase enzyme comprises the amino acid sequence of SEQ ID NO:91. 40. A polynucleotide (isolated polynucleotide) comprising a nucleotide sequence encoding an enzyme according to embodiment 37, 38, 39, 39a, 39b, 39c, 39d, 39e, 39f, 39g, or 39h, optionally wherein one or more regulatory sequences are operably linked to the nucleotide sequence, and preferably wherein the one or more regulatory sequences include a promoter sequence. 41. A food ingredient comprising a modified alpha-glucan (e.g., as recited in embodiment 16), or a food product comprising said food ingredient (i.e., the food product comprises the modified alpha-glucan), wherein the modified alpha-glucan is produced by providing a composition (reaction composition) comprising at least (i) water, (ii) an alpha-1,4-glucan substrate (e.g., starch, amylose, amylopectin, dextrin, amylodextrin, and / or maltodextrin), and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase (e.g., the enzyme is an isolated enzyme) (under suitable reaction conditions herein [e.g., temperature, pH, time] allowing for the enzyme to modify the alpha-1,4-glucan substrate) (i.e., the modified alpha-glucan is produced in a method / process comprising contacting at least the alpha-1,4-glucan substrate with the enzyme under suitable aqueous reaction conditions). 42. The food ingredient or food product of embodiment 41, wherein the enzyme is the dextrin dextranase. 43. The food ingredient or food product of embodiment 41, wherein the enzyme is the 4,6-alpha-glucanotransferase. 44. The food ingredient or food product of embodiment 43, wherein the 4,6-alpha- glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase (or is a GtfB, GtfC, or GtfD glucanotransferase). 45. The food ingredient or food product of embodiment 41, 42, 43, or 44, wherein the enzyme comprises an amino acid sequence that is at least 90% (e.g., ≥95%) identical to SEQ ID NO:1 (optionally to SEQ ID NO:28), 2 (optionally to SEQ ID NO:29), 3 (optionally to SEQ ID NO:30), 4 (optionally to SEQ ID NO:31), 5 (optionally to SEQ ID NO:32), 6 (optionally to SEQ ID NO:33), 7 (optionally to SEQ ID NO:34), 8 (optionally to SEQ ID NO:35), 9 (optionally to SEQ ID NO:36), 10 (optionally to SEQ ID NO:37), 11 (optionally to SEQ ID NO:38), 12 (optionally to SEQ ID NO:39), 13 (optionally to SEQ ID NO:40), 14 (optionally to SEQ ID NO:41), 15 (optionally to SEQ ID NO:42), 16 (optionally to SEQ ID NO:43), 17 (optionally to SEQ ID NO:44), 18 (optionally to SEQ ID NO:45), 19 (optionally to SEQ ID NO:46), 20 (optionally to SEQ ID NO:47), 21 (optionally to SEQ ID NO:48), 22 (optionally to SEQ ID NO:49), 23 (optionally to SEQ ID NO:50), 24 (optionally to SEQ ID NO:51), 25 (optionally to SEQ ID:52), 26 (optionally to SEQ ID:53), 27 (optionally to SEQ ID:54), 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6- alpha-glucanotransferase enzyme according to embodiment 37, 38, 39, 39a, 39b, 39c, 39d, 39e, 39f, 39g, or 39h. 46. The food ingredient or food product of embodiment 41, 42, 43, 44, or 45, wherein the alpha-1,4-glucan substrate comprises starch, amylose, and / or amylopectin. 47. The food ingredient or food product of embodiment 41, 42, 43, 44, 45, or 46, wherein the alpha-1,4-glucan substrate comprises a starch hydrolysate, dextrin, amylodextrin, and / or maltodextrin. 48. The food ingredient or food product of embodiment 41, 42, 43, 44, 45, 46, or 47, wherein, as compared to a control food ingredient or control food product that lacks said enzyme, the food ingredient or food product has one or more of the following features: (I) increased dietary fiber (e.g., dietary soluble fiber), (II) increased prebiotic activity, (III) reduced caloric density or reduced calories, (IV) reduced glycemic index, and / or (V) reduced digestibility (typically by virtue of comprising increased dietary fiber herein). EXAMPLES The present disclosure is described in further detail in the following examples, which are not in any way intended to limit the scope of the disclosure. The attached figures are meant to be considered as integral parts of the specification and description of the disclosure. The following examples are offered to illustrate, but not to limit, the present disclosure. Example 1. Cloning and transformation of candidate glucosyltransferase and dextrin dextranase sequences Glucosyltransferase (Gtf) and dextrin dextranase (DDase) were sourced either from public databases (such as NCBI) or from internal genomic data (see Table 1). Typically, the bacterial Gtf or DDase genes that encode mature peptides were codon-optimized according to the codon preferences of Bacillus subtilis and subsequently cloned into the p2 / 3JM vector (Vogtentanz, Protein Expr Purif.55:40-52, 2007). The AprE promoter and a signal peptide were employed to facilitate transcription and secretion of the proteins. To aid in purification, six histidine residues (6-His tag) were included at either the N- or C-terminus of each gene. The resulting plasmid was then subjected to rolling-circle amplification and transformed into a B. subtilis host. For expression in E. coli BL21, the genes were codon-optimized for E. coli and subcloned into the pET28b(+) vector. Example 2. Expression of candidate glucosyltransferase and dextrin dextranase enzymes B. subtilis transformants thereof were streaked on LB plates supplemented with 5 ppm chloramphenicol. Each colony was inoculated into 20 mL LB medium with 5 ppm chloramphenicol in a 250-mL shake flask for seed growth. Well-grown cells were inoculated into 350 mL enriched semi-defined media based on MOPS buffer, with urea, micronutrients, maltodextrin and soytone for robust cell growth. Culture supernatant was harvested by centrifugation and / or filtration, and then concentrated. E.coli BL21 transformants were streaked onto LB plates supplemented with 50 ppm kanamycin. Each colony was inoculated into 20 mL LB medium with 50 ppm kanamycin in a 250-mL shake flask for seed growth. 2% well-grown cells were inoculated into 300 mL TB medium supplemented with 50 ppm kanamycin in a 3-L ultra-yield shake flask and incubated at 37 °C with vigorous shaking at 220 rpm for about 3 hours until OD 600 was 0.6-0.8 and then the temperature was lowered to 20 °C and IPTG added to final concentration of 80 ppm. After incubating each strain for 16 hours, cell pellets were gathered and preserved at -80 °C for subsequent purification. Example 3. Purification of candidate glucosyltransferase and dextrin dextranase enzymes The fermentation broth of B. subtilis was loaded onto a 5-mL Ni Sepharose FF column (GE Healthcare) at 5 mL / min. The column was washed sequentially with 25 mL buffer A (20 mM Tris pH 7.5, 150 mM NaCl, 10 mM imidazole) and 50 mL buffer B (20 mM Tris pH 7.5, 150 mM NaCl, 30 mM imidazole) at 5 mL / min. The column was eluted with 30 mL buffer C (20 mM Tris pH 7.5, 150 mM NaCl, 300 mM imidazole). The pooled sample was concentrated and the buffer was changed to buffer D (20 mM Tris pH 7.5, 150 mM NaCl) using a 30 kDa MWCO Amicon Ultra centrifugal filter (Millipore). Glycerol was added to the sample to achieve a final concentration of 40% (w / v). The samples were then stored at -20 °C for long-term preservation. The cell pellet of BL21 was suspended in 100 mL of cell lysis buffer (50 mM Tris pH 7.5, 100 mM NaCl, 5% glycerol, 1 U / mL lysozyme, 25 U / mL nuclease). The sonication method was used to disrupt the cells, with a power of 400 W and a working time of 3 seconds followed by a pause of 3 seconds for 20 minutes. The resulting cell debris was removed by centrifugation at 15000 rpm for 1 hour. The BL21 supernatant was purified using similar steps as B. subtilis. Example 4. Action pattern of candidate GTF-like enzymes on maltoheptaose and amylose The action pattern of candidate GTF-like enzymes (including DDase, GtfB, GtfC, GtfD, and GH31 glucanotransferase) prepared above was investigated by HPLC analysis of the products formed from maltoheptaose (DP7) and amylose combined with three different types of alpha-glucan hydrolyzing enzyme treatments. The detailed methods are described as follows. 