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Lysozyme, 10 g

≥45 000 FIP U/mg, lyophilized
Examples of effect: Have an allergenic effect, carcinogenic, mutagenic, toxic to reproduction and cause developmental toxicity (reprotoxic) or damage to organs Safety: You must be well-informed before starting work with these substances; wear protective clothing and gloves, eye protection and mask or breathing protection.
i may cause allergy or asthma symptoms or breathing difficulties if inhaled
P260 P342+P311
i do not breathe dust, if experiencing respiratory symptoms: Call a POISON CENTER/doctor
Pack Qty.
Molar mass (M) ~14000 g/mol
Storage temp. -20 °C
Transport temp. ambient temp.
CAS No. [12650-88-3]
EG-Nr. 235-747-3

From chicken egg white, free from albumin.
Stock solution: 10-50 mg/ml in 10 mM Tris (pH 8,0), prepare directly before use

Salt and albumin free lyophilised powder. Quality product for molecular biology. Ideal for lysis of bacteria for preparing DNA.
Product details
Type analysis
€115.60 /Pack Qty.

€90.10/Pack Qty.  Campaign price!

excl. VAT. | 10 g per Pack Qty.

Art. No. 8259.2

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Product details

Salt and albumin free lyophilised powder. Quality product for molecular biology. Ideal for lysis of bacteria for preparing DNA.

Lysozyme preferentially hydrolyses the β-1,4-glycosidic bond between N-acetylmuraminic acid and N-acetylglucosamine. Muramic acid and acetylglucosamine are components of the proteoglycan cell wall of many microorganisms. The enzyme is mostly derived from chicken egg white and may efficiently be used for lysis of Gram+ bacteria. In genetic engineering, it is very often used during isolation of plasmid DNA or cellular RNAfor the lysis of E. coli or eukaryotic cells.

Directions for use

pH optimum: 6.0-7.0
Inhibitors: imidazole, indole, N-acetyl glucosamine
Stock solution: 10-50 mg/ml in 10 mM Tris (pH 8,0), prepare directly before use
Working solution: 5-10 mg/ml (bacteria), 1-2 mg/ml (eukaryotic cells)
Buffer: salt solution without detegents (0.1 M potassium phosphate buffer, 50 mM Tris buffer, 1x PBS, 1x TBS or similar)
Temperature optimum: 37 °C
Stability: The lyophilisate is stable at +4 °C and -20 °C for several years. The stability of the solution at pH 4-5 is several weeks at +4 °C and several days at room temperature.
Isoelectric point: approx. 11
Lysozyme solution should be frozen only once.

Lysozyme ≥45 000 FIP U/mg, lyophilized
Unit definition

1 FIP-Unit equals the amount of enzyme which reduces the absorbance by 0.001 per min. at 450 nm, 25 °C, pH 7.00 using a suspension of FIP Micrococcus luteus as substrate (acc. to Pharmaceutical Enzymes 1997). 1 FIP-Unit resembles approximately 1 Shugar-Unit.

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Order No. Pack Qty. Pack. Price Quantity
8259.1 1 g glass €23.35
8259.2 10 g glass €90.10
8259.3 25 g glass €267.45
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General information

Enzyme: a neoclassical, Greek artificial word ενζυμου, énzymon, derived from εν-, en- (in-) and ζυμη, zýmé (yeast, sourdough, archaic)
Ferments: comes from the Latin fermentum (ferments, sourdough)

There are six classes in which all enzymes are classified according to the particular reaction they catalyse:

Oxidoreductases (catalyse redox reactions)

Transferases (transfer functional groups among substrates)

Hydrolases (cleave bonds via addition of water)

Lyases/Synthases (cleave or synthesise complex products out of basic substrates without cleavage of ATP)

Isomerases (transform chemical isomers)

Ligases/Synthetases (cleave or synthesise complex products out of basic substrates via cleavage of ATP)

Certificates of Analysis

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The following analysis certificates have been found:

Type analysis

Appearancewhite powder  
Activity≥45000 FIP U/mg  
Water content≤8,0 %  
Ash content≤2,0 %  

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