Description
A highly thermostable Lysozyme developed from a unique thermophilic bacteriophage. The enzyme breaks down the cell wall of specific bacteria and is especially active against cells of thermophilic bacterial strains of the genus Thermus including T. thermophilus and T. aquaticus.
The enzyme is available for purchase in 0.1 mg size.
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Synonyms: muramidase, N-acetylmuramide glycanhydrolase, glycoside hydrolase
Enzyme classification: EC 3.5.1.28
Source: Thermophilic bacteriophage Ph2119
Description: ThermoPhage™ Lysozyme originates from a thermophilic bacteriophage known to infect thermophilic bacteria of the genus Thermus. The enzyme promotes lysis of certain bacterial species but has activity spectrum very different from the commonly used Hen egg white lysozyme (HEWL). The enzyme has high activity against bacteria of the genus Thermus including Thermusthermophilus and Thermus aquaticus as shown in the Table:
Bacterial species | Ts Lysozyme | HEWL |
Thermus thermophilus HB8 | 100 | 43 |
Thermus aquaticus | 100 | 41 |
Deinococcus radiodurans | 25 | 21 |
Echerichia coli | 34 | 100 |
Salmonella panama | 10 | 35 |
Pseudomonas fluorescence | 13 | 40 |
Serratia marcescens | 0 | 35 |
Enterococcus faecalis | 4 | 0 |
Bacillus subtilis | 2 | 0 |
Bacillus cereus | 15 | 75 |
Staphylococcus aureus | 0 | 0 |
Staphylococcus intermedius | 0 | 5 |
Staphylococcus epidermis | 0 | 0 |
Sarcina lutea | 2 | 48 |
Streptococcus pyogenes | 0 | 11 |
Lactococcus lactis | 0 | 11 |
Thermostability: Relative activity of ThermoPhage™ Lysozyme at different temperature vs. the activity of Hen Egg White Lysozyme
Applications: The enzyme is suitable for efficient lysis of Thermus bacteria such as for increasing total DNA or plasmid DNA isolation (See figure below). Reactions and enzyme dilutions can be done in a 10 mM K/PO4 buffer at pH 8.0. The use of EDTA is not recommended.
References:
Plotka M, Stefanska A, Kaczorowska A-K, Morzywolek A, Fridjonsson OF, Dunin-Horkawicz S, Hreggvidsson GO, Kristjansson JK, Dabrowski S, Bujnicki JM and Kaczorowski T. 2014 Purification and characterization of a novel highly thermostable lysozyme fromThermus scotoductus MAT2119 bacteriophage Ph2119 that shows amino-acid sequence similarity to eukaryotic peptidoglycan recognition proteins (PGRPs). Appl. Environ. Microbiol.