49101
β-Glucanase from Aspergillus niger
powder, dark brown, ~1 U/mg
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About This Item
Productos recomendados
form
powder
Quality Level
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Youn-Ju Jung et al.
Indian journal of biochemistry & biophysics, 47(4), 203-210 (2010-12-24)
A gene encoding a beta-1,3-1,4-glucanase (CelA) belonging to family 5 of glycoside hydrolases was cloned and sequenced from the Bacillus subtilis A8-8. The open-reading-frame of celA comprised 1499 base pairs and the enzyme was composed of 500 amino acids with
Jiufu Qin et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 26(9), 1293-1301 (2010-12-15)
In vitro evolution methods are often used to modify protein with improved characteristics. We developed a directed evolution protocol to enhance the thermostability of the beta-1,3-1,4-glucanase. The thermostability of the enzyme was significantly improved after two rounds of directed evolution.
Chengwei Hua et al.
Bioscience, biotechnology, and biochemistry, 75(9), 1807-1812 (2011-09-08)
The cDNA encoding β-1,3(4)-glucanase, named PsBg16A, from Paecilomyces sp. FLH30 was cloned, sequenced, and over expressed in Pichia pastoris, with a yield of about 61,754 U mL⁻¹ in a 5-L fermentor. PsBg16A has an open reading frame of 951 bp
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
T Kanda et al.
Journal of biochemistry, 79(5), 989-995 (1976-05-01)
An endo-cellulase [EC 3.2.1.4.] of carboxymethyl-cellulase type (F-1) which was fractionated from culture filtrate of Irpex lacetus and purified to electrophoretic and ultracentrifugal homogeneity, was found to show xylanase [EC 3.2.1.8.] activity. The activity was not removed from any of
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