1932

Abstract

Starch is one of the most abundant renewable biopolymers in nature and is the main constituent in the human diet and a raw material for the food industry. Native starches are limited in most industrial applications and often tailored by structural modification to enhance desirable attributes, minimize undesirable attributes, or create new attributes. Enzymatic approaches for structuring starch have become of interest to the food industry precisely because the reactions minimize the formation of undesirable by-products and coproducts and are therefore considered environmentally friendly methods for producing clean-label starches with better behavioral characteristics. Starches with improved functionalities for various applications are produced via enzyme hydrolysis and transfer reactions. Use of novel, multifunctional, starch-active enzymes to alter the structures of amylose and/or amylopectin molecules, and thus alter the starch's physiochemical attributes in a predictable and controllable manner, has been explored. This review provides state-of-the-art information on exploiting glycosyl transferases and glycosyl hydrolases for structuring starch to improve its functionalities. The characteristics of starch-active enzymes (including branching enzymes, amylomaltases, GH70 α-transglycosylases, amylosucrases, maltogenic amylases, cyclomaltodextrinases, neopullulanases, and maltooligosaccharide-forming amylases), structure–functionality-driven processing strategies, novel conversion products, and potential industrial applications are discussed.

Loading

Article metrics loading...

/content/journals/10.1146/annurev-food-072122-023510
2023-03-27
2024-06-20
Loading full text...

Full text loading...

/deliver/fulltext/food/14/1/annurev-food-072122-023510.html?itemId=/content/journals/10.1146/annurev-food-072122-023510&mimeType=html&fmt=ahah

Literature Cited

  1. Abdalla M, Jiang B, Hassanin HAM, Zheng L, Chen J 2021. One-pot production of maltoheptaose (DP7) from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase. Enzyme Microb. Technol. 149:109847
    [Google Scholar]
  2. Albenne C, Skov LK, Mirza O, Gajhede M, Feller G et al. 2004. Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase. J. Biol. Chem. 279:726–34
    [Google Scholar]
  3. Alting AC, van de Velde F, Kanning MW, Burgering M, Mulleners L et al. 2009. Improved creaminess of low-fat yoghurt: the impact of amylomaltase-treated starch domains. Food Hydrocoll 23:980–87
    [Google Scholar]
  4. Amigo JM, Olmo AD, Engelsen MM, Lundkvist H, Engelsen SB. 2021. Staling of white wheat bread crumb and effect of maltogenic α-amylases. Part 3: spatial evolution of bread staling with time by near infrared hyperspectral imaging. Food Chem 353:129478
    [Google Scholar]
  5. Auh JH, Chae HY, Kim YR, Shim KH, Yoo SH, Park KH. 2006. Modification of rice starch by selective degradation of amylose using alkalophilic Bacillus cyclomaltodextrinase. J. Agric. Food Chem. 54:2314–19
    [Google Scholar]
  6. Bae W, Lee SH, Yoo SH, Lee S 2014. Utilization of a maltotetraose-producing amylase as a whole wheat bread improver: dough rheology and baking performance. J. Food Sci. 79:1535–40
    [Google Scholar]
  7. Bai Y, Böger M, van der Kaaij RM, Woortman AJ, Pijning T et al. 2016. Lactobacillus reuteri strains convert starch and maltodextrins into homoexopolysaccharides using an extracellular and cell-associated 4,6-α-glucanotransferase. J. Agric. Food. Chem. 64:2941–52
    [Google Scholar]
  8. BeMiller JN. 1997. Starch modification: challenges and prospects. Starch 49:127–31
    [Google Scholar]
  9. BeMiller JN, Huber KC. 2015. Physical modification of food starch functionalities. Annu. Rev. Food Sci. Technol. 6:19–69
    [Google Scholar]
