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Key Documents

67138

Sigma-Aldrich

β-(1→3)-D-Glucanase from Helix pomatia

≥0.2 U/mg

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Helix pomatia

Quality Level

form

powder

specific activity

≥0.2 U/mg

storage temp.

−20°C

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Application

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 .

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 .

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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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
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
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
Magali Prigent et al.
Traffic (Copenhagen, Denmark), 12(8), 1084-1097 (2011-05-11)
The Rab GTPase-activating proteins (GAP) Gyp5p and Gyl1p are involved in the control of polarized exocytosis at the small-bud stage in Saccharomyces cerevisiae. Both Gyp5p and Gyl1p interact with the N-Bin1/Amphiphysin/Rvs167 (BAR) domain protein Rvs167p, but the biological function 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

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