Whole-cell biosynthesis of d-tagatose from maltodextrin by engineered Escherichia coli with multi-enzyme co-expression system

Dai, Yiwei; Li, Mengli; Jiang, Bo; Zhang, Tao; Chen, Jingjing

doi:10.1016/j.enzmictec.2021.109747

Cited by 9 publications

(5 citation statements)

References 24 publications

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“…To fulfill the needs of people for sugar reduction and diabetes, green and healthy sugar substitutes have a large market potential. d -Tagatose is a type of healthy sugar substitute, the sweetness of which is highly similar to that of sucrose, with only one-third of the calories of sucrose. − In 2000, d -tagatose was approved by the US Food and Drug Administration as generally recognized as safe (GRAS). , d -Tagatose has many physiological benefits, such as low calorie intake, low glycemic index, anticaries, antioxidation, prebiotics, improvement of intestinal function, and enhancement of immunity. It could be widely used in food, beverage, medicine, health care, and other health-relevant fields, with great economic potential .…”

Section: Introductionmentioning

confidence: 99%

“…They also coexpressed five enzymes in one E. coli host and used heat-treated whole cells to produce tagatose from starch. 1 Clearly, the above in vitro biosynthetic route, regardless of nonimmobilized enzymes or enzyme-containing whole cells, could have high potential in producing high-yield tagatose from inexpensive starch and maltodextrin. Nonetheless, prolonging the lifetime of enzymes accompanied by decreasing enzyme costs is urgently needed.…”

Section: ■ Introductionmentioning

confidence: 99%

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Synthesis of a Healthy Sweetener d-Tagatose from Starch Catalyzed by Semiartificial Cell Factories

Han

et al. 2023

J. Agric. Food Chem.

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d-Tagatose is one of the several healthy sweeteners that can be a substitute for sucrose and fructose in our daily life. Whole cell-catalyzed phosphorylation and dephosphorylation previously reported by our group afford a thermodynamic-driven strategy to achieve tagatose production directly from starch with high product yields. Nonetheless, the poor structural stability of cells and difficulty in biocatalyst recycling restrict its practical application. Herein, an efficient and stable semiartificial cell factory (SACF) was developed by constructing an organosilica network (OSN) artificial shell on the cells bearing five thermophilic enzymes to produce tagatose. The OSN artificial shell, the thickness of which can be regulated by changing the tetraethyl silicate concentration, exhibited tunable permeability and superior mechanical strength. In contrast with cells, SACFs showed a relative activity of 99.5% and an extended half-life from 33.3 to 57.8 h. Over 50% of initial activity was retained after 20 reuses. The SACFs can catalyze seven consecutive reactions with tagatose yields of over 40.7% in field applications.

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Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Synthesis of a Healthy Sweetener d-Tagatose from Starch Catalyzed by Semiartificial Cell Factories

Han

et al. 2023

J. Agric. Food Chem.

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“…However, a large amount of cofactors (ATP) increased the cost. A five-enzyme cascade route (e.g., αglucan phosphorylase, phosphoglucomutase, glucose 6-phosphate isomerase, D-tagatose 1,6-bisphosphate aldolase, and phosphoglycolate phosphatase) designed to generate Dtagatose from maltodextrin led to a final conversion of 20.8% [18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Novel In Vitro Multienzyme Cascade for Efficient Synthesis of d-Tagatose from Sucrose

Liu,

Tu,

et al. 2023

Catalysts

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d-Tagatose is a rare sugar with low calories, and is extensively used in food, beverage, and drug additives. In this study, an in vitro multienzyme cascade route for d-tagatose synthesis from sucrose (MCTS) was designed, which contains five enzymes (sucrose phosphorylase, fructokinase, d-fructose 6-phosphate 4-epimerase, d-tagatose 6-phosphate phosphatase, and polyphosphate kinase). The whole MCTS route comprised a sucrose phosphorylation reaction, and a phosphorylation–dephosphorylation reaction coupled with an ATP regeneration system. After optimization, the conversion of d-tagatose from 10 mM sucrose reached 82.3%. At an elevated sucrose concentration of 50 mM, 72.4% of d-tagatose conversion and 0.27 g·L–1·h−1 of space–time yield were obtained. Furthermore, ADP consumption decreased to 1% of the sucrose concentration after introducing the ATP regeneration system. The MCTS strategy is an efficient and cost-effective approach for d-tagatose production.

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“…d ‐tagatose is a rare low‐calorie sugar with similar sweetness characteristics to sucrose, but only accounts for 38% of the energy of sucrose (Zheng et al, 2019). As early as 2001, d ‐tagatose obtained the generally recognized safe food (GRAS) certification of the FDA (Dai et al, 2021). d ‐tagatose has the functions of inhibiting high blood sugar, improving intestinal flora, and anticaries.…”

Section: Introductionmentioning

confidence: 99%

Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

Liu

Jiang

Zhang

et al. 2022

Food Bioengineering

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As a rare low-calorie sugar with special medicinal value, D-tagatose is widely used in the field of food, beverages, medicine, and cosmetics. However, enzymatic D-tagatose production in vitro is commonly limited to low conversion efficiency and poor thermo-stability. Herein, taking advantage of the self-assembling property of protein scaffold EutM (ethanolamine bacterial microcompartments), Spy and Snoop peptide pairs was used to drive the linkage between the EutM and cargo proteins, βgalactosidase (BagB), and L-arabinose isomerase (TMAI) to construct a dual-enzymes cascade and realize the D-tagatose production from lactose. The optimal conditions of the cascade were shown to be pH of 8.0, temperature of 60°C, 100 g/L lactose as substrate with supplementing 5 mM Mn 2+ . When the ratio of immobilized enzymes to EutM scaffold reached 1:6, the D-tagatose productivity of the dual-enzymes cascade could reach 1.03 g/L/h, which was 1.24-fold higher than free enzymes. In addition, the EutM-based scaffold could efficiently improve the stability of immobilized enzymes, in which 45% of the activity remained after 12 h, 2.14-fold higher than the free one. Overall, an attractive EutM-based selfassembling platform immobilizing BagB and TMAI was developed, showing enhanced catalysis efficiency and enzyme thermo-stability for D-tagatose production.

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Whole-cell biosynthesis of d-tagatose from maltodextrin by engineered Escherichia coli with multi-enzyme co-expression system

Cited by 9 publications

References 24 publications

Synthesis of a Healthy Sweetener d-Tagatose from Starch Catalyzed by Semiartificial Cell Factories

Synthesis of a Healthy Sweetener d-Tagatose from Starch Catalyzed by Semiartificial Cell Factories

Novel In Vitro Multienzyme Cascade for Efficient Synthesis of d-Tagatose from Sucrose

Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

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