  10. BeMiller JN, Whistler RL. 2009. Starch: Chemistry and Technology New York: Acad. Press. , 3rd ed..
    [Google Scholar]
  11. Bertoft E. 2017. Understanding starch structure: recent progress. Agronomy 7:56
    [Google Scholar]
  12. Bhuiyan SH, Kitaoka M, Hayashi K. 2003. A cycloamylose-forming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli. J. Mol. Catal. B 22:45–53
    [Google Scholar]
  13. Bijttebier A, Goesaert H, Delcour JA. 2010. Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population. Carbohydr. Res. 345:235–42
    [Google Scholar]
  14. Boonna S, Rolland-Sabaté A, Lourdin D, Tongta S. 2019. Macromolecular characteristics and fine structure of amylomaltase-treated cassava starch. Carbohydr. Polym. 205:143–50
    [Google Scholar]
  15. Clark AH, Gidley MJ, Richardson RK, Ross-Murphy SB. 1989. Rheological studies of aqueous amylose gels: the effect of chain length and concentration on gel modulus. Macromolecules 22:346–51
    [Google Scholar]
  16. Chen C, Lu K, Hu X, Liu Y, Cui SW, Miao M. 2020. Biofabrication, structure and characterizations of amylopectin-based cyclic glucan. Food Funct 11:2543–54
    [Google Scholar]
  17. Cho KH, Auh JH, Kim JH, Ryu JH, Park KH et al. 2009. Effect of amylose content on corn starch modification by Thermus aquaticus 4-α-glucanotransferase. J. Microbiol. Biotechnol. 19:1201–5
    [Google Scholar]
  18. Choi SSH, Danielewska-Nikiel B, Ohdan K, Kojima I, Takata H, Kuriki T. 2009. Safety evaluation of highly-branched cyclic dextrin and a 1,4-α-glucan branching enzyme from Bacillus stearothermophilus. Regul. Toxicol. Pharmacol. 55:281–90
    [Google Scholar]
  19. Christophersen C, Otzen DE, Norman BE, Christensen S, Schafer T. 1998. Enzymatic characterization of Novamyl®, a thermostable α-amylase. Starch 50:39–45
    [Google Scholar]
  20. de Montalk GP, Remaud-Simeon M, Willemot RM, Sarçabal P, Planchot V, Monsan P. 2000. Amylosucrase from Neisseria polysaccharea: novel catalytic properties. FEBS Lett 471:219–23
    [Google Scholar]
  21. Dey G, Palit S, Banerjee R, Maitim BR. 2002. Purification and characterization of maltooligosaccharide-forming amylase from Bacillus circulans GRS 313. J. Ind. Microbiol. Biotechnol. 28:193–200
    [Google Scholar]
  22. Do HV, Lee EJ, Park JH, Park KH, Shim JY et al. 2012. Structural and physicochemical properties of starch gels prepared from partially modified starches using Thermus aquaticus 4-α-glucanotransferase. Carbohydr. Polym. 87:2455–63
    [Google Scholar]
  23. Do VH, Mun S, Kim YL, Rho SJ, Park KH, Kim YR. 2016. Novel formulation of low-fat spread using rice starch modified by 4-α-glucanotransferase. Food Chem 208:132–41
    [Google Scholar]
  24. Doan HXN, Song Y, Lee S, Lee BH, Yoo SH 2019. Characterization of rice starch gels reinforced with enzymatically-produced resistant starch. Food Hydrocoll 91:76–82
    [Google Scholar]
  25. Dobruchowska JM, Gerwig GJ, Kralj S, Grijpstra P, Leemhuis H et al. 2012. Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121. Glycobiology 22:517–28
    [Google Scholar]
  26. Eerlingen RC, Delcour JA. 1995. Formation, analysis, structure and properties of type III enzyme resistant starch. J. Cereal Sci. 22:129–38
    [Google Scholar]
  27. EFSA Panel Food Contact Mater. Enzym. Process. Aids, Silano V, Barat Baviera JM, Bolognesi C, Brüschweiler BJ et al. 2019. Safety evaluation of the food enzyme 4-α-glucanotransferase from Aeribacillus pallidus (strain AE-SAS). EFSA J 17:e05628
    [Google Scholar]
  28. Gaenssle ALO, van der Maarel MJEC, Jurak E 2022. The influence of amylose content on the modification of starches by glycogen branching enzymes. Food Chem 393:133294
    [Google Scholar]
  29. Gangoiti J, Corwin SF, Lamothe LM, Vafiadi C, Hamaker BR, Dijkhuizen L. 2020. Synthesis of novel α-glucans with potential health benefits through controlled glucose release in the human gastrointestinal tract. Crit. Rev. Food Sci. Nutr. 60:123–46
    [Google Scholar]
  30. Gangoiti J, Pijning T, Dijkhuizen L. 2015. The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Appl. Environ. Microbiol. 82:756–66
    [Google Scholar]
