C1184
Cellulase from Aspergillus niger
powder, ≥0.3 units/mg solid
Synonym(s):
1,4-(1,3:1,4)-β-D-Glucan 4-glucanohydrolase
Sign Into View Organizational & Contract Pricing
All Photos(4)
About This Item
Recommended Products
form
powder
Quality Level
specific activity
≥0.3 units/mg solid
greener alternative product characteristics
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
greener alternative category
, Enabling
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
Related Categories
General description
The FDA recognizes cellulase from A. niger as GRAS (Generally Regarded As Safe) if non-pathogenic and non-toxigenic strains, as well as current good manufacturing practices, are used in production.
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 used as enzyme for alternative energy. For more information see the Enzymes for Alternative Energy Research.
Cellulase belongs to the family of glycoside hydrolase, which is secreted by various cellulolytic microorganisms.
Cellulase belongs to the family of glycoside hydrolase, which is secreted by various cellulolytic microorganisms.
Application
Cellulase from Sigma has been used to study the ability of several of its possible substrates, cellulose, Avicel PH-101, and filter paper, to protect enzyme activity during monogastric diegstion in animal and avian digestive tracts.
The enzyme has also been approved as a secondary direct food additive as an aid in clam and shrimp processing.
Biochem/physiol Actions
Cellulase from Aspergillus niger catalyzes the hydrolysis of endo-1,4-β-D-glycosidic linkages in cellulose, lichenin, barley glucan, and the cellooligosaccharides cellotriose to cellohexaose. It does not cleave cellobiose or p-nitrophenyl-β-D-glucoside. This enzyme will also cleave intact glycosaminoglycan from a core peptide by hydrolyzing the xylosyl serine linkage.
Unit Definition
One unit will liberate 1.0 μmole of glucose from cellulose in one hr at pH 5.0 at 37 °C (2 hr incubation time).
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
substrate
Product No.
Description
Pricing
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Meena Ganesan et al.
Biotechnology for biofuels, 13, 124-124 (2020-07-21)
The current production of bioethanol based on lignocellulosic biomass (LCB) highly depends on thermostable enzymes and extremophiles owing to less risk of contamination. Thermophilic bacterial cellulases are preferred over fungi due to their higher growth rate, presence of complex multi-enzymes
E Schuster et al.
Applied microbiology and biotechnology, 59(4-5), 426-435 (2002-08-13)
Aspergillus niger is one of the most important microorganisms used in biotechnology. It has been in use already for many decades to produce extracellular (food) enzymes and citric acid. In fact, citric acid and many A. niger enzymes are considered
Structural organization and a standardized nomenclature for plant endo-1, 4-beta-glucanases (cellulases) of glycosyl hydrolase family 9
Urbanowicz BR, et al.
Plant Physiology, 144(4), 1693-1696 (2007)
Fuxi Shi et al.
ACS omega, 5(38), 24780-24789 (2020-10-06)
A major challenge in converting lignocellulose to biofuel is overcoming the resistance of the biomass structure. Herein, sequential dilute acid-alkali/aqueous ammonia treatment was evaluated to enhance enzymatic hydrolysis of poplar biomass by removing hemicellulose first and then removing lignin with
Arun Sampathkumar et al.
Development (Cambridge, England), 146(10) (2019-05-12)
How organisms attain their specific shapes and modify their growth patterns in response to environmental and chemical signals has been the subject of many investigations. Plant cells are at high turgor pressure and are surrounded by a rigid yet flexible
Protocols
To standardize an enzymatic assay procedure of cellulase.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service