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Literature summary for 3.5.1.108 extracted from

  • Ko, Y.; Chen, C.; Shieh, C.; Liu, Y.
    Simultaneous purification and immobilization of D-hydantoinase on the immobilized metal affinity membrane via coordination bonds (2012), Biochem. Eng. J., 61, 20-27.
No PubMed abstract available

Application

Application Comment Organism
synthesis construction of immobilized metal affinity membrane via coupling of epichlorohydrin, iminodiacetic acid, and nickel ion on a regenerated cellulose membrane. The D-hydantoin-hydrolyzing enzyme harboring a poly-His tagged residue is immobilized on the prepared membrane. By employing a membrane with nickel ion of 155.5 micromol/disc immersed in 0.1 M Tris-HCl buffer pH 8, with 0.8 M sodium chloride, an enzyme activity of 4.2 U/disc is obtained. The immobilized DHTase membrane can achieve a larger pH and thermaltolerance range than the free enzyme. 99% of enzyme activity can be retained after 15 repeated uses Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Synonyms

Synonyms Comment Organism
DHTase
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Escherichia coli