67138
β-(1→3)-D-Glucanase from Helix pomatia
≥0.2 U/mg
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-927-3
MDL number:
Specific activity:
≥0.2 U/mg
Biological source:
Helix pomatia
Product Name
β-(1→3)-D-Glucanase from Helix pomatia, ≥0.2 U/mg
biological source
Helix pomatia
form
powder
specific activity
≥0.2 U/mg
storage temp.
−20°C
Quality Level
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Related Categories
Application
β-(1→3)-D-Glucanase from Helix pomatia is used to digest β -1,3-glucan, which is a major component of cell walls. β-(1→3)-D-Glucanase from Helix pomatia has been used fto digest the cell walls of C. albicans .
Biochem/physiol Actions
Deletion of the C.albicans histidine kinase gene (CHK1) improves recognition by phagocytes through an increased exposure of cell wall b-1,3-glucans, which are readily digested by β-(1→3)-D-Glucanases .
Other Notes
One unit corresponds to the amount of enzyme which liberates 1 μmol of glucose from laminarin (Cat. No. 61340) per minute at pH 5.0 and 37 °C
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
动植物源性产品
低风险生物材料
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Linglin Wan et al.
Planta, 233(2), 309-323 (2010-11-04)
Plant β-1,3-glucanases are involved in plant defense and development. In rice (Oryza sativa), 14 genes encoding putative β-1,3-glucanases have been isolated and sequenced. However, only limited information is available on the function of these β-1,3-glucanase genes. In this study, we
María de Medina-Redondo et al.
PloS one, 5(11), e14046-e14046 (2010-12-03)
The formation of the cell wall in Schizosaccharomyces pombe requires the coordinated activity of enzymes involved in the biosynthesis and modification of β-glucans. The β(1,3)-glucan synthase complex synthesizes linear β(1,3)-glucans, which remain unorganized until they are cross-linked to other β(1,3)-glucans
Alexander M Zakharenko et al.
Carbohydrate research, 346(2), 243-252 (2010-12-15)
The retaining endo-1,3-β-d-glucanase (EC 3.2.1.39) was isolated from the crystalline styles of the commercially available Vietnamese edible mussel Perna viridis. It catalyzes hydrolysis of β-1,3-bonds in glucans and enables to catalyze a transglycosylation reaction. Resources of mass-spectrometry for analysis of
Junio Cota et al.
Biochemical and biophysical research communications, 406(4), 590-594 (2011-03-01)
1,3-β-Glucan depolymerizing enzymes have considerable biotechnological applications including biofuel production, feedstock-chemicals and pharmaceuticals. Here we describe a comprehensive functional characterization and low-resolution structure of a hyperthermophilic laminarinase from Thermotoga petrophila (TpLam). We determine TpLam enzymatic mode of operation, which specifically
N P Sachivkina et al.
Bulletin of experimental biology and medicine, 149(6), 727-730 (2010-12-18)
Lyticase (a bacterial enzyme) was tested as a new antimycotic drug. Of all objects studied, Cellulomonas cellulans AC-870 strain proved to be most productive for this enzyme. A technology for lyticase isolation and purification was proposed. An experimental model of
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