1. Preparation of DP7 and amylose substrates. The DP7 substrate was prepared by dissolving DP7 (maltoheptaose, Hayashibara) in MILLI- Q water to a concentration of 8% (w / v). To prepare the amylose substrate, 0.4 g of amylose (A0512, Sigma-Aldrich) was added to 10 mL of 2 M NaOH solution to create a 4% (w / v) stock solution. The solution was vortexed to dissolve, and the pH of the stock solution was adjusted to neutral using 4 M HCl. The total volume of the solution was then brought to 20 mL with MILLI-Q water. The solution was freshly prepared each time before use. 2. Incubation of DP7 and amylose substrates with GTF-like enzymes. 250 µL / well of the above substrate solution and 500 µL / well of 20 mM MES buffer (4- morpholinoethanesulfonic acid, pH 6.0) were transferred into a 96-deepwell reaction plate (BioScience, China) using a Biomek i-7 Automated Workstation (Beckman, USA). Purified GTF-like enzymes were first diluted in glycerol (40%, w / v) with 100 mM NaCl to a final concentration of 1 mg / mL. The protein concentration of diluted enzyme samples was further quantified by examining the absorbance at 280 nm using BSA as standard. Then, the concentrations of enzyme samples were normalized to 200 µg / mL using MILLI-Q water, respectively. Each reaction was initiated by transferring 250 µL / well of the normalized enzyme solution into the reaction plate. 100 µg / mL of ampicillin was included in the reaction system to protect the mixture from microbial contamination. The reaction plates were then sealed and incubated in a ThermoMixer®(Eppendorf, Germany) at 37 °C and 650 rpm for 1, 2, 4, 6, 24, or 48 hours. At each end-of-time period, 150 µL / well of reaction mixture was taken out of the reaction plate and heated at 100 °C for 20 minutes to stop the reaction. 3. Enzymatic treatment on the product of GTF-like enzymes. The above terminated reaction mixtures (product of GTF-like enzymes) were subsequently treated with different types of alpha-glucan / dextran hydrolyzing enzymes, as follows: (1) GA / AA treatment: exohydrolysis of alpha-(1→4)-D-glycosidic linkages by glucoamylase combined with endohydrolysis of alpha-(1→4)-D-glycosidic linkages by alpha-amylase (Bacillus licheniformis); (2) DexA treatment: endohydrolysis of alpha-(1→6)-D-glycosidic linkages by dextranase (Trichoderma reesei); (3) PulA treatment: debranching of alpha- (1→6)-D-glycosidic bonds by pullulanase (Bacillus subtilis); or (4) no treatment: control group in which the enzyme solution was replaced by MILLI-Q water. The procedure was as follows: 25 µL / well of the GTF product was incubated with GA (50 µg / mL) / AA (2 µg / mL) containing 2 mM CaCl2; DexA (50 µg / mL); PulA (50 µg / mL); or MILLI-Q water, with each treatment having 10 mM MES buffer (pH 6.0) in a total of 100 µL / well (Corning 3641) at 50 °C and 650 rpm (ThermoMixer®) for 1 hour. At the end of incubation, each reaction mixture was diluted 5 times using MILLI-Q water and filtered through a 0.2-µm filter plate (Corning 3505). All liquid handling was performed with a Biomek i7 Automated Workstation (Beckman, USA). 4. HPLC analysis. Aliquots of the above filtered reaction mixture were analyzed by HPLC (Agilent 1200 series, USA) using an Aminex HPX-42A column (Bio-Rad, USA), run at 80 °C. 10 ^L samples were loaded on the column and separated with an isocratic gradient of MILLI-Q water as the mobile phase at a flow rate of 0.6 mL / min. The oligosaccharide products were detected using a refractive index detector (RID), and the standards were run to determine elution times of each DP(n) sugar of interest (DP1 ~ DP7). Results The results shown in Table 2 and FIGs.1-28 demonstrated that candidate GTF-like enzymes were able to hydrolyze DP7 and transfer the released glucose to form various products (solid line in FIGs.1-28). The subsequent enzymatic treatments further revealed the product linkage profiles. The decrease in HPLC signal following GA / AA treatment (shown as the long-dash line in the figures) indicated the presence of alpha-1,4 linkage. Similarly, the decrease in the related HPLC signal following DexA treatment (represented by the large-dot line) suggested the presence of alpha-1,6 linkage, while the decrease in the related HPLC signal following PulA treatment (depicted by the small-dot line) indicated the potential presence of alpha-1,6 branch points. The study provides valuable insights into the action pattern of GTF-like enzymes and their potential applications. Table 2. Summary of action patterns of candidate GTF-like enzymes on DP7 or amylose as substrate Example 5. Protein determination method Protein was quantified by SDS-PAGE gel and densitometry using Gel Doc™ EZ imaging system. Reagents used in the assay: Concentrated (2x) Laemmli Sample Buffer (Bio-Rad, Catalogue #161-0737); 26-well XT 4-12% Bis-Tris Gel (Bio-Rad, Catalogue #345- 0125); protein markers “Precision Plus Protein Standards” (Bio-Rad, Catalogue #161-0363); protein standard BSA (Thermo Scientific, Catalogue #23208) and SimplyBlue Safestain (Invitrogen, Catalogue #LC 6060. The assay was carried out as follow: In a 96-well PCR plate, 50 µL diluted enzyme sample was mixed with 50 µL sample buffer containing 2.7 mg DTT. The plate was sealed with Microseal ‘B’ Film from Bio-Rad and was placed into a PCR machine to be heated to 70 °C for 10 minutes. After that, the chamber was filled with running buffer, and the gel cassette was set. Then, 10 µL of each sample and standard (0.125-1.00 mg / mL BSA) was loaded on the gel and 5 µL of the markers was loaded. After that, the electrophoresis was run at 200 V for 45 minutes. Following electrophoresis, the gel was rinsed 3 times for 5 minutes in water, then stained in Safestain overnight and finally destained in water. Then the gel was transferred to Imager. Image Lab software was used for calculation of intensity of each band. A calibration curve was made using BSA (Thermo Scientific, Catalogue #23208) and the amount of the target protein was determined by the band intensity and calibration curve. The protein quantification method was employed to prepare enzyme samples used in subsequent Examples. Example 6. Viscosity assays using Gilson Viscoman in wheat flour slurry A buffered wheat flour system with 30% by weight dry solids (DS) was used to evaluate viscosity development for various candidate starch-acting enzymes. For this assay, a Gilson Viscoman PIPETMAN from Biolab A / S (Denmark) was used to determine the viscosity in slurry of each sample at 20 ^C. Flour: SOFT wheat flour from Valsemøllen A / S (280844 Hvedemel Soft NATURAKS 25, Esbjerg, Denmark, 10% protein) with a water content of 14% was used for the tests. Buffer: 0.1 M Sodium Acetate Buffer pH 5.2 was made by dissolving 9.57 g of sodium acetate (trihydrate) in 800 mL of MILLI-Q water followed by adjusting the pH to 5.2 with concentrated acetic acid while stirring. Q.S. to 1.0 L with MILLI-Q water and stored refrigerated in a closed container for up to 1 month. 