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L4025

Sigma-Aldrich

Lyticase from Arthrobacter luteus

lyophilized powder, ≥200 units/mg solid

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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

≥200 units/mg solid

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 for resuspending cells to extract high-molecular weight DNA for polymerase chain reaction (PCR) fingerprint analyses.
Lyticase from Arthrobacter luteus has been used:
  • as a component in spheroplasting buffer to prepare yeast nuclear extracts
  • for digestion in sample preparation for β-glucan enzymatic assay using yeast
  • to lyse cells for RNA isolation

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.
Lyticase is a lysing enzyme that is used to extract DNA from yeast cells by inducing partial spheroplast formation. Spheroplasts are subsequently lysed to release DNA. Lyticase is preferred to digest cell walls of yeast, which are difficult to disrupt because the cell walls may form capsules or resistant spores. Lyticase contains β-(1→;3)-glucan laminaripentaohydrolase along with β-(1→3)-glucanase, protease, and mannanase activities. It is useful with yeast cells such as e.g. 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.

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)

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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Lisbeth Rosager Poulsen et al.
The Plant cell, 20(3), 658-676 (2008-03-18)
Vesicle budding in eukaryotes depends on the activity of lipid translocases (P(4)-ATPases) that have been implicated in generating lipid asymmetry between the two leaflets of the membrane and in inducing membrane curvature. We show that Aminophospholipid ATPase3 (ALA3), a member
Naturally occurring novel promoters around pyruvate branch-point for recombinant protein production in Pichia pastoris (Komagataella phaffii): pyruvate decarboxylase-and pyruvate kinase-promoters
Massahi A and Calik P
Biochemical Engineering Journal, 138, 111-120 (2018)
A protein transformation protocol for introducing yeast prion particles into yeast
Tanaka M, et al.
Methods in Enzymology, 470, 681-693 (2010)
M Groenewald et al.
Persoonia, 21, 17-27 (2008-12-01)
The type species of the genus Debaryomyces, Debaryomyces hansenii, is a highly heterogeneous species. It has been isolated from a large diversity of natural sources including fruit, air, water, soil, but most frequently from processed food products. The species delineation
Tim K Footz et al.
Human molecular genetics, 18(7), 1276-1287 (2009-01-20)
Primary open-angle glaucoma (POAG) is a leading cause of blindness worldwide. POAG is associated with a characteristic progression of changes to ocular morphology and degeneration at the optic nerve head with the loss of visual fields. Physical mapping efforts identified

Protocols

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

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