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E6412

Sigma-Aldrich

Cellobiohydrolase I from Hypocrea jecorina

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0.13 U/mg, recombinant, expressed in corn

Synonym(s):

Cel7A, Cellobiosidase, Cellulase

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About This Item

Enzyme Commission number:
3.2.1.91 (BRENDA, IUBMB)
EC Number:
253-465-9
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in corn

form

liquid

specific activity

0.13 U/mg

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Design for Energy Efficiency
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sustainability

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greener alternative category

Enabling,

shipped in

dry ice

storage temp.

−20°C

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General description

Cellubiohydrolase I is an enzyme present in many fungi, but particularly wood rot fungi. It is a monomer of 53 kDa with a catalytic domain and a cellulose binding domain. The reaction adds water to the glucose bonds in cellulose (non-reducing ends of the chain), yielding cellobiose.
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Application

Cellobiohydrolase I can be used in combination with endocellulases and b-glucosidase to produce glucose from cellulose.

Biochem/physiol Actions

Cellobiohydrolase (CBH) is a cellulase which degrades cellulose by hydrolysing the 1,4-β-D-glycosidic bonds. CBH is an exocellulase which cleaves two to four units from the ends of cellulose. CBH I cleaves progressively from the reducing end. CBH I is commonly used in detergents for cleaning textiles. Its ezymatic activity ranges from 37° C to 50° C, with its optimal temperature being approximately 45° C. The optimum pH for the enzyme is 5-6.

Unit Definition

Unit Definition: A unit will turn over 1 nmole of methyl-umbelliferyl beta-D cellobioside per min at pH 5 at 50° C.

Physical form

Provided as an ammonium sulfate precipitate with the source as recombinant maize.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

E6412-BULK:
E6412-VAR:
E6412-100UN:

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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Oren Yaniv et al.
Acta crystallographica. Section D, Biological crystallography, 68(Pt 7), 819-828 (2012-07-04)
The crystal structure of the family 3b carbohydrate-binding module (CBM3b) of the cellulosomal multimodular hydrolytic enzyme cellobiohydrolase 9A (Cbh9A) from Clostridium thermocellum has been determined. Cbh9A CBM3b crystallized in space group P4(1) with four molecules in the asymmetric unit and
Jenni Liisa Rahikainen et al.
Bioresource technology, 146, 118-125 (2013-08-08)
Non-productive enzyme adsorption onto lignin inhibits enzymatic hydrolysis of lignocellulosic biomass. Three cellobiohydrolases, Trichoderma reesei Cel7A (TrCel7A) and two engineered fusion enzymes, with distinctive modular structures and temperature stabilities were employed to study the effect of temperature on inhibition arising
Nicolaj Cruys-Bagger et al.
The Journal of biological chemistry, 287(22), 18451-18458 (2012-04-12)
The transient kinetic behavior of enzyme reactions prior to the establishment of steady state is a major source of mechanistic information, yet this approach has not been utilized for cellulases acting on their natural substrate, insoluble cellulose. Here, we elucidate
Nicolaj Cruys-Bagger et al.
Biotechnology and bioengineering, 109(12), 3199-3204 (2012-07-07)
An amperometric enzyme biosensor for continuous detection of cellobiose has been implemented as an enzyme assay for cellulases. We show that the initial kinetics for cellobiohydrolase I, Cel7A from Trichoderma reesei, acting on different types of cellulose substrates, semi-crystalline and
Zachary K Haviland et al.
The Journal of biological chemistry, 297(3), 101029-101029 (2021-08-03)
Understanding the mechanism by which cellulases from bacteria, fungi, and protozoans catalyze the digestion of lignocellulose is important for developing cost-effective strategies for bioethanol production. Cel7A from the fungus Trichoderma reesei is a model exoglucanase that degrades cellulose strands from
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