04529
Nitrilase
recombinant, expressed in E. coli, ≥2.0 U/mg
Synonym(s):
Nitrile aminohydrolase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in E. coli
form
crystals
powder
specific activity
≥2.0 U/mg
mol wt
41 kDa
storage temp.
2-8°C
General description
Nitrilase belongs to the C-N hydrolase superfamily. It possesses the catalytic triad motifs: glutamate, lysine, and cysteine and are distributed in fungi, plants, and animals.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.
Biochem/physiol Actions
Nitrilases catalyze the liberation of ammonia and the formation of carboxylic acid from the nitriles. The oligomeric structural organization of nitrilase is crucial for its functionality. It displays broad substrate specificity.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Unit Definition
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Zhi-Qiang Liu et al.
PloS one, 8(6), e67197-e67197 (2013-07-05)
In this study, several nitrilase genes from phylogenetically distinct organisms were expressed and purified in E. coli in order to study their ability to mediate the biotransformation of nitriles. We identified three nitrilases: Acidovorax facilis nitrilase (AcN); Alcaligenes fecalis nitrilase
Y V D Nageshwar et al.
Bioprocess and biosystems engineering, 34(5), 515-523 (2010-12-29)
Microbial nitrilases are biocatalysts of interest and the enzyme produced using various inducers exhibits altered substrate specificity, which is of great interest in bioprocess development. The aim of the present study is to investigate the nitrilase-producing Alcaligenes faecalis MTCC 10757
Pablo Soriano-Maldonado et al.
Applied and environmental microbiology, 77(16), 5761-5769 (2011-06-28)
Formamidases (EC 3.5.1.49) are poorly characterized proteins. In spite of this scarce knowledge, ammonia has been described as playing a central role in the pathogenesis of human pathogens such as Helicobacter pylori, for which formamidase has been shown to participate
Kwok-Yan Chan et al.
Structure (London, England : 1993), 19(9), 1211-1218 (2011-09-07)
Many large biological macromolecules have inherent structural symmetry, being composed of a few distinct subunits, repeated in a symmetric array. These complexes are often not amenable to traditional high-resolution structural determination methods, but can be imaged in functionally relevant states
Chunsheng Yang et al.
Applied biochemistry and biotechnology, 165(7-8), 1556-1567 (2011-09-23)
The characteristics of the new nitrilase-producing strain Rhodobacter sphaeroides LHS-305 were investigated. By investigating several parameters influencing nitrilase production, the specific cell activity was ultimately increased from 24.5 to 75.0 μmol g(-1) min(-1), and hereinto, the choice of inducer proved
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