M4782
Mutanolysin from Streptomyces globisporus ATCC 21553
0.2 μm filtered, lyophilized powder, ≥4000 units/mg protein (biuret)
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About This Item
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Quality Level
sterility
0.2 μm filtered
form
lyophilized powder
specific activity
≥4000 units/mg protein (biuret)
mol wt
23 kDa
shipped in
wet ice
storage temp.
−20°C
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General description
Mutanolysin from Streptomyces globisporus consists of two main lytic enzymes and may be a useful agent for dental caries control.
Application
Provides gentle cell lysis for the isolation of easily degradable biomolecules and RNA from bacteria. It has been used in the formation of spheroplasts for isolation of DNA.
Biochem/physiol Actions
Mutanolysin is an N-acetylmuramidase. Like lysozyme, it is a muralytic enzyme that cleaves the β-N-acetylmuramyl-(1→4)-N-acetylglucosamine linkage of the bacterial cell wall polymer peptidoglycan-polysaccharide. Its carboxy terminal moieties are involved in the recognition and binding of unique cell wall polymers. Mutanolysin lyses Listeria and other Gram-positive bacteria such as Lactobacillus and Lactococcus.
Unit Definition
One unit will produce a ΔA600 of 0.01 per minute at pH 6.0 at 37 °C in a 1 mL volume using a suspension of Streptococcus faecalis cell wall as substrate.
Physical form
Lyophilized powder containing Ficoll and sodium succinate buffer salts
Preparation Note
Prepared from M 9901
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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John M Pfeffer et al.
Journal of bacteriology, 188(3), 902-908 (2006-01-24)
The O acetylation of peptidoglycan occurs specifically at the C-6 hydroxyl group of muramoyl residues. Using a combination of high-performance liquid chromatography-based organic acid analysis and carbohydrate analysis by high-pH anion-exchange chromatography, we determined that strains of Entercoccus durans, E.
Carli B Jones et al.
Frontiers in genetics, 13, 799615-799615 (2022-04-19)
Short read 16 S rRNA amplicon sequencing is a common technique used in microbiome research. However, inaccuracies in estimated bacterial community composition can occur due to amplification bias of the targeted hypervariable region. A potential solution is to sequence and assess
A rapid and efficient method of lysis of Listeria and other gram-positive bacteria using mutanolysin
Fliss, I., et al.
Biotechniques, 11, 456-457 (1991)
Tom Vanhoutte et al.
FEMS microbiology ecology, 48(3), 437-446 (2004-06-01)
According to the current insights, the predominant bacterial community in human feces is considered to be stable and unique for each individual over a prolonged period of time. In this study, the temporal stability of both the predominant population and
K Yokogawa et al.
Antimicrobial agents and chemotherapy, 6(2), 156-165 (1974-08-01)
Mutanolysin partially purified from the culture filtrate of Streptomyces globisporus 1829 consists of two main lytic enzymes with an isoelectric point near pH 8.5 and 10, respectively, and proteolytic enzyme is associated with the latter lytic enzyme. Mutanolysin exhibited maximal
Protocols
This procedure may be used for Mutanolysin products.
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