3.0 g of SOFT wheat flour was mixed with 10.0 mL 0.1 M Sodium Acetate Buffer pH 5.2 in small Wheaton glass containers with caps and incubated with magnetic stirring (150 rpm) in a dry bath at 30 ^C for 20 minutes to get complete homogenous flour slurry. The viscosity of all solutions was determined with Viscoman (cP) at 0 minutes prior to enzyme addition at 20 ^C as average of duplicate analysis. A starch-acting GTF-like enzyme was added according to protein amount as determined according to Example 5, LEI2176 (EacGtf1 SEQ ID NO:27) 7.4 mg / mL. The addition of starch-acting GTF-like enzyme sample is given in % of amount flour in slurry (Bakers percentage) in Table 3. Enzyme reaction mixtures were prepared and incubated 30 ^C with magnetic stirring (150 rpm) in a dry-block. Viscosity was determined for each enzyme reaction after 20, 40, 65, 120 and 160 minutes. Results for increasing dosage of GTF-C, LEI2176 (EacGtf1, SEQ ID NO:27) are shown in FIG.35. It was clear that viscosity of the buffered flour slurry without any added enzyme gradually showed minor decrease upon incubation at 30 ^C, from 17.9 cP to 15 cP. Addition of GTF-C, LEI2176 (EacGtf1 SEQ ID NO:27), to the buffered flour slurry clearly increased viscosity of the solution with increasing dosage of the GTF sample. Highest viscosity when using GTF-C, LEI2176 (EacGtf1 SEQ ID NO:27) was obtained after 40 minutes of using the highest tested dose of 74 ppm, suggesting that higher viscosities potentially could be obtained by optimizing incubation time and / or enzyme dose. Prolonged incubation to 120 and 160 minutes with the highest tested dose of 74 ppm GTF-C, LEI2176 (EacGtf1 SEQ ID NO:27) led to lower viscosity. Table 3. Protein candidate GTF-like enzyme addition according to flour in wheat flour slurry as given by Baker percentage. * Each wheat flour slurry consisted of 3.0 g SOFT hvedemel flour mixed with 10 mL 0.1 M sodium acetate buffer pH 5.2. Example 7. Determination of specific volumes of wheat dough punched rolls using candidate starch-acting GTF-like enzymes using a shaking table shock test Soft wheat flour (Valsemøllen, Esbjerg Denmark, 10% protein) with an initial water content of 14% was tempered to 44 °C in a heating cabinet. 300 g tempered soft flour, 1% salt, 1.6% sugar, 2% dry yeast (SAF instant Yeast, S. I. Lesaffre, France), 50 ppm Grindamyl A1000 (IFF, Brabrand, Denmark) and 0.125% Enovera^ 3001 (enzyme complex of lipase, amylase, xylanase and oxidase to provide increased bread volume provided by IFF, Brabrand, Denmark) were all mixed in a Kitchen Aid mixer (Artisan 5KSM125, Kitchen Aid, MI, USA) for 1 minute, then 55.5% water tempered to 44 °C (and enzyme) was added and mixed at low speed for 2 minutes followed by high speed for 8 minutes. The dough was then placed at 34 °C, 86% humidity in a proofing cabinet (Bago-raskeskab BMR-77, Bago-Line, Faaborg, Denmark) for 10 minutes. Eight 25.0-g dough samples were rolled out by rolling pin and round forms (4 cm in diameter) were punched and placed in silicone muffin molds on baking sheets with 8 rolls per sheet. Weight of doughs were determined. Next, the rounded doughs were proofed at 34 °C, 86% humidity for 45 minutes exactly. The rounded rolls on one of the two baking sheets (one for preparing 4 unshocked rolls, and one for 4 shocked rolls) were shocked on a shaking table (IKA KS 130 basic, Bie and Berntsen AS, Rødovre, Denmark) at 560 rpm for exactly 1 minute (fixed silicone muffin molds). The baking sheet with the shocked rounded doughs in molds was placed in an oven (Bago-mini oven BMO-77, Bago-Line, Faaborg, Denmark) together with the baking sheet with the unshocked rounded doughs and baked for 8 minutes at 220 °C. The unshocked rolls and shocked rolls were cooled at ambient temperature for 20 minutes before they were weighed, and volume determined using a volumetric glass cylinder and dried fine sand. To measure volume of rolls, the specific volume of the dried fine sand was carefully determined in a volumetric glass cylinder and by weight, thus the fine sand displacement by rolls was determined by weight and the total volume of the rolls calculated from the weight of baked rolls and difference of displaced sand. Volume determination by sand displacement was performed in duplicate. Specific volume of min. four rolls of the unshocked rolls and shocked rolls was calculated as the volume of the rolls (4) divided by the weight of the rolls (4). Purified starch-acting GTF-like enzyme candidates were added according to protein amount as described in Example 5: GH31 (CRC31440, SEQ ID NO:12) at 15.7 mg / mL, GtfB (CRC31302, SEQ ID NO:14) at 32.0 mg / mL and GtfD (CRC29205, SEQ ID NO:22) at 32.2 mg / mL. The addition of starch-acting GTF-like enzyme sample was 0.55% GH31 (CRC31440, SEQ ID NO:12), 0.27% GtfB (CRC31302, SEQ ID NO:14) and 0.27% GtfD (CRC29205, SEQ ID NO:22) given as % of amount flour (Bakers percentage); see also trial setup in Table 4 below. Adjustment of the fungal alpha-amylase content was achieved by addition of GRINDAMYL® A 1000 (A1000) at 0.33% to obtain better dough handling properties and slightly increased final volume. DATEM was used as a gluten strengthening emulsifier reference for dough development. PANODAN® A2020 (PANODAN® A2020 KOSHER) supplied by IFF (Brabrand, Denmark) is a diacetyl tartaric acid ester of mono- / di- glycerides (DATEM) made from edible, fully hydrogenated rapeseed- and / or palm-based oil containing calcium carbonate as carrier in the following ratio: 80% DATEM and 20% calcium carbonate. PANODAN® A2020 was added in a dosage of 0.3% of the flour (Bakers percentage). Table 4. Ingredients for wheat dough-punched rolls using 300 g wheat flour The specific volume of the unshocked and shocked breads (4 unshocked rolls and 4 shocked rolls) were determined in duplicate; the results are shown in FIG.36 (A) and 36 (B) for the specific volumes calculated on dough and bread weight, respectively. The candidate starch-acting GTF-like enzymes in this Example – GH31 (CRC31440, SEQ ID NO:12), GtfB (CRC31302, SEQ ID NO:14) and GtfD (CRC29205, SEQ ID NO:22) significantly improved the specific volumes of the unshocked breads, which were 3.98 mL / g, 4.35 mL / g and 4.18 mL / g, respectively, versus the blank reference (Enovera 3001 and no GTF) specific volume of 3.70 mL / g. The increases of specific volume by starch-acting GTF- like enzymes were nearly similar to the specific volume obtained with DATEM (PANODAN® A2020) used as a gluten strengthening emulsifier reference for dough development (4.40 mL / g). A somewhat similar trend was observed evaluating the specific volume based on the dough weight, with significant improvement of the specific volumes of the unshocked breads having starch-acting GTF-like enzymes added, with 3.16 mL / g, 3.35 mL / g and 3.47 mL / g versus the blank reference (Enovera 3001 and no GTF) specific volume of 3.05 mL / g. This result clearly indicated no difference between the individual doughs with different enzymes in water evaporation during bake-off. The shocked bread specific volumes (determined on bread weight) were increased for punched rolls prepared with all the starch-acting