  31. Gangoiti J, van Leeuwen SS, Gerwig GJ, Duboux S, Vafiadi C et al. 2017a. 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H. Sci. Rep. 7:39761
    [Google Scholar]
  32. Gangoiti J, van Leeuwen SS, Meng X, Duboux S, Vafiadi C et al. 2017b. Mining novel starch-converting glycoside hydrolase 70 enzymes from the Nestlé Culture Collection genome database: the Lactobacillus reuteri NCC 2613 GtfB. Sci. Rep 7:9947
    [Google Scholar]
  33. Gangoiti J, van Leeuwen SS, Vafeiadi C, Dijkhuizen L. 2016. The gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch. Biochem. Biophys. Acta 1860:1224–36
    [Google Scholar]
  34. Gilbert RG. 2011. Size-separation characterization of starch and glycogen for biosynthesis-structure-property relationships. Anal. Bioanal. Chem. 399:1425–38
    [Google Scholar]
  35. Gong B, Cheng L, Gilbert RG, Li C 2019. Distribution of short to medium amylose chains are major controllers of in vitro digestion of retrograded rice starch. Food Hydrocoll 96:634–43
    [Google Scholar]
  36. Grewal N, Faubion J, Feng G, Kaufman RC, Wilson JD, Shi YC. 2015. Structure of waxy maize starch hydrolyzed by maltogenic α-amylase in relation to its retrogradation. J. Agric. Food Chem. 63:4196–201
    [Google Scholar]
  37. Gu F, Borewicz K, Richter B, van der Zaal PH, Smidt H et al. 2018. In vitro fermentation behavior of isomalto/malto-polysaccharides using human fecal inoculum indicates prebiotic potential. Mol. Nutr. Food Res. 62:e1800232
    [Google Scholar]
  38. Han XZ, Hamaker BR. 2001. Amylopectin fine structure and rice starch paste breakdown. J. Cereal Sci. 34:279–84
    [Google Scholar]
  39. Hansen MR, Blennow A, Pedersen S, Engelsen SB. 2009. Enzyme modification of starch with amylomaltase results in increasing gel melting point. Carbohydr. Polym. 78:72–79
    [Google Scholar]
  40. Haralampu SG. 2000. Resistant starch: a review of the physical properties and biological impact of RS3. Carbohydr. Polym. 41:285–92
    [Google Scholar]
  41. Hayashi M, Suzuki R, Colleoni C, Ball SG, Fujita N, Suzuki E. 2017. Bound substrate in the structure of cyanobacterial branching enzyme supports a new mechanistic model. J. Biol. Chem. 292:5465–75
    [Google Scholar]
  42. Henrissat B, Sulzenbacher G, Bourne Y. 2008. Glycosyltransferases, glycoside hydrolases: surprise, surprise!. Curr. Opin. Struct. Biol. 18:527–33
    [Google Scholar]
  43. Imanaka T, Kuriki T. 1989. Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan. J. Bacteriol. 171:369–74
    [Google Scholar]
  44. İspirli H, Şimşek Ö, Skory C, Sağdıç O, Dertli E. 2019. Characterization of a 4,6-α-glucanotransferase from Lactobacillus reuteri E81 and production of malto-oligosaccharides with immune-modulatory roles. Int. J. Biol. Macromol. 124:1213–19
    [Google Scholar]
  45. Jane JL, Chen YY, Lee LF, McPherson AE, Wong KS et al. 1999. Effects of amylopectin branch chain length and amylose content on the gelatinization and pasting properties of starch. Cereal Chem 76:629–37
    [Google Scholar]
  46. Jang MU, Kang HJ, Jeong CK, Kang Y, Park JE, Kim TJ. 2018. Functional expression and enzymatic characterization of Lactobacillus plantarum cyclomaltodextrinase catalyzing novel acarbose hydrolysis. J. Microbiol. 56:113–18
    [Google Scholar]
  47. Ji H, Bai Y, Li X, Zheng D, Shen Y, Jin Z 2020. Structural and property characterization of corn starch modified by cyclodextrin glycosyltransferase and specific cyclodextrinase. Carbohydr. Polym. 237:116137
    [Google Scholar]
  48. Ji X, Zeng C, Yang D, Mu S, Shi Y, Huang Y et al. 2022. Addition of 1,4-α-glucan branching enzyme during the preparation of raw dough reduces the retrogradation and increases the slowly digestible fraction of starch in cooked noodles. J. Cereal Sci. 104:103431
    [Google Scholar]
  49. Jiang H, Miao M, Ye F, Jiang B, Zhang T. 2014. Enzymatic modification of corn starch with 4-α-glucanotransferase results in increasing slow digestible and resistant starch. Int. J. Biol. Macromol. 65:208–14
    [Google Scholar]
  50. Jung DH, Park CS, Kim HS, Nam TG, Lee BH et al. 2022. Enzymatic modification of potato starch by amylosucrase according to reaction temperature: effect of branch-chain length on structural, physicochemical, and digestive properties. Food Hydrocoll 122:107086
