Skip to Content
Merck
All Photos(3)

Key Documents

View All Documentation

C2730

Sigma-Aldrich

Cellulase from Trichoderma reesei

greener alternative

aqueous solution, ≥700 units/g

Synonym(s):

Celluclast®, Celluclast® 1.5L

Sign Into View Organizational & Contract Pricing
All Photos(3)

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

Looking for similar products? Visit Product Comparison Guide

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

Health hazard
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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Production of cellulase by Trichoderma reesei from pretreated straw and furfural residues
Zhao CH, et al.
Royal Society of Chemistry Advances, 8(63), 36233-36238 (2018)
Studies on the production and application of cellulase from Trichoderma reesei QM-9414
Krishna SH, et al.
Bioprocess Engineering, 22(5), 467-470 (2000)
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
New insights into the enzymatic hydrolysis of lignocellulosic polymers by using fluorescent tagged carbohydrate-binding modules
Khatri V, et al.
Sustainable Energy & Fuels, 2(2), 479-491 (2018)
S Luti et al.
International journal of biological macromolecules, 165(Pt B), 2845-2854 (2021-03-20)
Cerato-platanin family (CPF) proteins are produced by fungi and elicit defences when applied to plants, behaving as PAMPs/MAMPs. CPF proteins share structural similarity to plant and bacterial expansins, and have been demonstrated, in some cases, to possess expansin-like loosening activity
View All Related Papers

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