Production, purification, characterization, and safety evaluation of constructed recombinant D-psicose 3-epimerase [PDF]
Microbial Cell FactoriesBackground D-psicose 3-epimerase (DPEase) is a potential catalytic enzyme for D-psicose production. D-psicose, also known as D-allulose, is a low-calorie sweetener that has gained considerable attention as a healthy alternative sweetener due to its ...
Nisit Watthanasakphuban +5 more
doaj +5 more sources
In Silico Analysis and Development of the Secretory Expression of D-Psicose-3-Epimerase in Escherichia coli [PDF]
MicroorganismsD-psicose-3-epimerase (DPEase), a key enzyme for D-psicose production, has been successfully expressed in Escherichia coli with high yield.
Nisit Watthanasakphuban +4 more
doaj +5 more sources
A Novel D-Psicose 3-Epimerase from Halophilic, Anaerobic Iocasia fonsfrigidae and Its Application in Coconut Water. [PDF]
Int J Mol Sci, 2023 D-Psicose is a rare, low-calorie sugar that is found in limited quantities in national products. Recently, D-psicose has gained considerable attention due to its potential applications in the food, nutraceutical, and pharmaceutical industries. In this study, a novel D-psicose 3-epimerase (a group of ketose 3-epimerase) from an extremely halophilic ...
Wulansari S +9 more
europepmc +4 more sources
Enhanced Thermostability of D-Psicose 3-Epimerase from Clostridium bolteae through Rational Design and Engineering of New Disulfide Bridges. [PDF]
Int J Mol Sci, 2021 D-psicose 3-epimerase (DPEase) catalyzes the isomerization of D-fructose to D-psicose (aka D-allulose, a low-calorie sweetener), but its industrial application has been restricted by the poor thermostability of the naturally available enzymes. Computational rational design of disulfide bridges was used to select potential sites in the protein structure
Zhao J +5 more
europepmc +5 more sources
A Possible Mechanism of Graphene Oxide to Enhance Thermostability of D-Psicose 3-Epimerase Revealed by Molecular Dynamics Simulations. [PDF]
Int J Mol Sci, 2021 Thermal stability is a limiting factor for effective application of D-psicose 3-epimerase (DPEase) enzyme. Recently, it was reported that the thermal stability of DPEase was improved by immobilizing enzymes on graphene oxide (GO) nanoparticles. However, the detailed mechanism is not known.
Li C +5 more
europepmc +5 more sources
Crystal structures of d-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars [PDF]
Protein and Cell, 2012 D-psicose 3-epimerase (DPEase) is demonstrated to be useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature. Clostridium cellulolyticum H10 has recently been identified as a DPEase that can epimerize D-fructose to yield D-psicose with a much higher conversion rate when compared with the conventionally ...
Hsiu-Chien Chan +2 more
exaly +5 more sources
Microbial Cell Factories, 2017 Background d-Tagatose 3-epimerase epimerizes d-fructose to yield d-psicose, which is a rare sugar that exists in small quantities in nature and is difficult to synthesize chemically.
Zhengliang Qi +7 more
doaj +2 more sources
Preparation of a Flower-Like Immobilized D-Psicose 3-Epimerase with Enhanced Catalytic Performance [PDF]
Catalysts, 2018 In this present study, we proposed a smart biomineralization method for creating hybrid organic–inorganic nanoflowers using a Co2+-dependent enzyme (D-psicose 3-epimerase; DPEase) as the organic component and cobalt phosphate as the inorganic component. The prepared nanoflowers have many separated petals that have a nanometer size.
Lu Zheng +6 more
openaire +2 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 +3 more sources
Construction of hyperthermostable d-allulose 3-epimerase from Arthrobacter globiformis M30 using the sequence information from Arthrobacter psychrolactophilus. [PDF]
FEBS Open Biod‐Allulose can be produced from d‐fructose by d‐allulose 3‐epimerase. Based on sequence homology information, we successfully engineered thermostable mutants with the protein engineering method. By integrating positive mutations, we constructed an enzyme that exhibits hyperthermostability without a loss in the activity.
Shimada K +3 more
europepmc +2 more sources