GTF-like enzymes GH31 (CRC31440, SEQ ID NO:12), GtfB (CRC31302, SEQ ID NO:14) and GtfD (CRC29205, SEQ ID NO:22) to 3.32 mL / g, 3.39 mL / g and 3.23 mL / g, respectively, versus the specific volume for the blank reference of 3.18 mL / g. Thus, the relative shocked specific volumes were found to be 104%, 106% and 101% as compared to the control without GTF enzyme, which was set to 100%; thus, there was a relative increase of 4%, 6% and 1%, respectively. The shocked bread specific volumes (determined on bread weight) were further increased by DATEM (PANODAN® A2020) with a relative shocked specific volume that was 127% as compared to the control without GTF enzyme, which was set to 100%; thus, there was a relative increase of 27%. These results clearly demonstrate that starch-acting GTF-like enzymes can individually improve dough specific volume, stability and the relative shocked bread specific volume. Example 8. Dough development analyzed by Brabender farinograph The impact of GTF-like enzymes on dough development was analysed using a Brabender farinograph (calibrated and operated according to Brabender ICC_BIPEA_50). 50 g of Reform flour (Valsemøllen, Esbjerg Denmark, 12.5% protein) and 2% salt was dry- mixed for 1 minute in a Farinograph-E (Brabender, Duisburg, Germany) equipped with a 50- g moulding chamber (Mixer S 50N, model 820608), equilibrated at 30.0 ^C and set speed of 63 rounds / minute, then 59.5% tap water (adjusted to 30.0 ^C) was added and the dough was mixed for 20 minutes. Torque (BU) was recorded throughout the mixing. A blank consisting of the flour, salt and water, but no added enzyme herein, had a BU (Brabender unit) of 385±5 at 6 minutes of development. With doughs prepared having a GTF-like enzyme, enzyme was added together with the water and the total amount of liquid added was kept constant at 59.5%. BU as a function of mixing time with each added enzyme sample was compared to that of the blank. DATEM was used as a gluten strengthening emulsifier reference for dough development. PANODAN® A2020 (PANODAN® A2020 KOSHER) supplied by IFF (Brabrand, Denmark) is a diacetyl tartaric acid ester of mono- / di-glycerides (DATEM) made from edible, fully hydrogenated rapeseed- and / or palm-based oil containing calcium carbonate as carrier in the following ratio: 80% DATEM and 20% calcium carbonate. PANODAN® A2020 was added in a dosage of 0.3% of the flour (Bakers percentage). PowerFRESH 8100 (G4-forming amylase product by IFF, Denmark) was used as an exo-acting alpha-amylase in baking and is active on damaged starch or dextrins in flour. PowerFRESH 8100 was added in a dosage of 0.04% of the flour (Bakers percentage). The purified starch-acting GTF-like enzyme samples of DDase CRC29225-00001 (SEQ ID NO:1), GTF-C CRC28250 (SEQ ID NO:26), and DDase CRC29218 (SEQ ID NO:2) were added at 0.32%, 0.36%, 0.27% and 0.5%, respectively, of the flour (Bakers percentage). The results of the farinograph analysis are shown in FIG.38. After 6 minutes mixing time, it was clear that the exo-acting alpha-amylase PowerFRESH 8100 did not significantly produce a higher torque (in Brabender units [BU]) during dough development as compared to the blank, which had a torque of 385 BU (FIG.38). The individual addition of PANODAN® A2020 (DATEM), DDase CRC29225-00001 (SEQ ID NO:1), GTF-C CRC28250 (SEQ ID NO:26), and especially DDase CRC29218 (SEQ ID NO:2) resulted in a significantly increased torque of the dough after 6 minutes with a BU of 410, 408, 406, 409 and 429 respectively (FIG.26). Thus, these latter enzyme treatments are expected to be useful for preparing dough with higher strength and / or viscosity, which features would be useful for increasing dough stability in various baking applications. Example 9. Determination of alpha-glucan linkage in reaction mixtures of candidate GTF-like enzymes and substrate using NMR spectroscopy Preparation of reaction mixtures Reaction mixtures were prepared by incubating 50 μg / mL of purified GTF-like enzymes (each tested individually) from four enzyme classes (DDase, GtfB, GtfC, GtfD) with 1% (w / v) DP7 (maltoheptaose, Hayashibara) or amylose (from potato starch, A0512, Sigma-Aldrich) for 2 hours or 24 hours, respectively, in 20 mM MES buffer (pH 6.0) at 32 °C with 250 rpm shaking in a temperature-controlled shaker (INFORS HT, Switzerland). See HPLC results in FIGs.29-34 for reactions with amylose. The reaction mixtures were quenched by heating at 100 °C for 15 minutes at the end of each incubation time. Each quenched reaction mixture was divided into three parts: one part was immediately frozen at - 20 °C until NMR analyses were conducted, another part was lyophilized using a freeze-dryer (Labconco, USA) for NMR analyses, and the remaining part was subjected to three different types of alpha-glucan hydrolyzing enzyme treatments and further analyzed by HPLC. The complementary data from HPLC provided additional information to support the NMR data. The detailed substrate preparation, reaction incubation, and HPLC conditions followed the same procedure as described in Example 4. NMR analysis Each liquid sample was prepared by mixing 500 µL enzyme reaction mixture with 100 µL D2O containing 0.05% 3-(trimethylsilyl)propionic acid-d4 sodium salt (TSP) as an internal standard. The lyophilized samples were dissolved in 700 µL of 3-wt% LiCl / DMSO-d6 and stirred overnight at 85 °C. Afterwards, 50 µL of 5 mM sodium 3-(trimethylsilyl)propane-1- sulfonate (DSS) was added as an internal standard. The NMR measurements were performed at 70 °C on a 600 MHz Bruker Avance III spectrometer equipped with a 5-mm BBO SmartProbe (Bruker Biospins, Rheinstetten, Germany). A standard 1D Noesy experiment with pre-saturation (Bruker “noesypr1d” sequence) was used to acquire1H NMR spectra. 256 scans in total were collected into 64K data points acquired with a spectral width of 20.03 ppm, a recycle delay of 3 seconds and an acquisition time of 2.73 seconds. The1H spectra were processed with an exponential line- broadening of 0.8 Hz prior to the Fourier transformation. Assignments were based on literature values on H-1 and C-1 chemical shifts of glucose units with different linkage in alpha-glucans (Meng et al., 2017, Food Chem; Torres-Rodriguez et al., 2014, Springerplus; van Leeuwen et al., 2008, Carbohydr. Res.); see FIG.37 with regard to linkage assignment. To aid spectral assignment, 2D13C–1H heteronuclear single quantum coherence (HSQC) experiments on selected samples are to be performed. The HSQC correlating spectrum was acquired with a spectral width of 12.15 ppm in the1H dimension and 180.00 ppm in the13C dimension, a data matrix with a size of 4096×512 data points, 32 transients per increment and a recycle delay of 1.5 seconds. Peak deconvolution using Global Spectral Deconvolution in MestReNova version 14.3.1 was applied to calculate the linkage composition based on the H- 1 region of the1H spectra. The molar ratios of the identified linkages of each enzyme reaction mixture are shown in Table 5. It was clearly seen that reaction of various enzymes (DDase, GtfB, GtfC, GtfD) with either 1% (w / v) DP7 (maltoheptaose) or amylose increased the content of alpha-1,2, alpha-1,3 and / or alpha-1,6 linkages and decreased the content of alpha-1,4 linkages in the respective products. These observations are expected to similarly apply upon reaction of these enzymes with starch or starch-like substrates.

