Results 121 to 130 of about 1,259 (144)
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World Journal of Microbiology and Biotechnology, 2018
D-Allulose as a low-energy and special bioactive monosaccharide sugar is essential for human health. In this study, the D-psicose-3-epimerase gene (DPEase) of Agrobacterium tumefaciens was transferred into thermotolerant Kluyveromyces marxianus to decrease the production cost of D-allulose and reduce the number of manufacturing procedures.
Peizhou Yang +7 more
semanticscholar +3 more sources
D-Allulose as a low-energy and special bioactive monosaccharide sugar is essential for human health. In this study, the D-psicose-3-epimerase gene (DPEase) of Agrobacterium tumefaciens was transferred into thermotolerant Kluyveromyces marxianus to decrease the production cost of D-allulose and reduce the number of manufacturing procedures.
Peizhou Yang +7 more
semanticscholar +3 more sources
Journal of Molecular Catalysis B: Enzymatic, 2015
Abstract Ketose 3-epimerase displayed an important role in not only the cyclic monosaccharides bioconversion strategy, named Izumoring, but also in the industrial biological production of d -psicose, a novel low-calorie rare sugar widely used in food and medical industries.
Wenli Zhang +5 more
semanticscholar +2 more sources
Abstract Ketose 3-epimerase displayed an important role in not only the cyclic monosaccharides bioconversion strategy, named Izumoring, but also in the industrial biological production of d -psicose, a novel low-calorie rare sugar widely used in food and medical industries.
Wenli Zhang +5 more
semanticscholar +2 more sources
Immobilization of Clostridium cellulolyticum D-psicose 3-epimerase on artificial oil bodies.
Journal of Agricultural and Food Chemistry, 2014The rare sugar D-psicose possesses several fundamental biological functions. D-Psicose 3-epimerase from Clostridium cellulolyticum (CC-DPEase) has considerable potential for use in D-psicose production. In this study, CC-DPEase was fused to the N terminus of oleosin, a unique structural protein of seed oil bodies and was overexpressed in Escherichia ...
Chih-Wen Tseng +6 more
semanticscholar +3 more sources
Biotechnology and applied biochemistry, 2021
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.
Jianwei Wang +5 more
semanticscholar +1 more source
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.
Jianwei Wang +5 more
semanticscholar +1 more source
Applied Microbiology and Biotechnology, 2013
D-Tagatose 3-epimerase family enzymes can efficiently catalyze the epimerization of free keto-sugars, which could be used for D-psicose production from D-fructose. In previous studies, all optimum pH values of these enzymes were found to be alkaline. In this study, a D-psicose 3-epimerase (DPEase) with neutral pH optimum from Clostridium bolteae (ATCC ...
Min, Jia +6 more
openaire +2 more sources
D-Tagatose 3-epimerase family enzymes can efficiently catalyze the epimerization of free keto-sugars, which could be used for D-psicose production from D-fructose. In previous studies, all optimum pH values of these enzymes were found to be alkaline. In this study, a D-psicose 3-epimerase (DPEase) with neutral pH optimum from Clostridium bolteae (ATCC ...
Min, Jia +6 more
openaire +2 more sources
Preparation of d-psicose from d-fructose by immobilized d-tagatose 3-epimerase
Journal of Fermentation and Bioengineering, 1995Abstract d -Tagatose 3-epimerase ( d -TE) from Pseudomonas sp. ST-24 immobilized on Chitopearl beads of BCW 2503 was used in the preparation of d -psicose from d -fructose. When d -fructose solution (10%) was passed through a column packed with immobilized d -TE about 20% of the d -fructose was converted to d -psicose.
Hiromichi Itoh, Tomoko Sato, Ken Izumori
openaire +1 more source
Biotechnology Letters, 2009
A non-characterized gene, previously proposed as the D-tagatose-3-epimerase gene from Rhodobacter sphaeroides, was cloned and expressed in Escherichia coli. Its molecular mass was estimated to be 64 kDa with two identical subunits. The enzyme specificity was highest with D-fructose and decreased for other substrates in the order: D-tagatose, D-psicose,
Longtao, Zhang +3 more
openaire +2 more sources
A non-characterized gene, previously proposed as the D-tagatose-3-epimerase gene from Rhodobacter sphaeroides, was cloned and expressed in Escherichia coli. Its molecular mass was estimated to be 64 kDa with two identical subunits. The enzyme specificity was highest with D-fructose and decreased for other substrates in the order: D-tagatose, D-psicose,
Longtao, Zhang +3 more
openaire +2 more sources
Biotechnology Letters, 2017
To explore deactivation kinetics and the effects of some additives on the activity and conformational changes of D-psicose 3-epimerase (DPEase) during its storage.The experimental data of DPEase inactivation during storage at 4-45 °C fitted with the first-order expression model.
Qiao, Zhang +3 more
openaire +2 more sources
To explore deactivation kinetics and the effects of some additives on the activity and conformational changes of D-psicose 3-epimerase (DPEase) during its storage.The experimental data of DPEase inactivation during storage at 4-45 °C fitted with the first-order expression model.
Qiao, Zhang +3 more
openaire +2 more sources
Journal of Bioscience and Bioengineering, 2000
An improved process for the mass production of D-psicose from D-fructose was developed. A D-fructose solution (60%, pH 7.0) was passed at 45 degrees C through a column filled with immobilized D-tagatose 3-epimerase (D-TE) which was produced using recombinant Escherichia coli, and 25% of the substrate was converted to D-psicose. After epimerization, the
K, Takeshita +3 more
openaire +2 more sources
An improved process for the mass production of D-psicose from D-fructose was developed. A D-fructose solution (60%, pH 7.0) was passed at 45 degrees C through a column filled with immobilized D-tagatose 3-epimerase (D-TE) which was produced using recombinant Escherichia coli, and 25% of the substrate was converted to D-psicose. After epimerization, the
K, Takeshita +3 more
openaire +2 more sources
Enzyme and Microbial Technology, 2020
d-Psicose, as important rare sugar and epimer of d-fructose on the C-3 position, displays unique health benefits and physiological functions in various fields. The production of d-psicose is currently obtained via enzymatic bioconversion, mostly with of d-tagatose 3-epimerase.
Jun Zhang +9 more
openaire +3 more sources
d-Psicose, as important rare sugar and epimer of d-fructose on the C-3 position, displays unique health benefits and physiological functions in various fields. The production of d-psicose is currently obtained via enzymatic bioconversion, mostly with of d-tagatose 3-epimerase.
Jun Zhang +9 more
openaire +3 more sources