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C2730

Cellulase from Trichoderma reesei

Name: Cellulase from <I>Trichoderma reesei</I>
Brand: SIGMA

aqueous solution, ≥700 units/g

Synonym(s):

Celluclast^®, Celluclast^® 1.5L

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About This Item

CAS Number:

9012-54-8

Enzyme Commission number:

3.2.1.4 (BRENDA, IUBMB)

EC Number:

232-734-4

MDL number:

MFCD00081510

UNSPSC Code:

12352204

NACRES:

NA.54

biological source

fungus (Trichoderma reesei)

form

aqueous solution

specific activity

≥700 units/g

mol wt

68 kDa

greener alternative product characteristics

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

sustainability

Greener Alternative Product

density

1.10-1.30 g/mL

greener alternative category

Enabling,

storage temp.

2-8°C

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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 efficiency and waste prevention when used in cellulosic ethanol research. For more information see the article in biofiles and Enzymes for Alternative Energy Research.

Cellulase from Trichoderma reesei is produced by submerged fermentation of a selected strain of the fungus Trichoderma reesei and catalyzes the breakdown of cellulose into glucose, cellobiose, and higher glucose polymers. It corresponds to a molecular mass of 68 kDa with optimum pH and temperature of 6 and 52° C, respectively.

Application

Cellulase from Trichoderma reesei has been used:

for aqueous extraction of oil from corn germ
in the enzymatic hydrolysis of Sweet Sorghum Bagasse (SSB)
in the enzymatic digestion of paper grids

Cellulase from Sigma has been used to degrade cello-oligosaccharides into glucose in order to investigate the biodegradability of bioabsorbable bacterial cellulose (BBC).

Biochem/physiol Actions

Cellulase complexes with β-glucosidase for degrading cellobiose to glucose polymer. The lignin content in straw and furfural residues hampers cellulase production.

Legal Information

A product of Novozyme Corp.

Celluclast is a registered trademark of Novozymes Corp.

Pictograms

GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

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’.

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Purification and characterization of cellulase from Trichoderma reesei.

Zhu N, et al.

Chinese Journal of Bioprocess Engineering, 8(3), 40-43 (2010)

Lipid production by Cryptococcus curvatus on hydrolysates derived from corn fiber and sweet sorghum bagasse following dilute acid pretreatment

Liang Y, et al.

Applied Biochemistry and Biotechnology, 173(8), 2086-2098 (2014)

Revalorization of sunflower stalk pith as feedstock for the coproduction of pectin and glucose using a two-step dilute acid pretreatment process.

Qibo Zhang et al.

Biotechnology for biofuels, 14(1), 194-194 (2021-10-03)

Sunflower stalk pith, residue from the processing of sunflower, is rich in pectin and cellulose, thereby acting as an economic raw material for the acquisition of these compounds. In order to increase the commercial value of sunflower processing industry, a

A biorefinery approach for the production of ferulic acid from agroresidues through ferulic acid esterase of lactic acid bacteria.

Abha Sharma et al.

3 Biotech, 10(8), 367-367 (2020-08-25)

Ferulic acid is a known precursor for vanillin production but the significance of agro waste as substrates for its extraction, in combination with microbes is a less explored option. Various lactic acid bacteria were screened for the production of ferulic

Studies on the production and application of cellulase from Trichoderma reesei QM-9414

Krishna SH, et al.

Bioprocess Engineering, 22(5), 467-470 (2000)

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