310 results about "Glucose dehydrogenase" patented technology

The present invention provides a high-performance glucose sensor having excellent storage stability and an improved response characteristic. This sensor comprises: an electrically insulating base plate; an electrode system including at least a working electrode and a counter electrode formed on the base plate; and a reaction layer containing at least pyrrolo-quinoline quinone dependent glucose dehydrogenase, formed in contact with or in the vicinity of the electrode system, and the reaction layer contains at least one kind of additive selected from the group consisting of gluconic acid and salts thereof.

The present invention is directed to glucose dehydrogenase (GDH) polypeptides that have enhanced GDH activity and/or thermostability relative to the backbone wild-type glucose dehydrogenase polypeptide. In addition, the present invention is directed to a polynucleotide that encodes for the GDH polypeptides of the present invention, to nucleic acid sequences comprising the polynucleotides, to expression vectors comprising the polynucleotides operatively linked to a promoter, to host cells transformed to express the GDH polypeptides, and to a method for producing the GDH polypeptides of the present invention.

A flavin-bound glucose dehydrogenase (FAD-GDH) with high substrate specificity for D-glucose. A gene encoding a mutant FAD-GDH with its N-terminal region, containing an amino acid sequence corresponding to MKITAAIITVATAFASFASA that exists in the N-terminal region, deleted from the amino acid sequence of a wild-type FAD-GDH derived from Mucor is introduced into E. coli to obtain an E. coli transformant. Subsequently, this E. coli transformant is cultured to obtain an FAD-GDH with a specific N-terminal region deleted. The transformant allows the production of a large amount of GDH in a short time as compared with the original microorganism. An FAD-GDH that is less susceptible to the effects of dissolved oxygen and allows accurate measurement of glucose even in the presence of sugar compounds other than glucose in a sample.

A heat-resistant flavin-bound glucose dehydrogenase having a high substrate specificity for D-glucose, an method for producing the same, and a transformant used for the same. A flavin-bound glucose dehydrogenase gene encoding a flavin-bound glucose dehydrogenase derived from Mucor is introduced into yeast, Zygosaccharomyces, to obtain a transformant. Subsequently, the yeast transformant is cultured to obtain a flavin-bound glucose dehydrogenase from the culture. The heat-resistant flavin-bound glucose dehydrogenase is less susceptible to the effects of dissolved oxygen and allows accurate measurement of glucose even in the presence of sugar compounds other than glucose in a sample.

The invention provides a blood sugar biosensor of carbon nanometer tube, it includes floor, three electrode system, insulation, forming the reaction lumen body around three electrode system, setting the conversion zone in the reaction lumen body, laying over the cover plate on the reaction lumen body, the conversion zone includes, enzyme and electron transport agent, the enzyme is the glc dh pyrrole and quinone for coenzyme. The transducer's corresponding sensitivity improves evidently, it has not infection for measuring the dextrose deepness in the blood with the oxygen pressure, thickness in the measuring site and oxygen content of blood sample. The invention has the excellence of easy manufacture artwork, low cost, suited to volume-produce and the low sample quantity etc.

Object: An object of the present invention is to provide a more practically advantageous enzyme usable as a reagent for measuring blood glucose than the known enzymes used as blood glucose sensors.

Method for Achieving the Object: A modified flavin adenine dinucleotide dependent glucose dehydrogenase (FADGDH) with more improved heat stability than FADGDH derived from wild-type FADGDH, the modified FADGDH being derived from preferably a eukaryote, more preferably a filamentous fungus, and furthermore preferably an Aspergillus fungus, and, for example, those having a primary structure with at least one amino acid substituted, deleted, inserted or added to FADGDH having an amino acid sequence represented by SEQ ID Nos. 2 or 46 in the sequence table.

[Object] To provide an FAD-conjugated glucose dehydrogenase having a higher specificity for glucose.

[Means for Resolution] A modified glucose dehydrogenase (GLD) which includes a substitution of at least one amino acid residue selected from the group consisting of amino acid residues at positions 37, 69, 72, 73, 76, 78, 102, 217, 228, 240, 356, 407, 424, 437, 527, and 530 in an amino acid sequence of a wild-type FAD-conjugated glucose dehydrogenase (GLD) represented by SEQ ID NO: 1, and has a decreased ratio of activity for xylose/activity for glucose as compared with the wild-type GLD; a polynucleotide encoding the modified GLD; a recombinant vector containing the polynucleotide; a transformed cell produced by using the recombinant vector; etc.