    [Google Scholar]
  51. Jung JH, An YK, Son SY, Jeong SY, Seo DH et al. 2019a. Characterization of a novel extracellular α-amylase from Ruminococcus bromii ATCC 27255 with neopullulanase-like activity. Int. J. Biol. Macromol. 130:605–14
    [Google Scholar]
  52. Jung YS, Hong MG, Park SH, Lee BH, Yoo SH. 2019b. Biocatalytic fabrication of α-glucan-coated porous starch granules by amylolytic and glucan-synthesizing enzymes as a target-specific delivery carrier. Biomacromolecules 20:4143–49
    [Google Scholar]
  53. Kadota K, Senda A, Tagishi H, Ayorinde JO, Tozuka Y. 2017. Evaluation of highly branched cyclic dextrin in inhalable particles of combined antibiotics for the pulmonary delivery of antituberculosis drugs. Int. J. Pharm. 517:8–18
    [Google Scholar]
  54. Kageyama A, Yanase M, Yuguchi Y. 2019. Structural characterization of enzymatically synthesized glucan dendrimers. Carbohydr. Polym. 204:104–10
    [Google Scholar]
  55. Kajiura H, Takata H, Kuriki T, Kitamura S. 2010. Structure and solution properties of enzymatically synthesized glycogen. Carbohydr. Res. 345:817–24
    [Google Scholar]
  56. Kamasaka H, Sugimoto K, Takata H, Nishimura T, Kuriki T. 2002. Bacillus stearothermophilus neopullulanase selective hydrolysis of amylose to maltose in the presence of amylopectin. Appl. Environ. Microbiol. 68:1658–64
    [Google Scholar]
  57. Kamasaka H, Sugimoto K, Takata H, Nishimura T, Kuriki T. 2003. Neopullulanase exhibits distinct specificity toward amylose and amylopectin. J. Appl. Glycosci. 50:273–75
    [Google Scholar]
  58. Kaneo Y, Taguchi K, Tanaka T, Yamamoto S. 2014. Nanoparticles of hydrophobized cluster dextrin as biodegradable drug carriers: solubilization and encapsulation of amphotericin B. J. Drug Deliv. Sci. Technol. 24:344–51
    [Google Scholar]
  59. Kaper T, Talik B, Ettema TJ, Bos H, van der Maarel MJEC, Dijkhuizen L 2005. Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels. Appl. Environ. Microbiol. 71:5098–106
    [Google Scholar]
  60. Kelly RM, Dijkhuizen L, Leemhuis H. 2009. Starch and α-glucan acting enzymes, modulating their properties by directed evolution. J. Biotechnol. 140:184–93
    [Google Scholar]
  61. Kim BK, Kim HI, Moon TW, Choi SJ. 2014. Branch chain elongation by amylosucrase: production of waxy corn starch with a slow digestion property. Food Chem 152:113–20
    [Google Scholar]
  62. Kim BS, Kim HS, Yoo SH. 2015. Characterization of enzymatically modified rice and barley starches with amylosucrase at scale-up production. Carbohydr. Polym. 125:61–68
    [Google Scholar]
  63. Kim JE, Tran PL, Ko JM, Kim SR, Kim JH, Park JT. 2021. Comparison of catalyzing properties of bacterial 4-α-glucanotransferases focusing on their cyclizing activity. J. Microbiol. Biotechnol. 31:43–50
    [Google Scholar]
  64. Kim JS, Cha SS, Kim HJ, Kim TJ, Ha NC et al. 1999. Crystal structure of a maltogenic amylase provides insights into a catalytic versatility. J. Biol. Chem. 274:26279–86
    [Google Scholar]
  65. Kim TJ, Shin JH, Oh JH, Kim MJ, Lee SB et al. 1998. Analysis of the gene encoding cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 and characterization of enzymatic properties. Arch. Biochem. Biophys. 353:221–27
    [Google Scholar]
  66. Klostermann CE, Buwalda PL, Leemhuis H, de Vos P, Schols HA, Bitter JH. 2021. Digestibility of resistant starch type 3 is affected by crystal type, molecular weight and molecular weight distribution. Carbohydr. Polym. 265:118069
    [Google Scholar]
  67. Korompokis K, Deleu LJ, De Brier N, Delcour JA. 2021. Investigation of starch functionality and digestibility in white wheat bread produced from a recipe containing added maltogenic amylase or amylomaltase. Food Chem 362:130203
    [Google Scholar]
  68. Kuriki T, Tsuda M, Imanaka T. 1992. Continuous production of panose by immobilized neopullulanase. J. Ferment. Bioeng. 73:198–202
    [Google Scholar]
  69. Kuriki T, Yanase M, Takata H, Takesada Y, Imanaka T, Okada S. 1993. A new way of producing isomalto-oligosaccharide syrup by using the transglycosylation reaction of neopullulanase. Appl. Environ. Microbiol. 59:953–59
