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C1184

Sigma-Aldrich

Cellulase from Aspergillus niger

greener alternative

powder, ≥0.3 units/mg solid

Synonyme(s) :

1,4-(1,3:1,4)-β-D-Glucan 4-glucanohydrolase

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About This Item

Numéro CAS:
9012-54-8
Numéro de classification (Commission des enzymes):
3.2.1.4 (BRENDA, IUBMB)
Numéro CE :
232-734-4
Numéro MDL:
MFCD00081510
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

powder

Niveau de qualité

200

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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Catégories apparentées

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, 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.

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

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

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
0000365062
0000365061
0000365062
0000365061
0000327486

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
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)
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)
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Protocoles

Enzymatic Assay of Cellulase

To standardize an enzymatic assay procedure of cellulase.

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