[0002] Table 5. Molar ratio of linkage composition of each enzyme reaction mixture. SEQ I NO 2 14 22 26 27 Abbre Samples were analyzed in liquid format.

[0003] Example 10. Determination of specific volumes of wheat dough punched rolls using candidate starch-acting GTF-like enzymes using a shaking table shock test Mini baking trials were performed as described in Example 7 using soft wheat flour (Valsemøllen, Esbjerg Denmark, 10% protein) with an initial water content of 14% tempered to 44 °C in a heating cabinet. Purified starch-acting GTF-like enzyme candidates were added according to protein amount as determined according to Example 5: DDase (CRC29225-00001, SEQ ID NO:1) at 30.11 mg / mL, DDase (CRC29234-WT, SEQ ID NO:6) at 28.8 mg / mL, DDase (CRC29233- WT, SEQ ID NO:5) at 9.13 mg / mL and GTF-C (CRC28250-WT, SEQ ID NO:26) at 7.0 mg / mL. The addition of starch-acting GTF-like enzyme sample was 0.14%, 0.29% and 0.58% DDase (CRC29225-00001, SEQ ID NO:1), 0.3% DDase (CRC29234-WT, SEQ ID NO:6), 0.47% DDase (CRC29233-WT, SEQ ID NO:5) and 1.24% GTF-C (CRC28250-WT, SEQ ID NO:26) given as % of amount flour (Bakers percentage); see also trial setup in Tables 6 and 7 below. Adjustment of the fungal alpha-amylase content was achieved by addition of GRINDAMYL® A 1000 (A1000) at 0.33% and 0.125% Enovera^ 3001 (enzyme complex of lipase, amylase, xylanase and oxidase to provide increased bread volume provided by IFF, Brabrand, Denmark) were all mixed in a Kitchen Aid (Artisan 5KSM125, Kitchen Aid, MI, USA) to obtain better dough handling properties and slightly increased final volume.