    [Google Scholar]
  70. Kuttiyawong K, Saehu S, Ito K, Pongsawasdi P. 2015. Synthesis of large-ring cyclodextrin from tapioca starch by amylomaltase and complex formation with vitamin E acetate for solubility enhancement. Process Biochem 50:2168–76
    [Google Scholar]
  71. Kwon KS, Auh JH, Choi SK, Kang GJ, Kim JW, Park KH. 1999. Characterization of branched oligosaccharides produced by Bacillus licheniformis maltogenic amylase. J. Food Sci. 64:258–61
    [Google Scholar]
  72. Lee BH, Koh DW, Territo PR, Park CS, Hamaker BR, Yoo SH. 2015. Enzymatic synthesis of 2-deoxyglucose-containing maltooligosaccharides for tracing the location of glucose absorption from starch digestion. Carbohydr. Polym. 132:41–49
    [Google Scholar]
  73. Lee ES, Song EJ, Nam YD, Nam TG, Kim HJ et al. 2020. Effects of enzymatically modified chestnut starch on the gut microbiome, microbial metabolome, and transcriptome of diet-induced obese mice. Int. J. Biol. Macromol. 145:235–43
    [Google Scholar]
  74. Lee HS, Auh JH, Yoon HG, Kim MJ, Park JH et al. 2002a. Cooperative action of α-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production. J. Agric. Food Chem. 50:2812–17
    [Google Scholar]
  75. Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ et al. 2002b. Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J. Biol. Chem. 277:21891–97
    [Google Scholar]
  76. Lee KY, Kim YR, Park KH, Lee HG. 2006. Effects of α-glucanotransferase treatment on the thermo-reversibility and freeze-thaw stability of a rice starch gel. Carbohydr. Polym. 63:347–54
    [Google Scholar]
  77. Lee KY, Kim YR, Park KH, Lee HG. 2008. Rheological and gelation properties of rice starch modified with 4-α-glucanotransferase. Int. J. Biol. Macromol. 42:298–304
    [Google Scholar]
  78. Leemhuis H, Dobruchowska JM, Ebbelaar M, Faber F, Buwalda PL et al. 2014. Isomalto/malto-polysaccharide, a novel soluble dietary fiber made via enzymatic conversion of starch. J. Agric. Food Chem. 62:12034–44
    [Google Scholar]
  79. Lekakarn H, Bunterngsook B, Pajongpakdeekul N, Prongjit D, Champreda V 2022. A novel low temperature active maltooligosaccharides-forming amylase from Bacillus koreensis HL12 as biocatalyst for maltooligosaccharide production. 3 Biotech 12:134
    [Google Scholar]
  80. Leman P, Goesaert H, Delcour JA. 2009. Residual amylopectin structures of amylase-treated wheat starch slurries reflect amylase mode of action. Food Hydrocoll 23:153–64
    [Google Scholar]
  81. Leman P, Goesaert H, Vandeputte GE, Lagrain B, Delcour JA. 2005. Maltogenic amylase has a nontypical impact on the molecular and rheological properties of starch. Carbohydr. Polym. 62:205–13
    [Google Scholar]
  82. Letona CAM, Park CS, Kim YR. 2017. Amylosucrase-mediated β-carotene encapsulation in amylose microparticles. Biotechnol. Prog. 33:1640–46
    [Google Scholar]
  83. Li C, Wu A, Yu W, Hu Y, Li E et al. 2020. Parameterizing starch chain-length distributions for structure-property relations. Carbohydr. Polym. 241:116390
    [Google Scholar]
  84. Li D, Fei T, Wang Y, Zhao Y, Dai L et al. 2020. A cold-active 1,4-α-glucan branching enzyme from Bifidobacterium longum reduces the retrogradation and enhances the slow digestibility of wheat starch. Food Chem 324:126855
    [Google Scholar]
  85. Li D, Park SH, Shim JH, Lee HS, Tang SY et al. 2004. In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase. Carbohydr. Res. 339:2789–97
    [Google Scholar]
  86. Li D, Zhao Y, Fei T, Wang Y, Lee BH et al. 2019. Effects of Streptococcus thermophilus GtfB enzyme on dough rheology, bread quality and starch digestibility. Food Hydrocoll 96:134–39
    [Google Scholar]
  87. Li J, Kong X, Ai Y 2022. Modification of granular waxy, normal and high-amylose maize starches by maltogenic α-amylase to improve functionality. Carbohydr. Polym. 290:119503
    [Google Scholar]
  88. Li W, Li C, Cheng L, Hong Y, Qiu Y et al. 2016. Relationship between structure and retrogradation properties of corn starch treated with 1,4-α-glucan branching enzyme. Food Hydrocoll 52:868–75
    [Google Scholar]
