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analysis
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enzyme can be used for glucose determination
analysis
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usage for quantitative determination of glucose in clinical tests and in the food industry
analysis
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use of glucose dehydrogenase in enzyme cycling method for measurement of allantoin in human serum
analysis
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enzyme can be used for glucose determination
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biotechnology
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larger scale production of NAD(P)H in bioreactors by usage of the enzyme, a thermostable enzyme is advantageous
biotechnology
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azoreductase and glucose 1-dehydrogenase are coupled for both continuous generation of the cofactor NADH and azo dye removal. The results show that 85% maximum relative activity of azoreductase in an integrated enzyme system is obtained at the conditions: 1 U azoreductase: 10 U glucose 1-dehydrogenase, 250 mM glucose, 1.0 mM NAD+ and 150 microM methyl red
biotechnology
Escherichia coli transformants are prepared coexpressing the yeast reductase YOL151W and Bacillus GDH for the production of Ethyl (R, S)-4-chloro-3-hydroxybutanoate
biotechnology
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(±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate
biotechnology
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co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes
biotechnology
enzymatic reduction of the nicotinamide biomimetic cofactors 1-phenethyl-1,4-dihydropyridine-3-carboxamide using glucose dehydrogenase mutant I192T/V306I provides a regeneration system for artificial cofactors. The I192T/V306I mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor
biotechnology
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production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day
biotechnology
the robust stability of the enzyme makes it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature
biotechnology
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the robust stability of the enzyme makes it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature
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biotechnology
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larger scale production of NAD(P)H in bioreactors by usage of the enzyme, a thermostable enzyme is advantageous
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diagnostics
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enzyme can be used for glucose determination
diagnostics
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usage for quantitative determination of glucose in clinical tests and in the food industry
diagnostics
the enzyme can be a potential diagnostic reagent for blood glucose measurement
diagnostics
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the enzyme can be a potential diagnostic reagent for blood glucose measurement
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diagnostics
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enzyme can be used for glucose determination
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energy production
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NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
energy production
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NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
energy production
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NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
synthesis
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enzyme can be used for gluconic acid production in low water systems
synthesis
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usage as NADP+ cofactor regenerator for enzymatic synthesis of chiral compounds such as ethyl-(S)-4-chloro-3-hydroxybutanoate and ethyl 4-chloro-3-oxobutanoate
synthesis
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production of recombinant glucose 1-dehydrogenase in Escherichia coli, optimization of culture and induction conditions. Glucose 1-dehydrogenase is used to regenerate NADPH in vivo and in vitro and coupled with a NADPH-dependent bioreduction for efficient synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate from ethyl-4-chloro-3-oxobutanoate
synthesis
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(±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate
synthesis
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co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes
synthesis
glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application
synthesis
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production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day
synthesis
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production of recombinant glucose 1-dehydrogenase in Escherichia coli, optimization of culture and induction conditions. Glucose 1-dehydrogenase is used to regenerate NADPH in vivo and in vitro and coupled with a NADPH-dependent bioreduction for efficient synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate from ethyl-4-chloro-3-oxobutanoate
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synthesis
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glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application
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