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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:
EC Number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in corn

Quality Level

form

liquid

specific activity

0.13 U/mg

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sustainability

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shipped in

dry ice

storage temp.

−20°C

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

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Microbial cellulases-Production, applications and challenges.
Sukumaran RK, et al.
J. Sci. Ind. Res., 64(11), 832-844 (2005)
Christina M Payne et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(36), 14646-14651 (2013-08-21)
Plant cell-wall polysaccharides represent a vast source of food in nature. To depolymerize polysaccharides to soluble sugars, many organisms use multifunctional enzyme mixtures consisting of glycoside hydrolases, lytic polysaccharide mono-oxygenases, polysaccharide lyases, and carbohydrate esterases, as well as accessory, redox-active
Daguan Nong et al.
Biomedical optics express, 12(6), 3253-3264 (2021-07-06)
We describe a multimodal microscope for visualizing processive enzymes moving on immobilized substrates. The instrument combines interference reflection microscopy (IRM) with multi-wavelength total internal reflectance fluorescence microscopy (TIRFM). The microscope can localize quantum dots with a precision of 2.8 nm at
Daisuke Taneda et al.
Bioresource technology, 121, 154-160 (2012-08-04)
The effect of enzyme loading under static and agitated conditions was investigated. Enzymatic hydrolysis of 10 w/v% de-lignified cellulose slurry such as filter paper, avicel and pulp was conducted under agitated (120 rpm) and static condition, and the enzyme loading
K E Eriksson et al.
European journal of biochemistry, 51(1), 213-218 (1975-02-03)
An exo-1,4-beta-glucanase from culture solution of the rot fungus Sporotrichum pulverulentum (formerly called Chrysosporium lignorum) grown on powder cellulose as the sole carbon source has been extensively purified and characterized with respect to some physico-chemical properties. The purification has been

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