[0004] Table 6. Ingredient table for wheat dough punched rolls using 300 g wheat flour with starch- acting GTF-like enzymes

[0005] Table 7. Ingredient table for wheat dough punched rolls using 300 g wheat flour with starch- acting GTF-like enzymes. The specific volume of the unshocked and shocked breads (4 unshocked rolls and 4 shocked rolls) were determined in duplicate; the results are shown in FIG.39 based on dough weight and the specific volume of the unshocked and shocked breads are given in FIG.40 based on bread weight. The candidate starch-acting GTF-like enzymes in this Example – 0.14%, 0.29% and 0.58% DDase (CRC29225-00001, SEQ ID NO:1), 0.3% DDase (CRC29234-WT, SEQ ID NO:6), 0.47% DDase (CRC29233-WT, SEQ ID NO:5) and 1.24% GTF-C (CRC28250-WT, SEQ ID NO:26) all surprisingly improved the specific volumes of the unshocked breads, which were 4.66 mL / g, 4.76 mL / g and 4.37mL / g, 4.72 mL / g, 4.65 mL / g and 4.38 mL / g, respectively, versus the blank reference (Enovera 3001 and no GTF) specific volume of 4.36 mL / g. The relative volume increases ranged from 101% to 109% as compared to blank reference (Enovera 3001 and no GTF), which was set to 100%; thus, there was a relative increase of 1 and 9%, respectively. A somewhat similar trend was observed evaluating the specific volume based on the dough weight with significantly improve the specific volumes of the unshocked breads having starch-acting GTF-like enzymes added, with 3.75 mL / g, 3.74 mL / g, 3.46 mL / g, 3.52 mL / g, 3.68 mL / g, and 3.67 mL / g versus the blank reference (Enovera 3001 and no GTF enzyme) specific volume of 3.44 mL / g. These results clearly indicated no difference between the individual doughs with different enzymes in water evaporation during bake-off. The shocked bread specific volumes (determined on bread weight) were increased for punched rolls in bread prepared with all the starch-acting GTF-like enzymes 0.14% and 0.29% DDase (CRC29225-00001, SEQ ID NO:1), 0.3% DDase (CRC29234-WT, SEQ ID NO:6), 0.47% DDase (CRC29233-WT, SEQ ID NO:5) and 1.24% GTF-C (CRC28250-WT, SEQ ID NO:26), respectively, as compared to the specific volume for the blank (Enovera 3001 and no GTF) reference. Thus, the relative shocked specific volume was found to range from 103-114% vs the control, which was set to 100%; thus, there was a relative increase of 3-14%. A somewhat similar trend was observed evaluating the specific volume based on the dough weight with significantly improved specific volumes of the shocked breads. These results clearly demonstrate that starch-acting GTF-like enzymes can individually improve unshocked dough specific volume and stability by the relative shocked bread specific volume. Example 11. Determination of specific volumes of wheat dough punched rolls using candidate starch-acting GTF-like enzymes using a shaking table shock test Mini baking trials were performed as described in Example 7 using soft wheat flour (Valsemøllen, Esbjerg Denmark, 10% protein) with an initial water content of 14% that was tempered to 44 °C in a heating cabinet. A purified starch-acting GTF-like enzyme candidate was added according to protein amount as determined according to Example 5: DDase (CRC29218, SEQ ID NO:2) at 5.1 mg / mL. The addition of starch-acting GTF-like enzyme sample was 1.33% DDase (CRC29218, SEQ ID NO:2) given as % of amount flour (Bakers percentage); see also trial setup in Table 8 below. Adjustment of the fungal alpha-amylase content was achieved by addition of GRINDAMYL® A 1000 (A1000) at 0.33% and 0.125% Enovera^ 3001 (enzyme complex of lipase, amylase, xylanase and oxidase to provide increased bread volume provided by IFF, Brabrand, Denmark) and all mixed in a Kitchen Aid (Artisan 5KSM125, Kitchen Aid, MI, USA) to obtain better dough handling properties and slightly increased final volume. Table 8. Ingredient table for wheat dough punched rolls using 300 g wheat flour with the starch-acting GTF-like enzyme The specific volume of the unshocked and shocked breads (4 unshocked rolls and 4 shocked rolls) were determined in duplicate; the results are shown in FIG.41 based on dough and bread weight. The starch-acting GTF-like candidate enzyme in this Example, 1.33% DDase (CRC29218, SEQ ID NO:2), improved the specific volume of the unshocked breads, which was 4.73 mL / g versus the blank reference (Enovera 3001 and no GTF) specific volume of 3.98 mL / g. The relative volume increased to 118% as compared to blank reference (Enovera 3001 and no GTF), which was set at 100%; thus, there was a relative increase of 18%. A similar trend was observed evaluating the specific volume based on the dough weight with significantly improved specific volumes of the unshocked breads having starch-acting GTF- like enzymes added, with 3.75 mL / g versus the blank reference (Enovera 3001 and no GTF enzyme) specific volume of 3.18 mL / g. These results clearly indicated there was no difference between the individual doughs with different enzymes in water evaporation during bake-off. The starch-acting GTF-like candidate enzyme 1.33% DDase (CRC29218, SEQ ID NO:2) also improved the specific volumes of the shocked breads, which were 3.52 mL / g versus the blank reference (Enovera 3001 and no GTF) specific volume of 3.43 mL / g. This demonstrates that the starch-acting GTF-like enzyme can improve unshocked dough specific volume and stability by the relative shocked bread specific volume. Example 12. Product analysis of candidate GtfD glucosyltransferase enzymes using maltodextrin (DE4-7) as substrate The products of candidate GtfD glucosyltransferase enzymes formed on maltodextrin (DE4-7) substrate were investigated by HPLC analysis coupled with an SEC column. The detailed methods are described as follows. The DE4-7 substrate was prepared by dissolving it in MILLI-Q water to an initial concentration of 13% (w / v), and then 250 µL / well of the substrate solution and 500 µL / well of 10 mM sodium acetate buffer (pH 5.5) were transferred into a 96-deepwell reaction plate (BioScience, China) using a Biomek i-7 Automated Workstation (Beckman, USA). Purified enzyme samples (CRC29205, SEQ ID NO:22 and CRC29205-00002, SEQ ID NO:86) were firstly diluted in glycerol (40%, w / v) with 100 mM NaCl to a final concentration of 1 mg / mL. The protein concentration of each diluted enzyme sample was further quantified by examining the absorbance at 280 nm using BSA as a standard. Then the concentrations of all the enzyme samples were normalized to 200 µg / mL using MILLI-Q water. Each reaction was initiated by transferring 250 µL / well of normalized enzyme solution into the reaction plate. 100 µg / mL of ampicillin was included in the reaction system to protect the mixture from microbial contamination. The reaction plate was then sealed and incubated in a ThermoMixer®at 37 °C and 650 rpm for 3 or 24 hours. After incubation, the reaction mixture was heated at 100 °C for 20 minutes to stop the reaction. The stopped reaction mixture was diluted thirty times using the corresponded mobile phase and filtered through a 0.2-µm filter plate (Corning 3505) for HPLC analysis. All liquid handling was performed using a Biomek i-7 Automated Workstation (Beckman, USA). Aliquots of each of the above filtered reaction mixtures were analyzed by HPLC (Agilent 1200 series, USA) using an OHpak SB-806M HQ column (Shodex, Japan), run at 35 °C; or using an OHpak SB-803 HQ column (Shodex, Japan), run at 40 °C. 25 µL-samples were individually loaded on the column and separated with an isocratic gradient of MILLI-Q water or 10 mM NaCl as the mobile phase at a flow rate of 1.0 or 0.5 mL / min, as specified in the BRIEF DESCRIPTION OF THE DRAWINGS (above). The enzyme products were detected using a refractive index detector (RID) (FIG.42), and pullulan standards were run to determine the molecular weight of each product. The molecular weight and retention time of each pullulan standard are listed in Table 9. Table 9. Molecular weight and retention time of pullulan standards Analysis of the original maltodextrin substrate (FIG.42, “Sub only”) revealed no polymer peak larger than the pullulan P-800 standard, which has a molecular weight of about 7.8x10^5 Da. In contrast, the products generated by the wild-type CRC29205 (SEQ ID NO:22) and a variant thereof (CRC29205-00002, SEQ ID NO:86, has a Q487I substitution with respect to SEQ ID NO:22) exhibited polymer peaks exceeding the molecular weight of pullulan standard P-800 (FIG 42). This Gln-487 substitution is located at the +2 position in the substrate-binding pocket of the CRC29205 GtfD. Notably, the variant (modified) GtfD enzyme demonstrated a significant increase in yield of high molecular weight products compared to its wild-type counterpart. Example 13. Sequence identity of other GtfD enzymes compared to CRC29205-WT, and amino acid substitution studies The amino acid sequences of GtfD enzymes (SEQ ID NOs:23, 82, 83, 84 and 85) were aligned with CRC29205-WT (SEQ ID NO:22) using the BLAST function in the “Align My Sequences” tool from GENOMEQUEST, or using EMBOSS Needle (tool from European Molecular Biology Laboratory – European Bioinformatics Institute [EMBL-EBI]). SEQ ID NO:22 was used as the reference (subject), while SEQ ID NOs:23, 82, 83, 84 and 85 served as queries. Default BLAST or EMBOSS Needle parameters were applied for performing the alignments. The resulting sequence identity percentages are presented in Table 10. Table 10. Sequence Identity of Wildtype GtfD Enzymes Relative to CRC29205-WT Amino acid substitution studies were conducted further to Example 13, following the same procedure. Interestingly, it was observed that a variant GtfD enzyme, CRC29210-00001 (SEQ ID NO:87), demonstrated a significant increase in yield of high molecular weight products compared to its wild-type counterpart, CRC29210-WT (SEQ ID NO:23) (FIG.44). CRC29210-00001 (SEQ ID NO:87) has a Q543I substitution with respect to CRC29210-WT (SEQ ID NO:23). It is also noteworthy that, although the wildtype GtfD sequences of SEQ ID NO:22 and SEQ ID NO:23 only share about 40-50% amino acid identity with each other (Table 10), substitution of the glutamine residue in a conserved portion of the two enzymes resulted in product yield increases (refer to FIGs.42 and 44). Interestingly, it was observed that a variant GtfD enzyme, CRC34732-00001 (SEQ ID NO:89), demonstrated a significant increase in yield of high molecular weight products compared to its wild-type counterpart, CRC34732-WT (SEQ ID NO:83) (FIG.45). CRC34732-00001 (SEQ ID NO:89) has a Q487I substitution with respect to CRC34732-WT (SEQ ID NO:83). This product yield effect echoed what was observed for altering the GtfD sequence of SEQ ID NO:22 (refer to FIGs.42 and 45), which is consistent with the greater than 90% amino acid identity shared by SEQ ID NOs:22 and 83 (Table 10). Interestingly, it was observed that a variant GtfD enzyme, CRC34742-00001 (SEQ ID NO:90), demonstrated a significant increase in yield of high molecular weight products compared to its wild-type counterpart, CRC34742-WT (SEQ ID NO:84) (FIG.46). CRC34742-00001 (SEQ ID NO:90) has a Q487I substitution with respect to CRC34742-WT (SEQ ID NO:84). This product yield effect echoed what was observed for altering the GtfD sequence of SEQ ID NO:22 (refer to FIGs.42 and 46), which is consistent with the greater than 90% amino acid identity shared by SEQ ID NOs:22 and 84 (Table 10). Interestingly, it was observed that a variant GtfD enzyme, CRC34743-00001 (SEQ ID NO:91), demonstrated a significant increase in yield of high molecular weight products compared to its wild-type counterpart, CRC34743-WT (SEQ ID NO:85) (FIG.47). CRC34743-00001 (SEQ ID NO:91) has a Q487I substitution with respect to CRC34743-WT (SEQ ID NO:85). This product yield effect echoed what was observed for altering the GtfD sequence of SEQ ID NO:22 (refer to FIGs.42 and 47), which is consistent with the greater than 90% amino acid identity shared by SEQ ID NOs:22 and 54 (Table 10).

