Storage
Store at -20°C

Grade
Lysozyme is a single chain polypeptide of 129 amino acids cross-linked with four disulfide bridges. It hydrolyzes β(1-4) linkages between N-acetylmuraminic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. Lysozyme is used for bacterial cells lysis by hydrolyzing the peptidoglycan in cell walls. Gram-positive bacteria cells which have a high proportion of peptidoglycan are quite susceptible to the hydrolysis while gram-negative bacteria cells which have lower proportion of peptidoglycan as well as have the presence of outer membrane are less susceptible to the hydrolysis. With the presence of EDTA that chelates metal ions in the outer bacterial membrane, these cells may be hydrolyzed more easily. 
The lysozyme is supplied in lyophilized powder form. It is being purified from chicken egg white and being crystallized and dialyzed into lyophilized form. The highly purified enzyme preparation has been used in mass spectrometry as a protein mass calibration standard and in structural studies of protein. It is suitable to be used in plasmid DNA purification as a lysing agent in a boiling lysing technique.

Isoelectric point (pI): 11.35

Extinction co-efficients: E^1% (281.5nm): 26.4 in 0.1M potassium chloride 
E^mM (280nM): 36

Lysozyme is active between pH 6.0 – pH 9.0. At pH 6.2, maximal activity is observed over a wider range of ionic strengths (0.02-0.10M) than pH 9.2 (0.01-0.06M).

Description
Molecular Biology Grade

Specification

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Lysozyme, Egg White

Publication
This Product Has Been Used In: 
Mohd Shaufi, M.A., et al. (2015) Deciphering Chicken Gut Microbial Dynamics Based on High-Throughput 16S rRNA Metagenomics Analyses. Gut Pathogens. 20(2)7(4), p. 1-12.