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04529

Sigma-Aldrich

Nitrilase

recombinant, expressed in E. coli, ≥2.0 U/mg

Synonyme(s) :

Nitrile aminohydrolase

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10 MG
160,00 $
50 MG
555,00 $

160,00 $


En stockDétails



Sélectionner une taille de conditionnement

Changer de vue
10 MG
160,00 $
50 MG
555,00 $

About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

160,00 $


En stockDétails


Produit recombinant

expressed in E. coli

Niveau de qualité

Forme

crystals
powder

Activité spécifique

≥2.0 U/mg

Poids mol.

41 kDa

Température de stockage

2-8°C

Description générale

Nitrilase belongs to the C-N hydrolase superfamily.[1] It possesses the catalytic triad motifs: glutamate, lysine, and cysteine and are distributed in fungi, plants, and animals.[2]The isoelectric point (pI) of this protein is 8.1. Native polyacrylamide gel electrophoresis (PAGE).

Application

Nitrilase may be used for immobilization on acryloyl crosslinked cellulose dialdehyde (ACCD) for catalytic activity studies.[3]

Actions biochimiques/physiologiques

Nitrilases catalyze the liberation of ammonia and the formation of carboxylic acid from the nitriles.[4] The oligomeric structural organization of nitrilase is crucial for its functionality.[1] It displays broad substrate specificity.[1]

Conditionnement

Bottomless glass bottle. Contents are inside inserted fused cone.

Définition de l'unité

1 U corresponds to the amount of enzyme which liberates 1 μmol ammonia per minute at pH 7.2 and 25°C with the conversion of acrylonitrile to acrylic acid

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Ahmed Kamal et al.
Journal of microbiology and biotechnology, 21(1), 37-42 (2011-02-09)
A new versatile acrylonitrile-bioconverting strain isolated from a petroleum-contaminated sludge sample and identified as Rhodococcus ruber AKSH-84 was used for optimization of medium and biotransformation conditions for nitrilase activity to produce acrylic acid. A simple and rapid HPLC protocol was
Jeremy D Woodward et al.
Communications biology, 1, 186-186 (2018-11-13)
Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important enzymes are often specific for certain substrates, but directed attempts at modifying their substrate specificities
Alena Petříčková et al.
Applied microbiology and biotechnology, 93(4), 1553-1561 (2011-09-06)
Nitrilases from Aspergillus niger CBS 513.88, A. niger K10, Gibberella moniliformis, Neurospora crassa OR74A, and Penicillium marneffei ATCC 18224 were expressed in Escherichia coli BL21-Gold (DE3) after IPTG induction. N. crassa nitrilase exhibited the highest yield of 69,000 U L(-1)
Shivani Jamwal et al.
International journal of biological macromolecules, 131, 117-126 (2019-03-08)
Immobilization of enzymes to improve their catalytic properties is an attractive protocol which makes them suitable candidates to meet various industrial demands. Present study describes the synthesis of new acryloyl crosslinked cellulose dialdehyde (ACCD) for nitrilase immobilization. Nitrilase was immobilized
Joanna E Raczynska et al.
Journal of structural biology, 173(2), 294-302 (2010-11-26)
The nitrilase superfamily is a large and diverse superfamily of enzymes that catalyse the cleavage of various types of carbon-nitrogen bonds using a Cys-Glu-Lys catalytic triad. Thermoactive nitrilase from Pyrococcus abyssi (PaNit) hydrolyses small aliphatic nitriles like fumaro- and malononitryl.

Questions

1–3 of 3 Questions  
  1. what is the bacteria or organism whose genome sequence have been expressed in E.Coli for nitrilase procurement? I need the name of the organism for research purpose

    1 answer
    1. This enzyme is a recombinant protein produced in e. coli. The biological source and sequence of the protein is considered proprietary and may not be shared.

      Helpful?

  2. Can we get the source of the bacteria or organism whose genome sequence is being used for recombinant expressing in E.Coli for procuring nitrilase. Used for research purspose by a student

    1 answer
    1. Unfortunately, the source and sequence is considered proprietary.

      Helpful?

  3. Is the nitrilase been synthesized through DNA recombinant technology or is there any other source organism from which the nitrilase has been procured?

    1 answer
    1. Yes, this product is a recombinant protein expressed in E. coli.

      Helpful?

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