http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2016116470-A

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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N27-416
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filingDate 2014-12-19-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1ea96dd759937eca3c950f2d1f0a62ea
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_6ebfed21608e0a902d8b3118d385f569
publicationDate 2016-06-30-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-2016116470-A
titleOfInvention Mutant pyrroloquinoline quinone-dependent glucose dehydrogenase, isolated nucleic acid molecule encoding mutant pyrroloquinoline quinone-dependent glucose dehydrogenase, enzyme electrode and enzyme electrode immobilizing mutant pyrroloquinoline quinone-dependent glucose dehydrogenase And biosensor equipped with
abstract Disclosed is a mutant pyrroloquinoline quinone-dependent glucose dehydrogenase, an isolated nucleic acid molecule, an enzyme electrode that can stably exhibit its catalytic activity as an electrode catalyst for an enzyme electrode and can achieve a higher catalyst current density than the wild type. , Providing bio batteries and bio sensors. (A) an amino acid sequence in which amino acid residues at positions corresponding to the 26th valine and the 334th serine of a wild-type pyrroloquinoline quinone-dependent glucose dehydrogenase are substituted with cysteine, (b) An amino acid sequence in which one to several amino acids other than the 26th and 334th amino acids are substituted, deleted, added, or inserted, or (c) 80% or more of the amino acid sequence other than the above positions, Mutant pyrroloquinoline having an identical amino acid sequence and improved catalytic current density obtained when adsorbed and immobilized on an electrode substrate to form an enzyme electrode compared to wild-type pyrroloquinoline quinone-dependent glucose dehydrogenase Quinone-dependent glucose dehydrogenase. [Selection figure] None
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