D-Allulose Production from D-Fructose by Permeabilized Recombinant Cells of Corynebacterium glutamicum Cells Expressing D-Allulose 3-Epimerase Flavonifractor plautii

Park, Chul-Soon; Kim, Tae-Yong; Hong, Sunwook; Shin, Kyung‐Chul; Kim, Kyoung-Rok; Oh, Deok‐Kun

doi:10.1371/journal.pone.0160044

Cited by 46 publications

(21 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Metal ion Mn 2+ could enhance the thermostability of PDAE and retained more than 80% activity at 50°C (Figure d). When PDAE was incubated with 0.1 mM Mn 2+ , the half‐life extended to 140 min at 60°C which was similar to that of DAE from F. plautii (Park, Kim, et al, ). The substrate specificity of PDAE was further measured for four ketohexoses: D ‐fructose, D ‐allulose, D ‐tagatose, and D ‐sorbose.…”

Section: Resultssupporting

confidence: 57%

“…In this study, the specific productivity of strain DAE16 under 750 g/L fructose was 56.8 g·g −1 ·hr −1 (Table ). This value was 1.6‐fold higher than that of another recombinant C. glutamicum strain expressing DAE from F. plautii (Park, Kim, et al, ) but lower than the highest reported production values of 86.2 g·g −1 ·hr −1 using the recombinant E. coli cells expressing the double‐site variant (I33L‐S213C) DAE from Agrobacterium tumefaciens (Park, Park, et al, ; Table ). The initial D ‐allulose production rate of strain C‐DAE9 within 1 hr was with 83 g·g −1 ·hr −1 (Figure a).…”

Section: Resultsmentioning

confidence: 67%

“…To date, at least 15 kinds of D ‐tagatose 3‐epimerase (DTE) and D ‐allulose 3‐epimerase (DAE) have been verified, such as DTE from Pseudomonas cichorii (Yoshida et al, ), Clostridium sp. (Mu et al, ); DAE from Treponema primitia (Zhang, Zhang, Jiang, & Mu, ), Flavonifractor plautii (Park, Kim, et al, ), Arthrobacter globiformis M30 (Yoshihara et al, ), Agrobacterium sp. ATCC 31749 (Tseng et al, ), and so on.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Yang

Tian

Zhang

et al. 2019

Biotech & Bioengineering

View full text Add to dashboard Cite

D-Allulose 3-epimerase (DAE) has been applied to produce D-allulose, a low-calorie and functional sweetener. In this study, a new DAE from Paenibacillus senegalensis was characterized in Escherichia coli. Furthermore, we presented a tandem isoenzyme gene expression strategy to express multiple DAEs in one cell and construct foodgrade expression systems based on Corynebacterium glutamicum. Seventeen expression cassettes based on three DAE genes from different organisms were constructed.Among all recombinant strains, DAE16 harboring three DAE genes in an expression vector exhibited the highest enzyme activity with 22.7 U/mg. Whole-cell transformation of DAE16 produced 225 g/L D-allulose with a volumetric productivity of 353 g·g −1 ·hr −1 . The catalytic efficiency of strain C-DAE9 integrating total 11 DAE genes in chromosome was 16.4-fold higher than strains carrying one DAE. Fed-batch culture of C-DAE9 gave enzyme activity of 44,700 U/L. We also expressed a thermostable invertase in C. glutamicum and obtained enzyme activity of 29 U/mg. Immobilized cells expressing DAE or invertase exhibited 80% of retained activity after 30 cycles of catalytic reactions. Those immobilized cells were coupled to produce 61.2 g/L D-allulose from cane molasses in a two-step reaction process. This study provided an efficient approach for enzyme preparation and allowed access to produce D-allulose from other abundant and low-cost feedstock enriched with sucrose.

show abstract

Section: Resultssupporting

confidence: 57%

Section: Resultsmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Yang

Tian

Zhang

et al. 2019

Biotech & Bioengineering

View full text Add to dashboard Cite

show abstract

“…Rare sugars, ubiquitously found in nature as part of carbohydrate metabolism, are renowned for having a wide range of physiological functions. Many rare sugars possess 70–90% sweetness of sucrose and their low-calorie value allows these biomolecules to be valued by food industries (Park et al, 2016 ). As each rare sugar exerts its unique health benefits, the quest for many novel ways to produce rare sugars has become a key research area in the current decade.…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

et al. 2020

View full text Add to dashboard Cite

D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a Kcat/Km value of 45 mM−1min−1. The 500 g/L D-fructose, which corresponded to 30% conversion rate. With these interesting catalytic properties, this enzyme could be a promising candidate for industrial biocatalytic applications.

show abstract

“…Higher biocatalysis yields have been reached, for example 23% at 70°C when using purified DPEase from Dorea sp. CAG317 ( 44 ), 31% at 65°C when permeabilizing the membrane of cells ( 45 ) or even 70% at 45°C with a mutated DPEase from A. tumefaciens immobilized on a surface ( 46 ).…”

Section: Resultsmentioning

confidence: 99%

Biosensor-based enzyme engineering approach applied to psicose biosynthesis

et al. 2019

View full text Add to dashboard Cite

Bioproduction of chemical compounds is of great interest for modern industries, as it reduces their production costs and ecological impact. With the use of synthetic biology, metabolic engineering and enzyme engineering tools, the yield of production can be improved to reach mass production and cost-effectiveness expectations. In this study, we explore the bioproduction of D-psicose, also known as D-allulose, a rare non-toxic sugar and a sweetener present in nature in low amounts. D-psicose has interesting properties and seemingly the ability to fight against obesity and type 2 diabetes. We developed a biosensor-based enzyme screening approach as a tool for enzyme selection that we benchmarked with the Clostridium cellulolyticum D-psicose 3-epimerase for the production of D-psicose from D-fructose. For this purpose, we constructed and characterized seven psicose responsive biosensors based on previously uncharacterized transcription factors and either their predicted promoters or an engineered promoter. In order to standardize our system, we created the Universal Biosensor Chassis, a construct with a highly modular architecture that allows rapid engineering of any transcription factor-based biosensor. Among the seven biosensors, we chose the one displaying the most linear behavior and the highest increase in fluorescence fold change. Next, we generated a library of D-psicose 3-epimerase mutants by error-prone PCR and screened it using the biosensor to select gain of function enzyme mutants, thus demonstrating the framework’s efficiency.

show abstract

D-Allulose Production from D-Fructose by Permeabilized Recombinant Cells of Corynebacterium glutamicum Cells Expressing D-Allulose 3-Epimerase Flavonifractor plautii

Cited by 46 publications

References 33 publications

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

Biosensor-based enzyme engineering approach applied to psicose biosynthesis

Contact Info

Product

Resources

About