Results 81 to 90 of about 277 (107)
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Preparation of d-psicose from d-fructose by immobilized d-tagatose 3-epimerase
Journal of Bioscience 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
exaly +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
Kei Takeshita
exaly +5 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
Kei Takeshita
exaly +5 more sources
Biotechnology Letters, 2009
D-Psicose 3-epimerase from Agrobacterium tumefacience catalyzes the conversion of D: -fructose to D-psicose. According to mutational analysis, the ring at position 112, the negative charge at position 156, and the positive charge at position 215 were essential components for enzyme activity and for binding fructose and psicose. The surface contact area
Hye-Jung, Kim +5 more
openaire +2 more sources
D-Psicose 3-epimerase from Agrobacterium tumefacience catalyzes the conversion of D: -fructose to D-psicose. According to mutational analysis, the ring at position 112, the negative charge at position 156, and the positive charge at position 215 were essential components for enzyme activity and for binding fructose and psicose. The surface contact area
Hye-Jung, Kim +5 more
openaire +2 more sources
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,
Wanmeng Mu, Bo Jiang, Long-Tao Zhang
exaly +3 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,
Wanmeng Mu, Bo Jiang, Long-Tao Zhang
exaly +3 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
Enzyme and Microbial Technology, 2017
D-Psicose (D-ribo-2-hexulose or D-allulose), an epimer of D-fructose is considered as a rare low-calorie sugar displaying important physiological functions. Enzymatic production using ketose 3-epimerases is the feasible process for the production of D-Psicose.
Samir R, Dedania +4 more
openaire +2 more sources
D-Psicose (D-ribo-2-hexulose or D-allulose), an epimer of D-fructose is considered as a rare low-calorie sugar displaying important physiological functions. Enzymatic production using ketose 3-epimerases is the feasible process for the production of D-Psicose.
Samir R, Dedania +4 more
openaire +2 more sources
Bioprocess and Biosystems Engineering, 2019
D-Allose is a rare sugar, can be used as an ingredient in a range of foods and dietary supplements, has alimentary activities, especially excellent anti-cancer effects and used in assisting cancer chemotherapy and radiotherapy, etc. To develop a simple and low-cost process for D-allose production, a one-pot enzymatic process using the substrate of D ...
Can, Li +6 more
openaire +2 more sources
D-Allose is a rare sugar, can be used as an ingredient in a range of foods and dietary supplements, has alimentary activities, especially excellent anti-cancer effects and used in assisting cancer chemotherapy and radiotherapy, etc. To develop a simple and low-cost process for D-allose production, a one-pot enzymatic process using the substrate of D ...
Can, Li +6 more
openaire +2 more sources
Biotechnology Letters, 2009
Using site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of D: -psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D: -fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the K (m ...
Hye-Jung, Kim +5 more
openaire +2 more sources
Using site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of D: -psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D: -fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the K (m ...
Hye-Jung, Kim +5 more
openaire +2 more sources
Bioprocess and Biosystems Engineering, 2013
The aim of this study is to achieve high-level extracellular production of D-Psicose-3-epimerase (DPE) with recombinant Escherichia coli. High-level production of DPE is one of the key factors in D-Psicose production. In the present study, the gene AAL45544.1 from Agrobacterium tumefaciens str.
Lei, Gu +5 more
openaire +2 more sources
The aim of this study is to achieve high-level extracellular production of D-Psicose-3-epimerase (DPE) with recombinant Escherichia coli. High-level production of DPE is one of the key factors in D-Psicose production. In the present study, the gene AAL45544.1 from Agrobacterium tumefaciens str.
Lei, Gu +5 more
openaire +2 more sources