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 RNA for the lysis of E. coli or eukaryotic cells.

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.

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)
pH optimum: 6.0-7.0
Inhibitors: imidazole, indole, N-acetyl glucosamine
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.