67138
β-(1→3)-D-Glucanase from Helix pomatia
≥0.2 U/mg
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About This Item
Productos recomendados
origen biológico
Helix pomatia
Nivel de calidad
Formulario
powder
actividad específica
≥0.2 U/mg
temp. de almacenamiento
−20°C
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Aplicación
β-(1→3)-D-Glucanase from 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 .
Acciones bioquímicas o fisiológicas
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 .
Envase
Bottomless glass bottle. Contents are inside inserted fused cone.
Definición de unidad
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
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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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
Enrico Ragni et al.
Fungal genetics and biology : FG & B, 48(8), 793-805 (2011-05-24)
Cell wall biogenesis is a dynamic process relying on the coordinated activity of several extracellular enzymes. PHR1 is a pH-regulated gene of Candida albicans encoding a glycosylphosphatidylinositol-anchored β(1,3)-glucanosyltransferase of family GH72 which acts as a cell wall remodelling enzyme and
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
Tomonari Tamashiro et al.
Glycoconjugate journal, 29(1), 77-85 (2011-12-27)
A carbohydrate-binding module from family 13 (CBM13), appended to the catalytic domain of endo-1,3-β-glucanase from Cellulosimicrobium cellulans, was overexpressed in E. coli, and its interactions with β-glucans, laminarin and laminarioligosaccharides, were analyzed using surface plasmon resonance biosensor and isothermal titration
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
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