This product is stored and shipped at ambient temperature. In the powder form, this material is quite robust and does not require controlled temperature storage. This item is stable at room temperature until the lot specific expiration date.
L6876
Lysozyme from chicken egg white
powder or granules, ≥39,000 units/mg protein
Synonym(s):
Mucopeptide N-acetylmuramoylhydrolase, Muramidase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
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Product Name
Lysozyme from chicken egg white, powder or granules, ≥39,000 units/mg protein
biological source
chicken egg white
form
powder or granules
specific activity
≥39,000 units/mg protein
mol wt
single-chain 14.3 kDa
technique(s)
cell based assay: suitable
suitability
suitable for cell lysis
UniProt accession no.
application(s)
cell analysis
storage temp.
room temp
Quality Level
Gene Information
chicken ... LYZ(396218)
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Related Categories
1 of 4
This Item | 62970 | L3790 | L4919 |
|---|---|---|---|
| specific activity ≥39,000 units/mg protein | specific activity ~100000 U/mg | specific activity - | specific activity ≥40,000 units/mg protein |
| technique(s) cell based assay: suitable | technique(s) cell based assay: suitable | technique(s) cell based assay: suitable | technique(s) cell based assay: suitable |
| biological source chicken egg white | biological source chicken egg white | biological source chicken egg white | biological source chicken egg white |
| Gene Information chicken ... LYZ(396218) | Gene Information chicken ... LYZ(396218) | Gene Information chicken ... LYZ(396218) | Gene Information - |
| form powder or granules | form powder | form liquid | form lyophilized powder |
| application(s) cell analysis | application(s) cell analysis | application(s) cell analysis | application(s) cell analysis |
Application
Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.
Biochem/physiol Actions
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).
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.
Features and Benefits
Lysozyme from chicken egg white is a versatile enzyme with unique properties that make it effective for various applications, including bacterial cell wall breakdown, genomic DNA extraction, and external standard for mass analysis. It is reliable, active over a broad pH range, and available in various packaging sizes.
Other Notes
One unit will lyse 0.6 μg of Micrococcus lysodeikticus per minute by turbidimetric detection at 600 nm when suspended in buffer at pH 6.2 at 25 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
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Protocols
该酶速率测定可用于溶菌酶产物。它不适用于在测定在琼脂糖上的重组型或不溶性溶菌酶。
This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.
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We typically store our lyophilized lysozyme at -20C, but one recent order (shipped at room temperature) was left at room temperature, sealed, for several weeks. Will it still be active?
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I have ordered this product and stored in -70 degree C. But there is no dilution preparation method available here. Can you please tell me hot to prepare that.
1 answer-
This product may be prepared in 10 mM Tris-HCl, pH 8.0 at 10 mg/mL. The material is also soluble in water at 10 mg/mL. Aqueous solutions are stable for at least one month when stored at 2-8 °C. Please see the link below to review additional information available in the product datasheet:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/938/215/l6876dat-ms.pdfHelpful?
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What's the best buffer and pH for the preparation of lysozyme stock solution, and can I incubate it at room temperature for 1 day?
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This product can be resuspended in 350 µL of STET buffer (10 mM Tris-HCl, pH 8.0, with 0.1 M NaCl,
1 mM EDTA, and 5% [w/v] TRITON® X-100). 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).During this assay, the end-user should Incubate E. coli (strain ATCC 37017) bearing the pBR322 plasmid overnight in Terrific Broth (Cat. No. T0918) with 25 µg/mL tetracycline (Cat. No. T3383) and 25 µg/mL ampicillin (Cat. No. A9518). The
optimal pH for E. coli cell lysis is 8.0 ± 0.1.16For more information please read through the product data sheet: https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/938/215/l6876dat-ms.pdf
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What is the amino acid sequence of Product L6876, Lysozyme from chicken egg white?
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Lysozyme is a single chain polypeptide of 129 amino acids. The amino acid sequence of chicken egg white Lysozyme is described in the Journal of Biological Chemistry, 238, 2698-2707 (1963).
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What is the Department of Transportation shipping information for this product?
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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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Can Product L6876, Lysozyme from chicken egg white, be inactivated by heat?
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Solutions of Lysozyme may be inactivated by boiling for 40 seconds at 100°C at an alkaline pH.
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How can Product L6876, Lysozyme from chicken egg white, be reconstituted and can stock solutions be prepared?
1 answer-
For the lysis procedure, use a freshly prepared solution of 500,000 units/ml in 10 mM Tris-HCl, pH 8.0. The product is also soluble in water (10 mg/ml) yielding a clear to slightly hazy colorless solution. Aqueous solutions should be stable for at least one month when stored between 2-8 °C.
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Under what conditions can Product L6876, Lysozyme from chicken egg white, be used to lyse E. coli?
1 answer-
The following procedure is for the lysis of E. coli. It may be used as a guideline for other species.1. Incubate E. coli (strain ATCC 37017) bearing the pBR322 plasmid overnight in Terrific Broth (Product No. T 0918) with 25 μg/ml tetracycline (Product No T 3383) and 25 μg/ml ampicillin (Product No. A 9518).2. Centrifuge 1-2 ml samples of the overnight culture.3. Resuspend the pellets in 350 μl of STET buffer (10 mM Tris-HCl, pH 8.0, with 0.1 M NaCl, 1 mM EDTA, and 5% [w/v] TRITON® X-100).4. Add 25 μl of a freshly prepared lysozyme solution (500,000 units/ml in 10 mM Tris-HCl, pH 8.0).5. Mix by vortexing for 3 seconds.6. Incubate the lysis mixture for 30 minutes at 37 °C7. After incubation, place the tube containing the lysis mixture in a boiling water bath for exactly 40 seconds.8. Centrifuge the lysis mixture at 14,000 x g.9. Remove the pellet (cell debris) from the tube using a sterile toothpick.10. Plasmid DNA from the supernatant may then be purified and analyzed.
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