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Literature summary 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

General Stability

EC Number General Stability Organism
4.2.1.84 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

EC Number Organism UniProt Comment Textmining
4.2.1.84 Rhodococcus sp.
-
-
-
4.2.1.84 Rhodococcus sp. J1
-
-
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.84 21
-
 assay at Rhodococcus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.84 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.84 8
-
 assay at Rhodococcus sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.84 4 12 pH profile of soluble and immobilized enzymes, overview Rhodococcus sp.