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Lysozyme is an enzyme used to break down bacterial cell walls to improve protein or nucleic acid extraction efficiency. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall. This hydrolysis in turn compromises the integrity of bacterial cell walls causing lysis of the bacteria. Molecular weight 14.4 kDa.


•Removal of the cell wall of Gram-positive bacteria

Biochem/physiol Functions

Catalyzes the hydrolysis of 1,4-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycans and between N-acetyl-D-glucosamine residues in chitodextrins

Definition of Activity Unit

1 unit is that amount of enzyme needed to reduce the absorption value of the enzyme solution by 0.001 per minute. The reaction substrate is a 0.2 mg/ml micro-wall lysozyme suspension prepared by phosphoric acid buffer solution (0.05 M, PH 6.1).

This lysozyme product has the specific activity of >20,000 U/mg. It functions as an antimicrobial agent by cleaving the peptidoglycan component of bacterial cell walls