The product is offered on the basis of activity. The purity has not been determined.
C1184
Cellulase from Aspergillus niger
powder, ≥0.3 units/mg solid
Synonyme(s) :
1,4-(1,3:1,4)-β-D-Glucan 4-glucanohydrolase
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5000 UNITS
89,50 €
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115,00 €
100000 UNITS
746,00 €
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5000 UNITS
89,50 €
25000 UNITS
115,00 €
100000 UNITS
746,00 €
About This Item
Produits recommandés
Forme
powder
Niveau de qualité
Activité spécifique
≥0.3 units/mg solid
Caractéristiques du produit alternatif plus écologique
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
Autre catégorie plus écologique
, Enabling
Température de stockage
2-8°C
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Description générale
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,[1] which is secreted by various cellulolytic microorganisms.[2]
Cellulase belongs to the family of glycoside hydrolase,[1] which is secreted by various cellulolytic microorganisms.[2]
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.[3]
The enzyme has also been approved as a secondary direct food additive as an aid in clam and shrimp processing.[4]
Actions biochimiques/physiologiques
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.
Définition de l'unité
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).
Autres remarques
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Substrat
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Certificats d'analyse (COA)
Lot/Batch Number
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Les clients ont également consulté
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
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
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
Usage of Enzyme Substrate to Protect the Activities of Cellulase, Protease and α-Amylase in Simulations of Monogastric Animal and Avian Sequential Total Tract Digestion
Wang HT and Hsu JT
Asian-Australasian Journal of Animal Sciences, 19(8), 1164-1173 (2006)
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)
Protocoles
To standardize an enzymatic assay procedure of cellulase.
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Can you please provide the percent purity of the product?
1 réponse-
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Does product C1184 have hemicellulase activity, such as xylanase? I am looking for cellulase without hemicellulase activity.
1 réponse-
Hemicellulase activity of this product has not been tested.
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What is the solution stability of Cellulase, Product C1184?
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Sigma-Aldrich has not determined the solution stability for this product. However, it is reported in Methods in Enzymology, 160, 264 (1988) that cellulase from Aspergillus niger is "completely stable over the range of pH 5.0-8.0 at 4°C for 24 hours and retains about 50% of its original activity after heating at 70°C for 10 minutes. The enzyme is completely inactivated by heating at 80°C for 10 minutes".
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What is the molecular weight of Product C1184, Cellulase from Aspergillus niger?
1 réponse-
The molecular weight is 26,000 Daltons.
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What is the Department of Transportation shipping information for this product?
1 réponse-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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Are there any additives to Cellulase, Product C1184, in addition to the enzyme itself?
1 réponse-
Per information from our supplier, maltodextrin is an extender in this product. Maltodextrin can vary in glucose chain lengths of 2-12. There can also be some free glucose in the product. Either sorbitol or propylene glycol is added to the product as a stabilizer during processing. These components may be "flashed off" during processing, but some small amount may still be present.
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