  89. Li X, Fei T, Wang Y, Zhao Y, Pan Y, Li D. 2018. Wheat starch with low retrogradation properties produced by modification of the GtfB enzyme 4,6-α-glucanotransferase from Streptococcus thermophilus. J. Agric. Food Chem. 66:3891–98
    [Google Scholar]
  90. Li X, Li D, Tian H, Park KH. 2014a. Reducing retrogradation of gelatinized rice starch and rice meal under low temperature storage by addition of extremely thermostable maltogenic amylase during their cooking. Food Res. Int. 62:1134–40
    [Google Scholar]
  91. Li X, Miao M, Jiang H, Xue J, Jiang B et al. 2014b. Partial branching enzyme treatment increases the low glycaemic property and α-1,6 branching ratio of maize starch. Food Chem 164:502–9
    [Google Scholar]
  92. Li X, Wang Y, Mu S, Ji X, Zeng C et al. 2022. Structure, retrogradation and digestibility of waxy corn starch modified by a GtfC enzyme from Geobacillus sp. 12AMOR1. Food Biosci 46:101527
    [Google Scholar]
  93. Li Y, Li C, Gu Z, Hong Y, Cheng L, Li Z. 2017. Effect of modification with 1,4-α-glucan branching enzyme on the rheological properties of cassava starch. Int. J. Biol. Macromol. 103:630–39
    [Google Scholar]
  94. Lim MC, Park KH, Choi JH, Lee DH, Letona CAM et al. 2016. Effect of short-chain fatty acids on the formation of amylose microparticles by amylosucrase. Carbohydr. Polym. 151:606–13
    [Google Scholar]
  95. MacGregor EA. 2005. An overview of clan GH-H and distantly-related families. Biologia 60:5–12
    [Google Scholar]
  96. Martinez MM, Li C, Okoniewska M, Mukherjee I, Vellucci D, Hamaker BR. 2018. Slowly digestible starch in fully gelatinized material is structurally driven by molecular size and A and B1 chain lengths. Carbohydr. Polym. 197:531–39
    [Google Scholar]
  97. Matalanis AM, Campanella OH, Hamaker BR. 2009. Storage retrogradation behavior of sorghum, maize and rice starch pastes related to amylopectin fine structure. J. Cereal Sci. 50:74–81
    [Google Scholar]
  98. Meng X, Gangoiti J, de Kok N, van Leeuwen SS, Pijning T, Dijkhuizen L. 2018. Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. Food Chem 253:236–46
    [Google Scholar]
  99. Miao M, Hamaker BR. 2021. Food matrix effects for modulating starch bioavailability. Annu. Rev. Food Sci. Technol. 12:169–91
    [Google Scholar]
  100. Miao M, Jiang B, Cui SW, Zhang T, Jin Z 2015a. Slowly digestible starch: a review. Crit. Rev. Food Sci. Nutr. 55:1642–57
    [Google Scholar]
  101. Miao M, Jiang B, Jin Z, BeMiller JN 2018. Microbial starch-converting enzymes: recent insights and perspectives. Comp. Rev. Food Sci. Food Saf. 17:1238–60
    [Google Scholar]
  102. Miao M, Jiang B, Zhang T. 2009. Effect of pullulanase debranching and recrystallization on structure and digestibility of waxy maize starch. Carbohydr. Polym. 112:214–21
    [Google Scholar]
  103. Miao M, Ma Y, Jiang B, Cui SW, Wu S, Zhang T. 2015b. Structural elucidation and in vitro fermentation of extracellular α-D-glucan from Lactobacillus reuteri SK24.003. Bioact. Carbohydr. Diet. Fiber 6:109–16
    [Google Scholar]
  104. Miao M, Xiong S, Ye F, Jiang B, Cui SW, Zhang T. 2014. Development of maize starch with a slow digestion property using maltogenic α-amylase. Carbohydr. Polym. 103:164–69
    [Google Scholar]
  105. Min BC, Yoon SH, Kim JW, Lee YW, Kim YB, Park KH. 1998. Cloning of novel maltooligosaccharide-producing amylases as antistaling agents for bread. J. Agric. Food Chem. 46:779–82
    [Google Scholar]
  106. Mirza O, Skov LK, Remaud-Simeon M, de Montalk GP, Albenne C et al. 2001. Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose. Biochemistry 40:9032–39
    [Google Scholar]
  107. Mistry RH, Borewicz K, Gu F, Verkade HJ, Schols HA et al. 2020. Dietary isomalto/malto-polysaccharides increase fecal bulk and microbial fermentation in mice. Mol. Nutr. Food Res. 64:e2000251
    [Google Scholar]
  108. Nagarajan DR, Rajagopalan G, Krishnan C 2006. Purification and characterization of a maltooligosaccharide-forming α-amylase from a new Bacillus subtilis KCC103. Appl. Microbiol. Biotechnol. 73:591–97
    [Google Scholar]
