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49101
β-Glucanase from Aspergillus niger
powder, dark brown, ~1 U/mg
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10 MG
CN¥160.95
25 G
CN¥225.31
100 G
CN¥696.70
1 KG
CN¥4,602.51
CN¥160.95
Available to ship onApril 14, 2025Details
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10 MG
CN¥160.95
25 G
CN¥225.31
100 G
CN¥696.70
1 KG
CN¥4,602.51
About This Item
CN¥160.95
Available to ship onApril 14, 2025Details
Recommended Products
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
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
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
Regulatory Information
常规特殊物品
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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%)
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
Xiaohu Shao et al.
New biotechnology, 29(3), 302-310 (2011-10-05)
An improved surface-immobilisation system was engineered to target heterologous proteins onto vegetative cells and spores of Bacillus thuringiensis plasmid-free recipient strain BMB171. The sporulation-dependent spore cortex-lytic enzyme from B. thuringiensis YBT-1520, SceA, was expressed in vegetative cells and used as
Pengjun Shi et al.
Applied and environmental microbiology, 76(11), 3620-3624 (2010-04-13)
Xylanases are utilized in a variety of industries for the breakdown of plant materials. Most native and engineered bifunctional/multifunctional xylanases have separate catalytic domains within the same polypeptide chain. Here we report a new bifunctional xylanase (XynBE18) produced by Paenibacillus
Rakesh Mohan Kestwal et al.
International journal of biological macromolecules, 49(5), 894-899 (2011-08-23)
Endo-1,3(4)-β-glucanase (EC 3.2.1.6) from Vigna aconitifolia sprouts was purified to 14.5 fold by gel filtration and ion-exchange chromatography. The enzyme was found to be a glycoprotein, its activity was Ca(2+) dependent and specific for β-1,3 linkages in different polysaccharides. The
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