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<p>Maltodextrin is a widely used commodity in the global food industry; however, its applications are limited by physicochemical instability caused by varying degrees of polymerization and high reducing properties. In this study, an enzymatic cascade was developed to synthesize non-reducing maltodextrin with a single degree of polymerization (N-G7) using β-cyclodextrin (β-CD) as the substrate. Cyclodextrinase (CDase) hydrolyzed β-CD into linear oligosaccharides, followed by maltooligosyltrehalose synthase (MTSase)-catalyzed transglycosylation forming a terminal α-1,1-glycosidic bond, imparting non-reducing properties. The enzymatic synthesis of N-G7 was optimized through kinetic analysis, demonstrating that controlled enzyme loading and reaction durations improved yield by balancing CDase-mediated β-CD hydrolysis and MTSase-driven transglycosylation. Notably, fermentation enzyme activities of 38.31 U/mL for CDase and 475.44 U/mL for MTSase were achieved through separate fed-batch fermentations. The synergistic interaction between these enzymes was governed by Le Chatelier’s principle, where MTSase-mediated transglycosylation drove the equilibrium shift from β-CD hydrolysis (catalyzed by CDase) to N-G7 synthesis, ultimately achieving a 57.3% conversion rate in pilot-scale synthesis. After purification using sequential simulated moving bed (SSMB) chromatography, 191 g of N-G7 with 93.23% purity was obtained, yielding a total recovery of 23.9% from the initial β-CD. This study establishes a foundational framework in pilot-scale production of N-G7 with purity exceeding 93%. With uniform molecular size and non-reducing properties, N-G7 effectively prevents Maillard reactions during food processing and storage while providing enhanced stability across various industrial applications, including food preservation and cosmetic formulations.</p>

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Enhanced Enzymatic Synthesis of Non-Reducing Maltoheptaose Via Synergistic Cascade of Cyclodextrinase and Maltooligosyltrehalose Synthase

  • 期刊论文

  • 发表日期：

    2025年12月20日

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  • Luhua Zheng,
  • Xia Huang,
  • Bo Jiang,
  • Ruiqi Zhou,
  • Honghong Zheng,
  • Yuanfeng Wu

摘要

Maltodextrin is a widely used commodity in the global food industry; however, its applications are limited by physicochemical instability caused by varying degrees of polymerization and high reducing properties. In this study, an enzymatic cascade was developed to synthesize non-reducing maltodextrin with a single degree of polymerization (N-G7) using β-cyclodextrin (β-CD) as the substrate. Cyclodextrinase (CDase) hydrolyzed β-CD into linear oligosaccharides, followed by maltooligosyltrehalose synthase (MTSase)-catalyzed transglycosylation forming a terminal α-1,1-glycosidic bond, imparting non-reducing properties. The enzymatic synthesis of N-G7 was optimized through kinetic analysis, demonstrating that controlled enzyme loading and reaction durations improved yield by balancing CDase-mediated β-CD hydrolysis and MTSase-driven transglycosylation. Notably, fermentation enzyme activities of 38.31 U/mL for CDase and 475.44 U/mL for MTSase were achieved through separate fed-batch fermentations. The synergistic interaction between these enzymes was governed by Le Chatelier’s principle, where MTSase-mediated transglycosylation drove the equilibrium shift from β-CD hydrolysis (catalyzed by CDase) to N-G7 synthesis, ultimately achieving a 57.3% conversion rate in pilot-scale synthesis. After purification using sequential simulated moving bed (SSMB) chromatography, 191 g of N-G7 with 93.23% purity was obtained, yielding a total recovery of 23.9% from the initial β-CD. This study establishes a foundational framework in pilot-scale production of N-G7 with purity exceeding 93%. With uniform molecular size and non-reducing properties, N-G7 effectively prevents Maillard reactions during food processing and storage while providing enhanced stability across various industrial applications, including food preservation and cosmetic formulations.