Claims

CLAIMS What is claimed is:

1. A method of producing a food dough, said method comprising: mixing at least (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase, thereby producing a food dough, optionally wherein: (a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks said enzyme, (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks said enzyme, and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks said enzyme.

2. The method of claim 1, wherein the enzyme is said dextrin dextranase.

3. The method of claim 1, wherein the enzyme is said 4,6-alpha-glucanotransferase.

4. The method of claim 3, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase.

5. The method of claim 1, wherein the enzyme comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6-alpha-glucanotransferase enzyme according to claim 38.

6. The method of claim 1, wherein said flour is used in the method, optionally wherein the flour is wheat flour.

7. The method of claim 1, further comprising: processing the food dough into a food.

8. The method of claim 7, wherein said processing comprises at least baking, frying, boiling, drying, chilling, extruding, and / or flattening the food dough.

9. The method of claim 6, wherein the food dough comprises a leavening agent, optionally wherein the leavening agent is yeast.

10. The method of claim 9, wherein the food dough is a bread dough.

11. The method of claim 9, further comprising allowing the food dough to rise, thereby providing risen food dough.

12. The method of claim 11, wherein the risen food dough is risen bread dough, optionally wherein the volume of the risen bread dough is at least 5% greater than it would be if the risen bread dough did not comprise said enzyme, wherein optionally the risen bread dough has not been shocked, or optionally the risen bread dough has been shocked.

13. The method of claim 12, further comprising dropping the risen bread dough at least one time over a distance of at least 1 cm, wherein, following said dropping, the volume of the risen bread dough is at least 2% greater than it would be if the risen bread dough did not comprise said enzyme.

14. The method of claim 6, wherein said mixing exhibits a torque that is at least 2% greater than it would be if the food dough did not comprise said enzyme.

