Abstract: An amadoriase having a substitution or a deletion of one or more amino acid residues at positions corresponding to amino acids selected from the group consisting of three amino acid residues from the carboxyl terminal and amino acids at positions 151, 43, 53, 267, 350, 185, 196, 299 and 323 in the amino acid sequence of amadoriase derived from the Coniochaeta species indicated in SEQ ID NO: 1. The amadoriase having a heat resistance which is superior to that of a conventional amadoriase.

Abstract: A flavin-binding glucose dehydrogenase having high substrate specificity for D-glucose and decreased reactivity to D-xylose and/or maltose. More specifically, a flavin-binding glucose dehydrogenase having one or more amino acid substitutions at a position corresponding to position 78, position 79, position 81, position 121, position 122, position 123, position 569 and position 612 of Mucor-derived flavin-binding glucose dehydrogenase. The flavin-binding glucose dehydrogenase enables D-glucose to be measured accurately without being susceptible to the effects of the presence of D-xylose and/or maltose, even under conditions of mounting a large amount of an enzyme such as in glucose sensors.

Abstract: Disclosed are: a eukaryotic amadoriase which is prepared by introducing a mutation into DNA encoding a eukaryotic amadoriase derived from a microorganism belonging to the genus Coniochaeta or Eupenicillium so as to introduce a substitution into a specific amino acid residue in the eukaryotic amadoriase, thereby overcoming the defect associated with thermal stability; a gene or recombinant DNA for the eukaryotic amadoriase; and a process for production of a eukaryotic amadoriase having excellent thermal stability.

Abstract: 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.

Abstract: 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.

Abstract: This invention provides an amadoriase having high substrate specificity to fructosyl valyl histidine. Such amadoriase comprises substitution of one or more amino acid residues at positions corresponding to amino acids selected from the group consisting of position 98, position 259, position 154, position 125, position 261, position 263, position 106, position 103, position 355, position 96, position 66, position 67, position 70, position 100, position 110, position 113, position 114, and position 156 in the amadoriase derived from the genus Coniochaeta. This invention enables accurate measurement of ?-fructosyl valyl histidine derived from the ?-chain amino terminus in glycated hemoglobin in the presence of ?-fructosyl lysine.

Abstract: A flavin-binding glucose dehydrogenase with a high substrate specificity for D-glucose. The flavin-binding glucose dehydrogenase which is derived from a microorganism belonging to the genus Mucor. The flavin-binding glucose dehydrogenase has a low reactivity for maltose, D-galactose and D-xylose compared to its reactivity for D-glucose, and therefore is relatively unaffected by these saccharide compounds. The flavin-binding glucose dehydrogenase is also relatively unaffected by dissolved oxygen, and allows accurate measurement of glucose amounts even in the presence of saccharide compounds other than glucose in samples.

Abstract: A flavin-binding glucose dehydrogenase with a high substrate specificity for D-glucose. The flavin-binding glucose dehydrogenase which is derived from a microorganism belonging to the genus Mucor. The flavin-binding glucose dehydrogenase has a low reactivity for maltose, D-galactose and D-xylose compared to its reactivity for D-glucose, and therefore is relatively unaffected by these saccharide compounds. The flavin-binding glucose dehydrogenase is also relatively unaffected by dissolved oxygen, and allows accurate measurement of glucose amounts even in the presence of saccharide compounds other than glucose in samples.

Abstract: Disclosed are: a eukaryotic amadoriase which is prepared by introducing a mutation into DNA encoding a eukaryotic amadoriase derived from a microorganism belonging to the genus Coniochaeta or Eupenicillium so as to introduce a substitution into a specific amino acid residue in the eukaryotic amadoriase, thereby overcoming the defect associated with thermal stability; a gene or recombinant DNA for the eukaryotic amadoriase; and a process for production of a eukaryotic amadoriase having excellent thermal stability.

Abstract: Disclosed are: a eukaryotic amadoriase which is prepared by introducing a mutation into DNA encoding a eukaryotic amadoriase derived from a microorganism belonging to the genus Coniochaeta or Eupenicillium so as to introduce a substitution into a specific amino acid residue in the eukaryotic amadoriase, thereby overcoming the defect associated with thermal stability; a gene or recombinant DNA for the eukaryotic amadoriase; and a process for production of a eukaryotic amadoriase having excellent thermal stability.

Abstract: Disclosed are: a eukaryotic amadoriase which is prepared by introducing a mutation into DNA encoding a eukaryotic amadoriase derived from a microorganism belonging to the genus Coniochaeta or Eupenicillium so as to introduce a substitution into a specific amino acid residue in the eukaryotic amadoriase, thereby overcoming the defect associated with thermal stability; a gene or recombinant DNA for the eukaryotic amadoriase; and a process for production of a eukaryotic amadoriase having excellent thermal stability.