Advanced Search



Lyticase from Arthrobacter luteus

SIGMA/L2524 - lyophilized powder, ≥2,000 units/mg protein, Protein ≥20 % by biuret

Synonym: (1,3)-β-D-Glucan endohydrolase; 1,3-β-Glucan glucohydrolase; Bacterial lyticase; Lysing enzyme

CAS Number: 37340-57-1
MDL Number: MFCD00131560
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-L2524-10KU 10000 units
$101.00
1/EA
Add To Favorites
45-L2524-25KU 25000 units
$203.00
1/EA
Add To Favorites
45-L2524-50KU 50000 units
$373.00
1/EA
Add To Favorites
45-L2524-200KU 200000 units
$1180.00
1/EA
Add To Favorites
Lyticase specificity: Yeast β-glucan is a polymer of β-(1-3)-D-glycopyranosyl units with branching at β-(1-6)-D-glycopyranosyl units.
Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. DNA can be extracted from yeast by using lysing enzymes. Lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. Lyticase contains β-(1→3)-glucan laminaripentaohydrolase with additional β-(1→3)-glucanase, protease, and mannanase activities.

 

application(s) diagnostic assay manufacturing
biological source bacterial (Arthrobacter luteus)
composition Protein, ≥20% biuret
form lyophilized powder
Quality Level 300 
specific activity ≥2,000 units/mg protein
storage temp. −20°C
suitability suitable for cell lysis
technique(s) cell based assay: suitable
Application: Lyticase from Arthrobacter luteus has been used to lyse the fungal cell wall for DNA isolation.
Application: Lyticase from Arthrobacter luteus has been used:
• for spheroplasting the cells
• as a component of digestion solution to incubate yeast cells for digestion of the cell wall
• in the enzymatic hydrolysis of the mycelium precipitate to prepare protoplasts

Biochem/physiol Actions: Lyticase enzyme is frequently used in fungal research, particularly for species identification using polymerase chain reaction (PCR)-based techniques. It can break down β (1→3) and β (1→4) bonds between glucose units. Lysozyme serves as an indicator of macrophage-mediated host response, correlates with white cell death, and exhibits a high turnover rate. Elevated levels of serum lysozyme have been observed in various chronic inflammatory conditions, inflammatory bowel diseases, hematological disorders, and renal disorders. The c-type lysozyme from hen egg white is commonly used as a model for studying protein structure and function. Muramidase primarily exhibits bactericidal activity against Gram-positive bacteria. The method described in the bulletin for determining molecular masses using gel filtration chromatography is a modified version of existing published techniques. The protein standards included in this kit may be compatible with other chromatographic systems like high-performance liquid chromatography (HPLC). However, certain buffer systems may affect the elution volumes of albumin and carbonic anhydrase. The proteins in this kit have a molecular mass range spanning from 29 kDa to 699 kDa.
Biochem/physiol Actions: Lyticase hydrolyzes poly-β(1→3)-glucose such as yeast cell wall glucan.
Biochem/physiol Actions: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. DNA can be extracted from yeast by using lysing enzymes such as lyticase to induce partial spheroplast formation. Spheroplasts are subsequently lysed to release DNA. Lyticase is preferred to digest the cell walls of yeast and generate spheroplasts from fungi for transformation. It contains β-(13)-glucan laminaripentaohydrolase along with β-(13)-glucanase, protease, and mannanase activities. Lyticase is used for yeast cells like Candida, Debaryomyces, Saccharomyces, Saccharomycopsis, Saccharomycodes, Eremothecium, and Schwanniomyces species.
Other Notes: For R&D use only. Not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.
Other Notes: One unit will produce a ΔA800 of 0.001 per min at pH 7.5 at 25 °C, using a suspension of yeast as substrate in a 3 mL reaction mixture.
Other Notes: View more information on enzymes for complex carbohydrate analysis  at www.sigma-aldrich.com/enzymeexplorer 
Packaging: 10000, 25000 units in glass bottle
Packaging: 50000, 200000 units in poly bottle
Physical form: Partially purified, lyophilized powder containing potassium phosphate buffer salts and stabilizers
Symbol GHS08  GHS08
Signal word Danger
Hazard statements H334
Precautionary statements P261 - P284 - P304 + P340 + P312 - P501
Hazard Codes Xn
Risk Statements 42
Safety Statements 22-45
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
activity specific activity: ≥2,000 units/mg protein
Storage Temp. −20°C
UNSPSC 12352204

The following items have been added to your cart:

Choose a favorite list for this item:

Catalog Number Description Price
$

Returns/Order support

Please fill out the form below if you want to request order support from Krackeler Scientific.


Quick Order

* Required


New Tariffs & Effects on Pricing

Tariff note: As we navigate the current environment of tariff surcharges and mid-year manufacturer price increases, we want to keep you informed. While we have avoided making specific decisions thus far, we anticipate that we will be forced to implement a cost adjustment policy to offset the fees we have already been absorbing. We are committed to transparency and moderation in this process.

800-334-7725
office@krackeler.com


Play Video

To Request a Quote

  1. Search or Browse for items and add to them to your Shopping Cart.
  2. Click the "Request Quote" button at the bottom of the Shopping Cart page.
  3. Fill out required fields.
  4. Optionally you can convert to standard checkout mode by choosing a payment type.
  5. Click "Request Quote" at the bottom of the page.

You will be contacted with a quote.

To Order From a Quote

  1. Register and login to the website.
  2. Receive a quote from your sales representative or customer service.
  3. Have your copy of the quote in hand.
  4. Visit our quote module to search for your quote.
Back to Top