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49101

Sigma-Aldrich

β-Glucanase from Aspergillus niger

greener alternative

powder, dark brown, ~1 U/mg

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About This Item

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

form

powder

specific activity

~1 U/mg

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

color

dark brown

greener alternative category

storage temp.

2-8°C

General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy eficiency and waste prevention when used in cellulosic ethanol research. For more information see the article in biofiles.

Biochem/physiol Actions

β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan.

Unit Definition

One unit corresponds to the amount of enzyme which will release 1 μmole of reducing sugar equivalents (expressed as glucose) per minute at pH 5.0 and 55 °C, using β-D-glucan (Cat. No. 49102) as substrate

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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Nhuan P Nghiem et al.
Applied biochemistry and biotechnology, 165(3-4), 870-882 (2011-06-15)
A fermentation process, which was designated the enhanced dry grind enzymatic (EDGE) process, has recently been developed for barley ethanol production. In the EDGE process, in addition to the enzymes normally required for starch hydrolysis, commercial β-glucanases were used to
Chengwei Hua et al.
Applied microbiology and biotechnology, 88(2), 509-518 (2010-07-21)
In this study, a novel beta-1,3-1,4-glucanase gene (designated as PtLic16A) from Paecilomyces thermophila was cloned and sequenced. PtLic16A has an open reading frame of 945 bp, encoding 314 amino acids. The deduced amino acid sequence shares the highest identity (61%)
Yigang Teng et al.
Acta biochimica et biophysica Sinica, 42(10), 729-734 (2010-09-28)
In this study, we confirmed that at least three endo-β-1,4-glucanases existed in the digestive juice of the giant snail, Achatina fulica ferussac, by Congo red staining assay. One of these enzymes, a novel endo-β-1,4-glucanase (AfEG22), was purified 29.5-fold by gel
Juntao Sun et al.
Biotechnology letters, 33(11), 2193-2199 (2011-07-08)
A new fusion gene (Bgl-licMB), encoding β-1,3-1,4-glucanase both from Bacillus amyloliquefaciens (Bgl) and Clostridium thermocellum (licMB), was constructed via end-to-end fusion and expressed in Escherichia coli to improve hydrolytic activity and thermostability of β-1,3-1,4-glucanase. The results of enzymatic properties showed
Kenji Matsuura et al.
Current biology : CB, 19(1), 30-36 (2008-12-27)
Insects and fungi share a long history of association in various habitats, including the wood-decomposition niche. Fungal mimicry of termite eggs is one of the most striking evolutionary consequences of insect-fungus association. Termites of the genus Reticulitermes often harbor fungal

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