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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
~13 U/mg
Biological source:
Bacillus sp. (Bacillus cereus)
biological source
Bacillus sp. (Bacillus cereus)
form
powder
quality
lyophilized
specific activity
~13 U/mg
mol wt
Mr ~30000
technique(s)
activity assay: suitable
color
white
suitability
suitable for component for culture media
application(s)
diagnostic assay manufacturing
foreign activity
β-lactamase II ≤2%
storage temp.
−20°C
Quality Level
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General description
Penicillinase from Bacillus cereus is both an extracellular and cell-bound enzyme. It has a single polypeptide chain and has a molecular weight of 31 kDa. It lacks cysteine in the protein sequence.
Application
Penicillinase from Bacillus cereus may be used in the preparation of biosensor for amperometric detection of hydrolysis of penicillin.
Used in the production of penicillin.
Biochem/physiol Actions
Penicillinase specifically catalyzes the hydrolysis of β-lactam ring of penicillin.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
One unit will hydrolyze 1.0 μmole of indicated substrate per min at pH 7.0 at 25 °C. Sold as benzylpenicillin units. This International Unit (using benzylpenicillin as substrate) is approximately equal to 600 Levy or 75 Pollock units.
Used to destroy β-lactam antibiotics in body fluids or culture media. For the determination of penicillin; In the coupled enzyme assay for isopenicillin N synthetase; ELISA of estradiol; Penicillinase optodes.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Regulatory Information
常规特殊物品
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W. Hobel et al.
Biosensors And Bioelectronics, 7, 549-549 (1992)
J E Baldwin et al.
Analytical biochemistry, 145(1), 183-187 (1985-02-15)
The development of a coupled enzyme assay for the determination of isopenicillin N synthetase activity in purified extracts from Cephalosporium acremonium was described. Isopenicillin N formed from its precursor, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV), by the synthetase was hydrolyzed by beta-lactamase I to
T. Scheper et al.
Analytica Chimica Acta, 163, 111-111 (1984)
Flow injection determination of penicillins using immobilized penicillinase in a single bead string reactor.
R Gnanasekaran et al.
Analytical chemistry, 57(6), 1005-1009 (1985-05-01)
Properties of penicillinase from Bacillus cereus 569
Imsande J, et al.
The Journal of Biological Chemistry, 245(9), 2205-2212 (1970)
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