Abstract: A novel diaphorase; a method for producing the diaphorase; and use of the diaphorase are provided. The diaphorase comprises any one of the following polypeptides (a) to (c): (a) a polypeptide having the amino acid sequence of SEQ ID NO: 1, (b) a polypeptide having the amino acid sequence of SEQ ID NO: 1 in which one or several amino acid residues are substituted, deleted, inserted, added, and/or inverted, and having diaphorase activity, and (c) a polypeptide having an amino acid sequence with 80% or more identity to the amino acid sequence of SEQ ID NO: 1, and having diaphorase activity.

Abstract: [Object] To provide: a novel diaphorase; a method for producing the diaphorase; and use of the diaphorase. [Solution] A diaphorase comprising any one of the following polypeptides (a) to (c): (a) a polypeptide having the amino acid sequence of SEQ ID NO: 1, (b) a polypeptide having the amino acid sequence of SEQ ID NO: 1 in which one or several amino acid residues are substituted, deleted, inserted, added, and/or inverted, and having diaphorase activity, and (c) a polypeptide having an amino acid sequence with 80% or more identity to the amino acid sequence of SEQ ID NO: 1, and having diaphorase activity.

Abstract: PQQGDH having an improved substrate specificity or having an improved specific activity in an assay system using ferricyanide ion as a mediator is provided. Modified PQQGDH having the enhanced substrate specificity by introducing an amino acid mutation in a particular region of PQQGDH, and a method of enhancing the specific activity compared with a wild type in the assay system using the ferricyanide ion as the mediator by deleting, substituting, or adding one or more amino acids in an amino acid sequence of the wild type pyrroloquinoline quinone dependent glucose dehydrogenase.

Abstract: The present invention relates to modified pyrroloquinoline quinone dependent glucose dehydrogenase (PQQGDH) having lower activity with respect to disaccharides and/or greater stability than wild-type PQQGDH.

Abstract: PQQGDH having an improved substrate specificity or having an improved specific activity in an assay system using ferricyanide ion as a mediator is provided. Modified PQQGDH having the enhanced substrate specificity by introducing an amino acid mutation in a particular region of PQQGDH, and a method of enhancing the specific activity compared with a wild type in the assay system using the ferricyanide ion as the mediator by deleting, substituting, or adding one or more amino acids in an amino acid sequence of the wild type pyrroloquinoline quinone dependent glucose dehydrogenase.

Abstract: The present invention provides a stable lyophilized PQQ-dependent glucose dehydrogenase composition comprising a PQQ-dependent glucose dehydrogenase together with (i) at least one compound selected from the group consisting of aspartic acid, glutamic acid, ?-ketoglutaric acid, malic acid, ?-ketogluconic acid, ?-cyclodextrin and their salts and (ii) an albumin.

Abstract: The present invention provides a high performance glucose sensor which can demonstrate high stability against preservation and produces only a low blank value. The glucose sensor comprises an electrically insulating base plate, an electrode system formed on the base plate, and a reaction layer which is formed in contact with or in the vicinity of the electrode system and contains at least a glucose dehydrogenase whose coenzyme is pyrrolo-quinoline quinone, the reaction layer further containing an additive such as phthalic acid.

Abstract: The present invention relates to modified pyrroloquinoline quinone dependent glucose dehydrogenase (PQQGDH) having lower activity with respect to disaccharides and/or greater stability than wild-type PQQGDH.

Abstract: The invention relates to a plasmid characterized in that the plasmid comprises a DNA fragment containing a gene coding for an enzyme taking PQQ as the prosthetic group as cloned in a broad-host-range vector defected of conjugative transfer function beforehand and that the plasmid is capable of being expressed in bacteria of the genus Pseudomonas.

Abstract: The present invention provides a stable lyophilized PQQ-dependent glucose dehydrogenase composition comprising a PQQ-dependent glucose dehydrogenase together with (i) at least one compound selected from the group consisting of aspartic acid, glutamic acid, &agr;-ketoglutaric acid, malic acid, &agr;-ketogluconic acid, &agr;-cyclodextrin and their salts and (ii) an albumin.

Abstract: A novel protein having a heat-resistant malate dehydrogenase activity, a DNA fragment having a gene encoding said protein, a recombinant vector having said DNA fragment, a transformant transformed with said vector, a method for producing the protein having heat-resistant malate dehydrogenase activity by the use of said transformant, a reagent for GOT determination, comprising the above-mentioned novel protein having a heat-resistant malate dehydrogenase activity and a method for determining GOT activity, which comprises the use of said reagent. According to the present invention, a protein having a heat-resistant malate dehydrogenase activity and having higher purity and superior heat stability can be obtained. In addition, a reagent for GOT determination which is superior in long-term storage can be prepared by the use of the protein having a heat-resistant malate dehydrogenase activity.

Abstract: A novel protein having a heat-resistant malate dehydrogenase activity, a DNA fragment having a gene encoding said protein, a recombinant vector having said DNA fragment, a transformant transformed with said vector, a method for producing the protein having heat-resistant malate dehydrogenase activity by the use of said transformant, a reagent for GOT determination, comprising the above-mentioned novel protein having a heat-resistant malate dehydrogenase activity and a method for determining GOT activity, which comprises the use of said reagent. According to the present invention, a protein having a heat-resistant malate dehydrogenase activity and having higher purity and superior heat stability can be obtained. In addition, a reagent for GOT determination which is superior in long-term storage can be prepared by the use of the protein having a heat-resistant malate dehydrogenase activity.