15. The method of claim 1, wherein the weight-average degree of polymerization (DPw) of gluco-oligosaccharides of the food dough is increased by at least 1 as compared to the DPw of gluco-oligosaccharides of the flour or meal before said mixing.

16. The method of claim 1, wherein the alpha-1,4 glycosidic linkage content of the alpha- 1,4-glucan of the food dough is reduced as compared to the alpha-1,4 glycosidic linkage content of the alpha-1,4-glucan of the flour or meal before said mixing, typically wherein the alpha-1,4-glucan of the food dough has an increased content of alpha-1,6 and / or alpha-1,3 glycosidic linkages as compared to the alpha-1,6 and / or alpha-1,3 glycosidic linkage content of the alpha-1,4-glucan of the flour or meal before said mixing.

17. The method of claim 6, wherein the flour has a gluten content that is less than about 12 wt%.

18. The method of claim 1, further comprising adding at least one of a lipase, alpha- amylase, xylanase, non-maltogenic exoamylase, glucoamylase, glucose oxidase, or hexose oxidase during production of the food dough.

19. A food dough produced by the method of claim 1.

20. A food product produced by the method of claim 7.

21. A food dough comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha- glucanotransferase, optionally wherein(a) the food dough has a shock stability that is increased as compared to the shock stability of a control food dough that lacks said enzyme, (b) the food dough has a viscosity that is increased as compared to the viscosity of a control food dough that lacks said enzyme, and / or (c) the food dough has a water-binding capacity that is increased as compared to the water-binding capacity of a control food dough that lacks said enzyme.

22. The food dough of claim 21, wherein the enzyme is said dextrin dextranase.

23. The food dough of claim 21, wherein the enzyme is said 4,6-alpha-glucanotransferase.

24. The food dough of claim 23, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase.

25. The food dough of claim 21, wherein the enzyme comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6-alpha- glucanotransferase enzyme according to claim 38.

26. The food dough of claim 21, wherein the food dough comprises said flour, optionally wherein the flour is wheat flour.

27. The food dough of claim 26, wherein the food dough comprises a leavening agent, optionally wherein the leavening agent is yeast.

28. The food dough of claim 26, wherein the food dough is a bread dough.

29. The food dough of claim 26, wherein food dough is a risen food dough.

30. A food product comprising (i) flour and / or meal, (ii) water or aqueous composition, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha- glucanotransferase, optionally wherein the food product has a water-binding capacity that is increased as compared to the water-binding capacity of a control food product that lacks said enzyme.

31. The food product of claim 30, wherein the enzyme is said dextrin dextranase.

32. The food product of claim 30, wherein the enzyme is said 4,6-alpha- glucanotransferase.

33. The food product of claim 32, wherein the 4,6-alpha-glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase.

34. The food product of claim 30, wherein the food product is a baked food product.

35. The food product of claim 34, wherein the baked food product is bread.

36. The food product of claim 30, wherein, as compared to a control food product that lacks said enzyme, the food product has one or more of the following features: (I) increased dietary fiber, (II) increased prebiotic activity, (III) reduced caloric density or reduced calories, (IV) reduced glycemic index, and / or (V) reduced digestibility.

37. An enzyme selected from a dextrin dextranase or a 4,6-alpha-glucanotransferase, wherein the enzyme comprises an amino acid sequence that is at least about 90% identical to SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148.

38. A modified 4,6-alpha-glucanotransferase enzyme, wherein the modified 4,6-alpha- glucanotransferase enzyme: (i) comprises an amino acid substitution at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:22 (or at a position corresponding with amino acid residue Gln-543 of SEQ ID NO:23, or at a position corresponding with amino acid residue Gln-487 of SEQ ID NO:83, 84, or 85), wherein the amino acid substitution is with an Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val residue, and (ii) comprises an amino acid sequence that is at least about 40% identical to SEQ ID NO:22 (or SEQ ID NO:23, 83, 84, or 85), optionally wherein the modified 4,6-alpha-glucanotransferase enzyme can produce a modified alpha-glucan at a yield that is higher than the yield of the modified alpha- glucan that would be produced by a control 4,6-alpha-glucanotransferase enzyme that only differs from the modified 4,6-alpha-glucanotransferase enzyme at the substitution position.

39. The modified 4,6-alpha-glucanotransferase enzyme of claim 38, wherein the amino acid substitution is with said Ile, Glu, His, Leu, Met, Phe, Thr, Trp, Tyr, or Val residue, optionally wherein the modified 4,6-alpha-glucanotransferase enzyme comprises (i) the amino acid sequence of SEQ ID NO:86, 87, 88, 89, 90, 91, 112, 114, 115, 117, 118, 121, 122, 123, or 124, or (ii) an amino acid sequence that is at least about 40% identical to the amino acid sequence of (i).

40. A polynucleotide comprising a nucleotide sequence encoding an enzyme according to claim 37, optionally wherein one or more regulatory sequences are operably linked to the nucleotide sequence, and preferably wherein said one or more regulatory sequences include a promoter sequence.

41. A food ingredient comprising a modified alpha-glucan, or a food product comprising said food ingredient, wherein the modified alpha-glucan is produced by providing a composition comprising at least (i) water, (ii) an alpha-1,4-glucan substrate, and (iii) an enzyme selected from a dextrin dextranase and / or a 4,6-alpha-glucanotransferase.

42. The food ingredient or food product of claim 41, wherein the enzyme is the dextrin dextranase.

43. The food ingredient or food product of claim 41, wherein the enzyme is the 4,6-alpha- glucanotransferase.

44. The food ingredient or food product of claim 43, wherein the 4,6-alpha- glucanotransferase enzyme is a GtfB, GtfC, or GtfD glucanotransferase, or a GH31 glucanotransferase.

45. The food ingredient or food product of claim 41, wherein the enzyme comprises an amino acid sequence that is at least 90% identical to SEQ ID NO:1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, or 148, or wherein the enzyme is a modified 4,6-alpha-glucanotransferase enzyme according to claim 38.

46. The food ingredient or food product of claim 41, wherein the alpha-1,4-glucan substrate comprises starch, amylose, and / or amylopectin.

47. The food ingredient or food product of claim 41, wherein the alpha-1,4-glucan substrate comprises a starch hydrolysate, dextrin, amylodextrin, and / or maltodextrin.

48. The food ingredient or food product of claim 41, wherein, as compared to a control food ingredient or food product that lacks said enzyme, the food ingredient or food product has one or more of the following features: (I) increased dietary fiber, (II) increased prebiotic activity, (III) reduced caloric density or reduced calories, (IV) reduced glycemic index, and / or (V) reduced digestibility.

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