- Home
- IVD
- By Technology Types
- By Diseases Types
- By Product Types
- Research
- Resource
- Distributors
- Company
| Product Name | Lysozyme |
| Catalog No. | IVDRM-0180 |
| Description | Lysozyme, also known as muramidase, is an enzyme that breaks down bacterial cell walls and improves the efficiency of protein and nucleic acid extraction. It hydrolyzes the β-1,4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in the cell wall, converting insoluble peptidoglycan into soluble glycopeptides. The resulting loss of cell wall integrity causes the release of intracellular contents and bacterial lysis. Because Gram-positive bacteria have a high peptidoglycan content in their cell walls, they are highly sensitive to lysozyme, whereas Gram-negative bacteria are less sensitive. When EDTA is present in the system, it chelates Ca2+ in the bacterial outer membrane and increases the sensitivity of Gram-negative bacteria. In addition, when lysozyme is used to lyse E. coli, adding a nuclease such as DNase I markedly improves lysis efficiency. |
| Intended Use | Hydrolysis of bacterial cell walls to improve the efficiency of protein or nucleic acid extraction; lysis of Gram-positive bacteria (and Gram-negative bacteria in the presence of EDTA). |
| Principle / Technology | A muramidase that hydrolyzes the β-1,4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in bacterial cell wall peptidoglycan, breaking the cell wall and lysing the bacteria. |
| Sample Type | Bacterial cells, particularly Gram-positive bacteria; Gram-negative bacteria in the presence of EDTA. |
| Performance Range / Specifications | Activity: >20 KU/mg. Active over a broad pH range of 6.0-9.0. Free of RNase, DNase, and protease. |
| Specificity | Hydrolyzes β-1,4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in bacterial cell wall peptidoglycan. Gram-positive bacteria are highly sensitive; Gram-negative bacteria show weaker sensitivity, which can be enhanced by EDTA. |
| Reaction Conditions / Protocol | Reaction temperature: 37°C. Reaction time should be adjusted according to the bacterial species being lysed and is generally 30 minutes or longer. |
| Components / Formulation | Lysozyme purified from egg white; free of RNase, DNase, and protease. |
| Storage Conditions | Store at -20°C. |
| Shelf Life | 3 years when stored at -20°C. |
| Package Specifications | 5 g; 10 × 5 g |
| Quality Control | Free of RNase, DNase, and protease; activity >20 KU/mg. |
| Purity | Purified from egg white; free of RNase, DNase, and protease. |
| Activity / Unit Definition | Activity >20 KU/mg. |
| Source / Origin | Purified from chicken egg white |
| pH Range / Optimal pH | Active over a broad pH range of 6.0-9.0. |
| Shipping Conditions | Shipped with ice packs. |
| Expiration Date / Stability | Stable for 3 years at -20°C. |
| Compatibility | EDTA chelates Ca2+ in the bacterial outer membrane and increases the sensitivity of Gram-negative bacteria to lysozyme. Adding a nuclease such as DNase I markedly improves the efficiency of E. coli lysis. |
| Application Notes / Precautions | Although Gram-negative bacteria are generally easier to lyse, this enzyme is most commonly used for lysis of Gram-positive bacteria. Perform the reaction at 37°C; adjust the incubation time (generally at least 30 minutes) according to the bacterial species. For Gram-negative bacteria, adding EDTA improves lysis efficiency; for E. coli, adding DNase I further improves efficiency. |
For research use only, not for clinical use.
|
There is no product in your cart. |
Copyright © 2026 Alta DiagnoTech. All rights reserved.
