Nitrocefin is a cephalosporin with chromogenic properties and is routinely used to detect beta-lactamase enzymes produced by beta-lactam resistant bacteria. Nitrocefin is soluble in DMSO and is commonly used at a 1.0 mg/mL concentration.
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Zhangming et al. used nitrocefin from TOKU-E as a substrate to study TEM-1 ß-lactamase activity from E. coli. "Label-Free Measurements of Reaction Kinetics Using a Droplet-Based Optofluidic Device."
Liu et al. used nitrocefin from TOKU-E to study and develop a homogeneous biosensor. "Parts-per-Million of Polyethylene Glycol as a Non-Interfering Blocking Agent for Homogeneous Biosensor Development."
Dahlin et al. used nitrocefin from TOKU-E in a surrogate ß-lactamase-nitrocefin assay. "A Cell-Free Fluorometric High-Throughput Screen for Inhibitors of Rtt109-Catalyzed Histone Acetylation."
Ohlhoff et al. used nitrocefin from TOKU-E as a substrate to study the activity of EstG34 ß-lactamases. "An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range"
Huang et al. used nitrocefin from TOKU-E as a substrate to study the activity of VIM-2 Metallo-ß-lactamases (MBLs). "Inhibiting the VIM-2 Metallo-ß-Lactamase by Graphene Oxide and Carbon Nanotubes."
Eze E et al. used nitrocefin from TOKU-E to confirm beta-lactamase production in E. coli and Klebsiella species from Nigeria. Read more here: "Occurrence of Beta-Lactamases and the Antibiogram Pattern of Clinical Isolates of Escherichia coli and Klebsiella Species in Nsukka Metropolis."
Choi et al. measured enzymatic activity of engineered protein switches by exploiting nitrocefinhydrolysis. Read more here: "Electrochemical Activation of Engineered Protein Switches."
Pierre, et al. used nitrocefin from TOKU-E to measure the enzymatic acivity of various beta-lactamases. Read more here: "Molecular Determinants for Protein Stabilization by Insertional Fusion to a Thermophilic Host Protein."
Tullman and Nicholes, et al. used nitrocefin from TOKU-E to study and characterize enzymatic protein switches. Read more here: "Enzymatic protein switches built from paralogous input domains."
Mechanism of Action
Essentially all beta-lactamase enzymes hydrolyze the amide bond between the carbonyl carbon and the nitrogen in the beta-lactam ring of nitrocefin. Macroscopic detection of this process is made possible because a ultraviolet absorption shift from intact versus hydrolyzed nitrocefin occurs within the visible light spectrum (~380 nm to ~500 nm, or yellow to red).
Nitrocefin is used to detect beta-lactamase activity from suspected beta-lactam resistant bacteria (see protocol below).
O'Callaghan, Cynthia H. et. al. "Novel Method for Detection of B-Lactamases by Using a Chromogenic Cephalosporin Substrate." Antimicrobial Agents and
Chemotherapy 1.4 (1972): 283-88. Ncbi.gov Web. 10 Oct. 2012.
Parr, T. R., Jr. "Simple Screening Method for Beta-lactamase-positive and -negative Ampicillin-resistant Haemophilus Influenzae Isolates." Journal of Clinical
Microbiology 20.1 (1984): 131-32. Ncbi.gov. Web. 10 Oct. 2012.
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