A chemistry matrix for use in determining the concentration of an analyte in a biological fluid includes a glucose dehydrogenase, nicotinamide adenine dinucleotide, an alkylphenazine quaternary salt, and/or a nitrosoaniline. The chemistry matrix is used with an electrochemical biosensor to determine the concentration of an analyte after a reaction occurs within the biosensor, at which time an analysis is completed to determine the concentration. A method of determining the concentration of an analyte using the chemistry matrix of glucose dehydrogenase, nicotinamide adenine dinucleotide, an alkylphenazine quaternary salt, and/or a nitrosoaniline is another aspect that is described. The method also further features test times of five seconds or less. Methods utilizing the new chemistry matrix can readily determine an analyte such as blood glucose at concentrations of from about 20-600 mg/dL at a pH of from about 6.5 to about 8.5.

A preparation method and an application of a paper-based self-power supply biosensor are provided. The invention discloses a three-dimensional hollow channel microfluidic paper chip adapter sensor having the advantages of simple operation, low cost and self-power supply and successfully used for on-site detection. The sensor successfully introduces a biofuel cell into a three-dimensional hollow channel microfluidic paper chip, utilizes a catalytic effect of a biological fuel cell cathode and anode on a substrate to voluntarily generate an electrical signal, and gets rid of limits on external power supply equipment. The biofuel cell anode prepared by growing gold improves the conductivity of the electrodes, and glucose dehydrogenase is immobilized on the anode; the biofuel cell cathode adopts a carbon nanotube-platinum nano composite material for catalyzing oxygen to reduce, and glucose is used as a fuel; mutual recognition between an adapter and heavy metal ions is generated on the gold-anode; the current intensity is detected by an electrochemical workstation, and thus the heavy metal ions in water are detected.

The invention relates to a biological preparation method of an intermediate of atazanavir. (S)-tertiary butyl (4-chloro-3-carbonyl-1-benzene butyl-2-yl) carbamic acid ester is taken as a substrate. The preparation method comprises the following steps of adding the substrate, a cosolvent and glucose into a reactor, stirring uniformly, weighing ketoreductase powder, glucose dehydrogenase and cofactor, dissolving in a water phase buffered solution with pH of 8-9, adding the obtained mixed solution into the reactor, stirring, controlling the temperature to be at 32DEG C-34 DEG C, and beginning reacting, wherein at the beginning of the reaction, the mass volume ratio concentration of the substrate is 0.05-0.2g/ml, and the mass ratio of the added ketoreductase to cofactor to glucose to the substrate is (0.02-0.03):(0.001-0.005):(0.8-1.2):1. Compared with the prior art, the biological preparation method realizes more environment-friendly and mild biological conversion process with high reaction efficiency, and has important application value.

The invention discloses an alcohol dehydrogenase, a gene thereof, a recombinant expression vector and a recombinant expression transformant respectively containing the gene, a recombinase of the alcohol dehydrogenase, and an application of the alcohol dehydrogenase in asymmetric reduction synthesis of chiral diaryl secondary alcohol as a catalyst, and belongs to the technical field of bioengineering. The alcohol dehydrogenase is from Kluyveromyces sp. CCTCCM2011385, has a carbonyl group reduction function, and also has a hydroxy group oxidation function. Extra addition of glucose dehydrogenase and other enzymes used for cofactor circulation is not needed when the alcohol dehydrogenase is used in the reduction of diaryl ketone into the chiral diaryl secondary alcohol as a biocatalyst, and the alcohol dehydrogenase has the advantages of high catalysis efficiency, mild reaction conditions, easy product recovery and low cost, so the alcohol dehydrogenase has very good application and exploitation prospect in the production of antihistamine medicines.

The present invention provides a method for highly expressing a recombinant FAD-GDH protein derived from filamentous fungi, protein obtained by the method, and a regent for measuring glucose using the protein. According to the invention, the FAD-GDH can be highly expressed by altering DNA sequence coding for a signal peptide of FAD-GDH gene isolated from Aspergillus oryzae. FAD-GDH can be stably produced by adjusting pH of 7.1 to 7.3 during culture production.

The present invention provides members that produce on a large scale a coenzyme-linked glucose dehydrogenase which has excellent substrate-recognizing ability toward glucose while providing low action on maltose. The present invention relates to a polynucleotide encoding a soluble coenzyme-linked glucose dehydrogenase that catalyzes the oxidation of glucose in the presence of an electron acceptor and has an activity toward maltose of 5% or lower; a polypeptide encoded by the nucleotide sequence of the polynucleotide; a recombinant vector carrying the polynucleotide; a transformed cell produced using the recombinant vector; a method for producing a polypeptide comprising culturing the transformed cell and collecting from the cultivated products a polypeptide that links to FAD to exert the glucose dehydration activity; a method for determination of glucose using the polypeptide; a reagent composition for determination of glucose; and a biosensor.

The present invention provides glucose dehydrogenase which is excellent in heat resistance and substrate specificity and is not affected by dissolved oxygen. Specifically, the present invention relates to glucose dehydrogenase characterized by being derived from an eukaryotic organism and keeping 90% or more activity after being treated with heat at 55° C. for 15 minutes in a liquid form compared with the activity before being treated.