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Merck

C1184

Sigma-Aldrich

Cellulase from Aspergillus niger

greener alternative

powder, ≥0.3 units/mg solid

Synonim(y):

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

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About This Item

Numer CAS:
Numer EC enzymu:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54

291,00 zł


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Formularz

powder

Poziom jakości

aktywność właściwa

≥0.3 units/mg solid

charakterystyka ekologicznej alternatywy

Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

kategoria ekologicznej alternatywy

temp. przechowywania

2-8°C

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Opis ogólny

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]

Zastosowanie

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]

Działania biochem./fizjol.

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.

Definicja jednostki

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).
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substrat

Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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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)

Protokoły

To standardize an enzymatic assay procedure of cellulase.

Ten protokół wykorzystuje test spektrofotometryczny do oceny aktywności celulazy. Celulaza z Aspergillus niger katalizuje hydrolizę wiązań endo-1,4-β-D-glikozydowych.

Questions

1–6 of 6 Questions  
  1. Can you please provide the percent purity of the product?

    1 answer
    1. The product is offered on the basis of activity. The purity has not been determined.

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  2. Does product C1184 have hemicellulase activity, such as xylanase? I am looking for cellulase without hemicellulase activity.

    1 answer
    1. Hemicellulase activity of this product has not been tested.

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  3. What is the solution stability of Cellulase, Product C1184?

    1 answer
    1. 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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  4. What is the molecular weight of Product C1184, Cellulase from Aspergillus niger?

    1 answer
    1. The molecular weight is 26,000 Daltons.

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  5. Are there any additives to Cellulase, Product C1184, in addition to the enzyme itself?

    1 answer
    1. 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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  6. What is the Department of Transportation shipping information for this product?

    1 answer
    1. 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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