  109. Nimpiboon P, Tumhom S, Nakapong S, Pongsawasdi P. 2020. Amylomaltase from Thermus filiformis: expression in Saccharomyces cerevisiae and its use in starch modification. J. Appl. Microbiol. 129:1287–96
    [Google Scholar]
  110. Nokkaew N, Srihirun K. 2020. Fluid containing highly branched cyclic dextrin: an alternative method to enhance endurance exercise performance. Res. Investig. Sports Med. 6:528–29
    [Google Scholar]
  111. Oh EJ, Choi SJ, Lee SJ, Kim CH, Moon TW. 2008. Modification of granular corn starch with 4-α-glucanotransferase from Thermotoga maritima: effects on structural and physical properties. J. Food Sci. 73:158–66
    [Google Scholar]
  112. Park HR, Rho SJ, Kim YR. 2019. Solubility, stability, and bioaccessibility improvement of curcumin encapsulated using 4-α-glucanotransferase-modified rice starch with reversible pH-induced aggregation property. Food Hydrocoll 95:19–32
    [Google Scholar]
  113. Park JH, Kim HJ, Kim YH, Cha H, Kim YW et al. 2007. The action mode of Thermus aquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin. Carbohydr. Polym. 67:164–73
    [Google Scholar]
  114. Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B. 2000. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochem. Biophys. Acta 1478:165–85
    [Google Scholar]
  115. Park MO, Chandrasekaran M, Yoo SH. 2019. Production and characterization of low-calorie turanose and digestion-resistant starch by an amylosucrase from Neisseria subflava. Food Chem 300:125225
    [Google Scholar]
  116. Palomo M, Pijning T, Booiman T, Dobruchowska JM, van der Vlist J et al. 2011. Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed. J. Biol. Chem. 286:3520–30
    [Google Scholar]
  117. Potocki-Veronese G, Putaux JL, Dupeyre D, Albenne C, Remaud-Siméon M et al. 2005. Amylose synthesized in vitro by amylosucrase: morphology, structure, and properties. Biomacromolecules 6:1000–11
    [Google Scholar]
  118. Putaux JL, Buléon A, Chanzy H. 2000. Network formation in dilute amylose and amylopectin studied by TEM. Macromolecules 33:6416–22
    [Google Scholar]
  119. Putaux JL, Potocki-Véronèse G, Remaud-Simeon M, Buleon A. 2006. α-D-glucan-based dendritic nanoparticles prepared by in vitro enzymatic chain extension of glycogen. Biomacromolecules 7:1720–28
    [Google Scholar]
  120. Ren J, Li Y, Li C, Gu Z, Cheng L et al. 2017. Pasting and thermal properties of waxy corn starch modified by 1,4-α-glucan branching enzyme. Int. J. Biol. Macromol. 97:679–87
    [Google Scholar]
  121. Roblin P, Potocki-Véronèse G, Guieysse D, Guerin F, Axelos MA et al. 2013. SAXS conformational tracking of amylose synthesized by amylosucrases. Biomacromolecules 14:232–39
    [Google Scholar]
  122. Rolland-Sabate A, Colonna P, Potocki-Veronese G, Monsan P, Planchot V. 2004. Elongation and insolubilisation of α-glucans by the action of Neisseria polysaccharea amylosucrase. J. Cereal Sci. 40:17–30
    [Google Scholar]
  123. Rudeekulthamrong P, Kaulpiboon J. 2020. Optimization of amylomaltase for the synthesis of α-arbutin derivatives as tyrosinase inhibitors. Carbohydr. Res. 494:108078
    [Google Scholar]
  124. Ryu JJ, Li X, Lee ES, Li D, Lee BH 2022. Slowly digestible property of highly branched α-limit dextrins produced by 4,6-α-glucanotransferase from Streptococcus thermophilus evaluated in vitro and in vivo. Carbohydr. Polym. 275:118685
    [Google Scholar]
  125. Seo NS, Roh SA, Auh JH, Park JH, Kim YR, Park KH. 2007. Structural characterization of rice starch in rice cake modified by Thermus scotoductus 4-α-glucanotransferase (TSαGTase). J. Food Sci. 72:331–36
    [Google Scholar]
  126. Shen X, Bertoft E, Zhang G, Hamaker BR. 2013. Iodine binding to explore the conformational state of internal chains of amylopectin. Carbohydr. Polym. 98:778–83
    [Google Scholar]
  127. Shin HJ, Choi SJ, Park CS, Moon TW. 2010. Preparation of starches with low glycaemic response using amylosucrase and their physicochemical properties. Carbohydr. Polym. 82:489–97
    [Google Scholar]
  128. Shinohara ML, Ihara M, Abo M, Hashida M, Takagi S, Beck TC. 2001. A novel thermostable branching enzyme from an extremely thermophilic bacterial species, Rhodothermus obamensis. Appl. Microbiol. Biotechnol. 57:653–59
    [Google Scholar]
