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61305 Sigma-Aldrich

Penicillinase from Bacillus cereus

lyophilized, powder, white, ~13 U/mg

Synonym: β-Lactamase I from Bacillus cereus, β-Lactamase II, Cephalosporinase, Penicillin amido-β-lactam hydrolase

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Properties

Related Categories 3.5.x.x Acting on C-N other than peptides, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Cell Biology,
Quality Level   100
form   powder
quality   lyophilized
mol wt   Mr ~30000
color   white
foreign activity   β-lactamase II ≤2%
storage temp.   −20°C

Description

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.

Unit Definition

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.

Other Notes

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

Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis (COA)

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Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Metabolomics, Molecular biology

Peer-Reviewed Papers
15

References

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