Lysosyme is an enzyme found in egg white that breaks down the cell walls in bacteria enhancing the efficiency of DNA and protein extraction.

Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.

Suitable for the purification of both DNA and protein from bacteria.

Lysozyme hydrolyzes β(1→4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. Gram-positive cells are quite susceptible to this hydrolysis as their cell walls have a high proportion of peptidoglycan. Gram-negative bacteria are less susceptible due to the presence of an outer membrane and a lower proportion of peptidoglycan. However, these cells may be hydrolyzed in the presence of EDTA that chelates metal ions in the outer bacterial membrane.

The enzyme is active over a broad pH range (6.0 to 9.0). At pH 6.2, maximal activity is observed over a wider range of ionic strengths (0.02 to 0.100 M) than at pH 9.2 (0.01 to 0.06 M).

Lysozyme hydrolyzes β(1→4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. Gram-positive cells are quite susceptible to this hydrolysis as their cell walls have a high proportion of peptidoglycan.

Tested for suitability with CelLytic^™ B in protein extraction from bacteria.

One unit will lyse 0.4 μg of Micrococcus lysodeikticus per minute by turbidimetric detection at 600 nm when suspended in buffer at pH 8.0 at 37 °C.

Ready to use solution:10 mg/mL lysozyme in 25 mM sodium acetate pH 4.5 with 50% glycerol.

Solution in 50% glycerol, 25 mM Sodium Acetate

CelLytic is a trademark of Sigma-Aldrich Co. LLC