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Literature summary for 4.2.1.53 extracted from

  • Todea, A.; Hiseni, A.; Otten, L.; Arends, I.; Peter, F.; Boeriu, C.
    Increase of stability of oleate hydratase by appropriate immobilization technique and conditions (2015), J. Mol. Catal. B, 119, 40-47 .
No PubMed abstract available
Search for more literature for 4.2.1.53

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Elizabethkingia meningoseptica

General Stability

General Stability Organism
immobilization results in a radical improvement of operational stability of the enzyme, as the covalently bound enzyme preserves 75% of the initial activity after five reuses Elizabethkingia meningoseptica

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica C7DLJ6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Elizabethkingia meningoseptica

Storage Stability

Storage Stability Organism
4°C, 7 days, the native enzyme loses 60% of its activity Elizabethkingia meningoseptica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oleate + H2O
-
 Elizabethkingia meningoseptica (R)-10-hydroxystearate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Elizabethkingia meningoseptica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 the immobilized enzyme (covalent immobilization of the enzyme using glutaraldehyde as cross-linking agent with chitosan-magnetic composite as carrier) preserves 40% of the initial activity, while the native enzyme is completely inactivated Elizabethkingia meningoseptica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Elizabethkingia meningoseptica