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Literature summary for 4.2.1.84 extracted from

  • van Pelt, S.; Quignard, S.; Kubac, D.; Sorokin, D.Y.; van Rantwijk, F.; Sheldon, R.A.
    Nitrile hydratase CLEAs: The immobilization and stabilization of an industrially important enzyme (2008), Green Chem., 10, 395-400.
No PubMed abstract available
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General Stability

General Stability Organism
immobilization and stabilization of a nitrile hydratase in the form of a cross-linked enzyme aggregate using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde, method development and evaluation, overview. The stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-
Rhodococcus sp. J1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acrylonitrile + H2O
-
 Rhodococcus sp. acrylamide
-
 ?
acrylonitrile + H2O
-
 Rhodococcus sp. J1 acrylamide
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
21
-
 assay at Rhodococcus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 50 20 min, the stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells Rhodococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Rhodococcus sp.

pH Range

pH Minimum pH Maximum Comment Organism
4 12 pH profile of soluble and immobilized enzymes, overview Rhodococcus sp.