  129. Sun L, Miao M. 2020. Dietary polyphenols modulate starch digestion and glycaemic level: a review. Crit. Rev. Food Sci. Nutr. 60:541–55
    [Google Scholar]
  130. Takata H, Akiyama T, Kajiura H, Kakutani R, Furuyashiki T et al. 2010. Application of branching enzyme in starch processing. Biocatal. Biotransform. 28:60–63
    [Google Scholar]
  131. Takata H, Kuriki T, Okada S, Takesada Y, Iizuka M et al. 1992. Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1→4)- and α-(1→6)-glucosidic linkages. J. Biol. Chem. 267:18447–52
    [Google Scholar]
  132. Tao KY, Li C, Yu WW, Gilbert RG, Li EP. 2019. How amylose molecular fine structure of rice starch affects functional properties. Carbohydr. Polym. 204:24–31
    [Google Scholar]
  133. Te Poele EM, van der Hoek SE, Chatziioannou AC, Gerwig GJ, Duisterwinkel WJ et al. 2021. GtfC enzyme of Geobacillus sp. 12AMOR1 represents a novel thermostable type of GH70 4,6-α-glucanotransferase that synthesizes a linear alternating (α1→6)/(α1→4) α-glucan and delays bread staling. J. Agric. Food Chem. 69:9859–68
    [Google Scholar]
  134. Vamadevan V, Bertoft E. 2018. Impact of different structural types of amylopectin on retrogradation. Food Hydrocoll 80:88–96
    [Google Scholar]
  135. van der Maarel MJEC, van der Veen B, Uitdehaag JCM, Leemhuis H, Dijkhuizen L 2002. Properties and applications of starch-converting enzymes of the α-amylase family. J. Biotechnol. 94:137–55
    [Google Scholar]
  136. van der Maarel MJEC, Vos A, Sanders P, Dkjkhuizen L. 2003. Properties of the glucan branching enzyme of the hyperthermophilic bacterium Aquifex aeolicus. Biocatal. Biotransform. 21:199–207
    [Google Scholar]
  137. van der Zaal PH, Klostermann CE, Schols HA, Bitter JH, Buwalda PL. 2019. Enzymatic fingerprinting of isomalto/malto-polysaccharides. Carbohydr. Polym. 205:279–86
    [Google Scholar]
  138. Wang R, Zhang T, He J, Zhang H, Zhou X et al. 2020. Tailoring digestibility of starches by chain elongation using amylosucrase from Neisseria polysaccharea via a zipper reaction mode. J. Agric. Food. Chem. 68:225–34
    [Google Scholar]
  139. Wang Y, Chen C, Hu X, Campanella OH, Miao M 2022. Fabrication and characterizations of cyclic amylopectin-based delivery system incorporated with β-carotene. Food Hydrocoll 130:107680
    [Google Scholar]
  140. Wilburn D, Machek S, Ismaeel A. 2021. Highly branched cyclic dextrin and its ergogenic effects in athletes: a brief review. J. Exerc. Nutr. 4:15
    [Google Scholar]
  141. Woo GJ, McCord JD. 1993. Bioconversion of unmodified native starches by Pseudomonas stutzeri maltotetraohydrolase: effect of starch type. Appl. Microbiol. Biotechnol. 38:586–91
    [Google Scholar]
  142. Wu C, Zhou X, Tian Y, Xu X, Jin Z 2017. Hydrolytic mechanism of α-maltotriohydrolase on waxy maize starch and retrogradation properties of the hydrolysates. Food Hydrocoll 66:136–43
    [Google Scholar]
  143. Yang Y, Zhao X, Zhang T, Hamaker BR, Miao M. 2021. Development of a novel starch-based dietary fiber using glucanotransferase. Food Funct 12:5745–54
    [Google Scholar]
  144. Zhang G, Ao Z, Hamaker BR. 2008. Nutritional property of endosperm starches from maize mutants: a parabolic relationship between slowly digestible starch and amylopectin fine structure. J. Agric. Food Chem. 56:4686–94
    [Google Scholar]
  145. Zhang X, Leemhuis H, van der Maarel MJEC. 2020. Digestion kinetics of low, intermediate and highly branched maltodextrins produced from gelatinized starches with various microbial glycogen branching enzymes. Carbohydr. Polym. 247:116729
    [Google Scholar]
  146. Zhou X, Campanella OH, Hamaker BR, Miao M. 2021. Deciphering molecular interaction and digestibility in retrogradation of amylopectin gel network. Food Funct 12:11460–68
    [Google Scholar]
  147. Zhu F, Corke H, Bertoft E. 2011. Amylopectin internal molecular structure in relation to physical properties of sweet potato starch. Carbohydr. Polym. 84:907–18
    [Google Scholar]
/content/journals/10.1146/annurev-food-072122-023510
Loading
/content/journals/10.1146/annurev-food-072122-023510
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error