Glucose dehydrogenase
AssigneeUltizyme International Ltd.
InventorsKoji Sode, Satoshi Igarashi
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Abstract
Disclosed is a water-soluble PQQGDH wherein two subunits are linked together via a disulfide bond. The water-soluble PQQGDH of the invention exhibits improved thermal stability.
Claims8
An isolated mutant water-soluble pyrrolo-quinoline quinine glucose dehydrogenase (PQQGDH) protein, wherein two subunits of said mutant PQQGDH are linked together via one or more disulfide bonds, wherein said mutant PQQGDH is a mutant of a PQQGDH comprising the amino acid sequence of SEQ ID NO:1 and wherein said mutant PQQGDH only has one or more amino acid substitutions selected from the group consisting of:
- (1) serine at position 415 is substituted with a cysteine residue in SEQ ID NO:1,
- (2) tyrosine at position 414 is substituted with a cysteine residue in SEQ ID NO:1,
- (3) aspartate at position 340 is substituted with a cysteine residue in SEQ ID NO:1, and
- (4) tyrosine at position 418 is substituted with a cysteine residue in SEQ ID NO:1.
An isolated mutant PQQGDH protein, wherein two subunits of said mutant PQQGDH are linked together via one or more disulfide bonds, wherein said mutant PQQGDH is a mutant of a PQQGDH comprising the amino acid sequence of SEQ ID NO:1 and wherein said mutant PQQGDH only has the following amino acid substitutions:
- (1) serine at position 415 is substituted with a cysteine residue and aspartate at position 167 is substituted with a glutamate residue in SEQ ID NO:1,
- (2) serine at position 415 is substituted with a cysteine residue and serine at position 231 is substituted with a lysine residue in SEQ ID NO:1, or
- (3) serine at position 415 is substituted with a cysteine residue, aspartate at position 167 is substituted with a glutamate residue and serine at position 231 is substituted with a lysine residue in SEQ ID NO:1.
Dependencies are inferred from the claim text.