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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

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

Helix pomatia

Livello qualitativo

Forma fisica

powder

Attività specifica

≥0.2 U/mg

Temperatura di conservazione

−20°C

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Applicazioni

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 .

Azioni biochim/fisiol

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 .

Confezionamento

Bottomless glass bottle. Contents are inside inserted fused cone.

Definizione di unità

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

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Yoichi Tanabe et al.
Biochimica et biophysica acta, 1814(12), 1713-1719 (2011-10-08)
An endo-1,3-β-glucanase was purified from Tunicase®, a crude enzyme preparation from Cellulosimicrobium cellulans DK-1, and determined to be a 383-residue protein (Ala1-Leu383), comprising a catalytic domain of the glycoside hydrolase family 16 and a C-terminal carbohydrate-binding module family 13. The
Enrico Cabib et al.
Eukaryotic cell, 11(4), 388-400 (2012-03-01)
Previous results suggested that the chitin ring present at the yeast mother-bud neck, which is linked specifically to the nonreducing ends of β(1-3)glucan, may help to suppress cell wall growth at the neck by competing with β(1-6)glucan and thereby with
Marián Mazáň et al.
The Biochemical journal, 438(2), 275-282 (2011-06-10)
BGTs [β-(1,3)-glucanosyltransglycosylases; EC 2.4.1.-] of the GH72 (family 72 of glycosylhydrolases) are GPI (glycosylphosphatidylinositol)-anchored proteins that play an important role in the biogenesis of fungal cell walls. They randomly cleave glycosidic linkages in β-(1,3)-glucan chains and ligate the polysaccharide portions
Nina Klippel et al.
Microbiology (Reading, England), 156(Pt 11), 3432-3444 (2010-08-07)
The pathogenic fungus Candida albicans is able to cover its most potent proinflammatory cell wall molecules, the β-glucans, underneath a dense mannan layer, so that the pathogen becomes partly invisible for immune cells such as phagocytes. As the C. albicans
Poonam Gautam et al.
Mycopathologia, 172(5), 331-346 (2011-07-15)
Artemisinin, an antimalarial drug, and its derivatives are reported to have antifungal activity against some fungi. We report its antifungal activity against Aspergillus fumigatus (A. fumigatus), a pathogenic filamentous fungus responsible for allergic and invasive aspergillosis in humans, and its

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