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Literature summary for 1.4.1.2 extracted from

  • Sakamoto, H.; Komatsu, T.; Yamasaki, K.; Satomura, T.; Suye, S.
    Design of a multi-enzyme reaction on an electrode surface for an L-glutamate biofuel anode (2017), Biotechnol. Lett., 39, 235-240 .
    View publication on PubMed

Application

Application Comment Organism
energy production a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride Pyrobaculum islandicum

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Pyrobaculum islandicum

Organism

Organism UniProt Comment Textmining
Pyrobaculum islandicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme Pyrobaculum islandicum