Production of <scp>d</scp>‐allulose from <scp>d</scp>‐glucose by <i>Escherichia coli</i> transformant cells co‐expressing <scp>d</scp>‐glucose isomerase and <scp>d</scp>‐psicose 3‐epimerase genes

Zhang, Wenli; Li, Hao; Jiang, Bo; Zhang, Tao; Mu, Wanmeng

doi:10.1002/jsfa.8193

Cited by 25 publications

(18 citation statements)

References 27 publications

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“…Cascade catalysis is considered as a very attractive approach compared with traditional step-by-step synthesis. This strategy is often used to produce rare sugars from inexpensive materials, such as sucrose, Jerusalem artichoke, inulin, and fruit/vegetable residues ( Figure 3 ; Wagner et al, 2015 ; Song et al, 2016 , 2017 ; Zhang et al, 2017 ; Yang et al, 2019 ; Li et al, 2020a ). D-Allulose has been efficiently synthesized from sucrose using purified recombinant invertase, D-xylose isomerase, and DTEase.…”

Section: Biological Production Of D-allulosementioning

confidence: 99%

“…Engineered Escherichia coli is one of the most commonly used organisms for the production of D-allulose because of its clear background, fast growth rates, simple culture, and stable genetics. DAEase and D-glucose isomerase (GIase) from Acidothermus cellulolyticus were coexpressed to produce D-allulose from D-glucose ( Zhang et al, 2017 ). Similarly, DAEase and xylose isomerase (XI) were coexpressed to produce D-allulose with D-glucose as the substrate ( Chen et al, 2017 ).…”

Section: Biological Production Of D-allulosementioning

confidence: 99%

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Recent Advances Regarding the Physiological Functions and Biosynthesis of D-Allulose

Zhou

Gao

2022

Front. Microbiol.

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D-Allulose, a generally regarded as safe (GRAS) sugar, is rare in nature. It is among the most promising sweeteners for future use due to its low caloric content, sucrose-like taste, and unique functions. D-Allulose has many physiological effects, such as antiobesity, antihyperglycemia, antidiabetes, anti-inflammatory, antioxidant, and neuroprotective effects. Therefore, D-allulose has important application value in the food, pharmaceutical, and healthcare industries. However, the high cost of D-allulose production limits its large-scale application. Currently, biotransformation is very attractive for D-allulose synthesis, with the two main methods of biosynthesis being the Izumoring strategy and the DHAP-dependent aldolase strategy. This article reviews recent advances regarding the physiological functions and biosynthesis of D-allulose. In addition, future perspectives on the production of D-allulose are presented.

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Section: Biological Production Of D-allulosementioning

confidence: 99%

Section: Biological Production Of D-allulosementioning

confidence: 99%

Recent Advances Regarding the Physiological Functions and Biosynthesis of D-Allulose

Zhou

Gao

2022

Front. Microbiol.

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“…In addition, the two enzymes are situated close together in space, creating a microenvironment rich in Dfructose for DPE, and reducing the diffusion time of Dfructose to DPE (Men et al, 2014). Zhang et al (2017) developed another recombinant E. coli strain that co-expressed both glucose isomerase and DPE. When 500 g/L glucose was used as the substrate, 204.3 g/L of D-fructose and 89.1 g/L of D-allulose could be obtained from D-glucose isomerase and DPE, respectively.…”

Section: Dual Enzyme Strategiesmentioning

confidence: 99%

Bioproduction of D‐allulose: Properties, applications, purification, and future perspectives

Jiang

et al. 2021

Comp Rev Food Sci Food Safe

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D-allulose is the C-3 epimer of D-fructose, which rarely exists in nature, and can be biosynthesized from D-fructose by the catalysis of D-psicose 3-epimerase. Dallulose is safe for human consumption and was recently approved by the United States Food and Drug Administration for food applications. It is not only able be used in food and dietary supplements as a low-calorie sweetener, but also modulates a variety of physiological functions. D-allulose has gained increasing attention owing to its excellent properties. This article presents a review of recent progress on the properties, applications, and bioproduction progress of D-allulose.

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“…It has been demonstrated that immobilization of whole cells via different polymers, agar, carrageenan, alginate gels, polyvinyl alcohol, or polyurethane foam, can effectively increase whole-cell stability and reusability [21][22][23][24][25]. Immobilized whole-cell systems can minimize damage from external environmental factors and maintain their stability under high-temperature conditions [26], immobilization technology was used for biocatalyst d-psicose production.…”

Section: Introductionmentioning

confidence: 99%

High production of d‐psicose from d‐fructose by immobilized whole recombinant Bacillus subtilis cells expressing d‐psicose 3‐epimerase from Agrobacterium tumefaciens

Wang

Sun

et al. 2021

Biotech and App Biochem

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D-Psicose 3-epimerase (DPEase) can catalyze the isomerization of D-fructose to be rare sugar D-psicose, which has wide application prospects in the food and medical fields. In this study, the DPEase gene from Agrobacterium tumefaciens was constructed into plasmid pMA5, and was successfully expressed in the host Bacillus subtilis WB600 (B. subtilis). After optimization of the fermentation conditions, whole recombinant B. subtilis WB600/pMA5-At-DEPase(O) cells produced D-psicose from D-fructose with a conversion rate of 29.01 ± 0.19%, which could be used for the efficient synthesis of D-psicose. To further improve the whole recombinant B. subtilis application, B. subtilis cells were immobilized onto a gel bead biocatalyst by Ca-alginate. After optimization of the biotransformation conditions, the conversion rate of the immobilized biocatalyst reached 20.74 ± 0.39%, which was lower than the free cells. However, the results showed that the immobilized biocatalyst had higher thermal/pH stability and storability, and the gel beads could be recycled for at least six batches. The results showed that the amount of D-psicose generated reached 32.83 ± 2.56 g/L with the immobilized biocatalyst after six times biotransformation, whereas the free cells produced only approximately 10.44 ± 0.07 g/L. The results showed that immobilized recombinant B. subtilis cells are promising to use for the efficient synthesis of D-psicose. ©

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Production of d‐allulose from d‐glucose by Escherichia coli transformant cells co‐expressing d‐glucose isomerase and d‐psicose 3‐epimerase genes

Cited by 25 publications

References 27 publications

Recent Advances Regarding the Physiological Functions and Biosynthesis of D-Allulose

Recent Advances Regarding the Physiological Functions and Biosynthesis of D-Allulose

Bioproduction of D‐allulose: Properties, applications, purification, and future perspectives

High production of d‐psicose from d‐fructose by immobilized whole recombinant Bacillus subtilis cells expressing d‐psicose 3‐epimerase from Agrobacterium tumefaciens

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