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L2524

Sigma-Aldrich

Lyticase from Arthrobacter luteus

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

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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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)
Bing Zhai et al.
Nature medicine, 26(1), 59-64 (2020-01-08)
The intestinal microbiota is a complex community of bacteria, archaea, viruses, protists and fungi1,2. Although the composition of bacterial constituents has been linked to immune homeostasis and infectious susceptibility3-7, the role of non-bacterial constituents and cross-kingdom microbial interactions in these
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
Irina Leonardi et al.
Cell host & microbe, 27(5), 823-829 (2020-04-17)
Fecal microbiota transplantation (FMT) targeting gut microbiota has recently been successfully applied to ulcerative colitis. However, only a subset of patients responds to FMT, and there is a pressing need for biomarkers of responsiveness. Fungi (the mycobiota) represent a highly
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

Protocols

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

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