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International Journal of Biological Macromolecules
D-allulose, a low-calorie functional sweetener, is produced by the enzymatic conversion of d-fructose via D-allulose 3-epimerase (DAE) and holds significant market potential, particularly for individuals with obesity and diabetes. However, the limited reusability and stability of DAE have restricted its industrial application.
Ziqun Xiao, Jingjing Chen
exaly +3 more sources
D-allulose, a low-calorie functional sweetener, is produced by the enzymatic conversion of d-fructose via D-allulose 3-epimerase (DAE) and holds significant market potential, particularly for individuals with obesity and diabetes. However, the limited reusability and stability of DAE have restricted its industrial application.
Ziqun Xiao, Jingjing Chen
exaly +3 more sources
Elucidation of d-allulose recognition mechanism in ketose 3-epimerase
Journal of Bioscience and Bioengineeringd-Allulose is a low-calorie sweetener with multiple nutritional functions that can be produced through d-fructose isomerization by ketose 3-epimerase (KEase). l-Ribulose 3-epimerase from Arthrobacterglobiformis (AgLRE) is one of the most important enzymes that produce d-allulose; however, its substrate recognition mechanism is unknown.
Masahiro Watanabe +2 more
openaire +2 more sources
International Journal of Biological Macromolecules, 2018
d-Allulose 3-epimerase (DAEase) catalyzes the epimerization between d-fructose and d-allulose. We had PCR-cloned and overexpressed the gene encoding Agrobacterium sp. ATCC 31749 DAEase (AsDAEase) in Escherichia coli. A high yield of active AsDAEase, 35,300U/L or 1350U/g of wet cells, was acquired with isopropyl β-d-1-thiogalactopyranoside induction at ...
Wen-Chi Tseng, Tsuei-Yun Fang
exaly +3 more sources
d-Allulose 3-epimerase (DAEase) catalyzes the epimerization between d-fructose and d-allulose. We had PCR-cloned and overexpressed the gene encoding Agrobacterium sp. ATCC 31749 DAEase (AsDAEase) in Escherichia coli. A high yield of active AsDAEase, 35,300U/L or 1350U/g of wet cells, was acquired with isopropyl β-d-1-thiogalactopyranoside induction at ...
Wen-Chi Tseng, Tsuei-Yun Fang
exaly +3 more sources
[Construction and immobilization of recombinant Bacillus subtilis with D-allulose 3-epimerase].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2022D-allulose-3-epimerase (DPEase) is the key enzyme for isomerization of D-fructose to D-allulose. In order to improve its thermal stability, short amphiphilic peptides (SAP) were fused to the N-terminal of DPEase. SDS-PAGE analysis showed that the heterologously expressed DPEase folded correctly in Bacillus subtilis, and the protein size was 33 kDa ...
Yuxia, Wei +6 more
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Process Biochemistry, 2020
Abstract Inulin has been widely used as a cheap bioresource for producing many valuable products by enzymatic hydrolysis or microbial fermentation, such as high-fructose syrup and fructooligosaccharides. In this work, a one-pot two-enzyme reaction system was developed to produce d -allulose from inulin using A. piperis exoinulinase and Dorea sp. d -
Wen Li +5 more
openaire +1 more source
Abstract Inulin has been widely used as a cheap bioresource for producing many valuable products by enzymatic hydrolysis or microbial fermentation, such as high-fructose syrup and fructooligosaccharides. In this work, a one-pot two-enzyme reaction system was developed to produce d -allulose from inulin using A. piperis exoinulinase and Dorea sp. d -
Wen Li +5 more
openaire +1 more source
Protein Expression and Purification, 2022
d-allulose, a rare sugar that is scarce in nature, exerts several beneficial effects and has commercial potential. d-allulose 3-epimerase (DAEase) plays a vital role in catalyzing the isomerization from d-fructose to d-allulose. However, the industrial application of DAEase for d-allulose production is hindered by its poor long-term thermostability. In
Huiyi Wang +5 more
openaire +2 more sources
d-allulose, a rare sugar that is scarce in nature, exerts several beneficial effects and has commercial potential. d-allulose 3-epimerase (DAEase) plays a vital role in catalyzing the isomerization from d-fructose to d-allulose. However, the industrial application of DAEase for d-allulose production is hindered by its poor long-term thermostability. In
Huiyi Wang +5 more
openaire +2 more sources
Biotechnology Journal
AbstractBackgroundD‐Allulose is one of the most well‐known rare sugars widely used in food, cosmetics, and pharmaceutical industries. The most popular method for D‐allulose production is the conversion from D‐fructose catalyzed by D‐allulose 3‐epimerase (DAEase).
Zijie Li +6 more
openaire +2 more sources
AbstractBackgroundD‐Allulose is one of the most well‐known rare sugars widely used in food, cosmetics, and pharmaceutical industries. The most popular method for D‐allulose production is the conversion from D‐fructose catalyzed by D‐allulose 3‐epimerase (DAEase).
Zijie Li +6 more
openaire +2 more sources
International Journal of Biological Macromolecules
D-allulose, a low-calorie rare sugar catalyzed by D-allulose 3-epimerase (DAE), is highly sought after for its potential health benefits. However, poor reusability and stability of DAE limited its popularization in industrial applications. Although metal-organic frameworks (MOFs) offer a promising enzyme platform for enzyme immobilization, developing ...
Huayang, Tang +4 more
openaire +2 more sources
D-allulose, a low-calorie rare sugar catalyzed by D-allulose 3-epimerase (DAE), is highly sought after for its potential health benefits. However, poor reusability and stability of DAE limited its popularization in industrial applications. Although metal-organic frameworks (MOFs) offer a promising enzyme platform for enzyme immobilization, developing ...
Huayang, Tang +4 more
openaire +2 more sources
Bioprocess and Biosystems Engineering
D-Allulose 3-epimerase (DAE) is a vital biocatalyst for the industrial synthesis of D-allulose, an ultra-low calorie rare sugar. However, limited thermostability of DAEs hinders their use at high-temperature production. In this research, hyperthermophilic TI-DAE (Tm = 98.4 ± 0.7 ℃) from Thermotoga sp. was identified via in silico screening.
Ji-Dong, Shen +8 more
openaire +2 more sources
D-Allulose 3-epimerase (DAE) is a vital biocatalyst for the industrial synthesis of D-allulose, an ultra-low calorie rare sugar. However, limited thermostability of DAEs hinders their use at high-temperature production. In this research, hyperthermophilic TI-DAE (Tm = 98.4 ± 0.7 ℃) from Thermotoga sp. was identified via in silico screening.
Ji-Dong, Shen +8 more
openaire +2 more sources
International Journal of Biological Macromolecules
D-allulose is a rare, low-calorie sugar substitute with multiple physiological functions and is widely used in food and pharmaceutical industries. D-allulose is primarily produced by the catalytic conversion of d-fructose via D-allulose 3-epimerase (DAEase). In this study, a DAEase gene, dpema4, was isolated from an Antarctic bacterium and expressed in
Jingqi, Li +4 more
openaire +2 more sources
D-allulose is a rare, low-calorie sugar substitute with multiple physiological functions and is widely used in food and pharmaceutical industries. D-allulose is primarily produced by the catalytic conversion of d-fructose via D-allulose 3-epimerase (DAEase). In this study, a DAEase gene, dpema4, was isolated from an Antarctic bacterium and expressed in
Jingqi, Li +4 more
openaire +2 more sources