1.1.99.21: D-sorbitol dehydrogenase (acceptor)
This is an abbreviated version!
For detailed information about D-sorbitol dehydrogenase (acceptor), go to the full flat file.
Reaction
Synonyms
D-sorbitol dehydrogenase, FAD-SLDH, GoSLDH, mSLDH, PQQ-dependent D-sorbitol dehydrogenase, SDH, SLDH, sldhAB, sorbitol dehydrogenase
ECTree
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Engineering
Engineering on EC 1.1.99.21 - D-sorbitol dehydrogenase (acceptor)
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K294Q
additional information
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enzyme disruption mutant, oxidation activity against D-arabitol, D-sorbitol, D-mannitol, ribitol, meso-erythritol and glycerol are diminished
additional information
method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
additional information
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method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
additional information
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stability of GoSLDH significantly improves up to 13.6fold after cross-linking of immobilized enzyme on silica nanoparticles and retains 62.8% residual activity after 10 cycles of reuse. Covalent immobilization of GoSLDH onto SiO2 nanoparticles: the amino groups of amino acids such as lysine present on the surface of GoSLDH react with the glutaraldehyde activates SiO2 nanoparticles to form covalent bonds during immobilization at pH 7. The IY and IE of GoSLDH immobilized on different silica nanoparticles are in the ranges of 40.4-71.2% and 53.5-76.7%, respectively
additional information
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stability of GoSLDH significantly improves up to 13.6fold after cross-linking of immobilized enzyme on silica nanoparticles and retains 62.8% residual activity after 10 cycles of reuse. Covalent immobilization of GoSLDH onto SiO2 nanoparticles: the amino groups of amino acids such as lysine present on the surface of GoSLDH react with the glutaraldehyde activates SiO2 nanoparticles to form covalent bonds during immobilization at pH 7. The IY and IE of GoSLDH immobilized on different silica nanoparticles are in the ranges of 40.4-71.2% and 53.5-76.7%, respectively
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additional information
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method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
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