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L2524

Sigma-Aldrich

Lyticase from Arthrobacter luteus

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

Synonym(s):

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

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Arthrobacter luteus)

Quality Level

form

lyophilized powder

specific activity

≥2,000 units/mg protein

composition

Protein, ≥20% biuret

technique(s)

cell based assay: suitable

suitability

suitable for cell lysis

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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Application

Lyticase from Arthrobacter luteus has been used to lyse the fungal cell wall for DNA isolation.
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.
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-(1→3)-glucan laminaripentaohydrolase along with β-(1→3)-glucanase, protease, and mannanase activities. Lyticase is used for yeast cells like Candida, Debaryomyces, Saccharomyces, Saccharomycopsis, Saccharomycodes, Eremothecium, and Schwanniomyces species.
Lyticase hydrolyzes poly-β(1→3)-glucose such as yeast cell wall glucan.

Unit Definition

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.

Physical form

Partially purified, lyophilized powder containing potassium phosphate buffer salts and stabilizers

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A protein transformation protocol for introducing yeast prion particles into yeast
Tanaka M, et al.
Methods in Enzymology, 470, 681-693 (2010)
Hagen Frickmann et al.
BMC microbiology, 19(1), 75-75 (2019-04-10)
The potential of next-generation sequencing (NGS) for hypothesis-free pathogen diagnosis from (poly-)microbially contaminated, formalin-fixed, paraffin embedded tissue samples from patients with invasive fungal infections and amebiasis was investigated. Samples from patients with chromoblastomycosis (n = 3), coccidioidomycosis (n = 2), histoplasmosis (n = 4), histoplasmosis or
Daniel Zenklusen et al.
Nature structural & molecular biology, 15(12), 1263-1271 (2008-11-18)
Proper execution of transcriptional programs is a key requirement of gene expression regulation, demanding accurate control of timing and amplitude. How precisely the transcription machinery fulfills this task is not known. Using an in situ hybridization approach that detects single
Anne Schwabe et al.
Nature communications, 5, 4798-4798 (2014-09-03)
Individual cells respond very differently to changes in environmental conditions. Stochasticity causes cells to respond at different times, magnitudes or both. Here we disentangle and quantify these two sources of heterogeneity. We track the adaptation dynamics of single Saccharomyces cerevisiae
Joana Segura et al.
Nature communications, 9(1), 3989-3989 (2018-09-30)
The interplay between chromatin structure and DNA topology is a fundamental, yet elusive, regulator of genome activities. A paradigmatic case is the "linking number paradox" of nucleosomal DNA, which refers to the incongruence between the near two left-handed superhelical turns

Protocols

This procedure may be used for the determination of Lyticase activity using Baker’s yeast as the substrate.

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