Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.5.9 extracted from

  • Yamazaki, T.; Tsugawa, W.; Sode, K.
    Increased thermal stability of glucose dehydrogenase by cross-linking chemical modification (1999), Biotechnol. Lett., 21, 199-202.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Bacteria
-
SM4, moderate thermophilic
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + 2,6-dichlorophenolindophenol
-
Bacteria D-gluconic acid + reduced 2,6-dichlorophenolindophenol
-
?

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
45
-
and a second lower optimum at 75┬░C, native enzyme Bacteria
65
-
glucose dehydrogenase cross-linked with glutaraldehyde Bacteria

Temperature Range [┬░C]

Temperature Minimum [┬░C] Temperature Maximum [┬░C] Comment Organism
30 60 30┬░C: about 45% of maximal activity, 60┬░C: about 25% of maximal activity, native enzyme Bacteria
40 80 40┬░C: about 45% of maximal activity, 80┬░C: about 45% of maximal activity, glucose dehydrogenase cross-linked with glutaraldehyde Bacteria

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
65
-
half-life of native enzyme: 2.5 min, half life of enzyme cross-linked to glutaraldehyde: 72 min Bacteria