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E6412

Sigma-Aldrich

Cellobiohydrolase I from Hypocrea jecorina

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0.13 U/mg, recombinant, expressed in corn

Sinónimos:

Cel7A, Cellobiosidase, Cellulase

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About This Item

Comisión internacional de enzimas:
3.2.1.91 (BRENDA, IUBMB)
EC Number:
253-465-9
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in corn

Quality Level

200

form

liquid

specific activity

0.13 U/mg

greener alternative product characteristics

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

sustainability

Greener Alternative Product

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

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
0000401510
0000385097
0000353852
0000299837
0000401510

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Larissa C Textor et al.
The FEBS journal, 280(1), 56-69 (2012-11-02)
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic enzymes, we report here the first crystal structure of the catalytic core domain of Cel7A (cellobiohydrolase I) from the filamentous fungus Trichoderma harzianum IOC 3844. Our structural studies and
Svein J Horn et al.
Methods in enzymology, 510, 69-95 (2012-05-23)
Natural cellulolytic enzyme systems as well as leading commercial cellulase cocktails are dominated by enzymes that degrade cellulose chains in a processive manner. Despite the abundance of processivity among natural cellulases, the molecular basis as well as the biotechnological implications
Kiyohiko Igarashi et al.
Methods in enzymology, 510, 169-182 (2012-05-23)
Cellulases hydrolyze β-1,4-glucosidic linkages of insoluble cellulose at the solid/liquid interface, generating soluble cellooligosaccharides. We describe here our method for real-time observation of the behavior of cellulase molecules on the substrate, using high-speed atomic force microscopy (HS-AFM). When glycoside hydrolase
Naohisa Sugimoto et al.
Langmuir : the ACS journal of surfaces and colloids, 28(40), 14323-14329 (2012-09-07)
Cellobiohydrolases (CBHs) hydrolyzing crystalline cellulose share a two-domain structure of catalytic domain (CD) and cellulose-binding domain (CBD). To focus on the binding characteristics of CBD, we analyzed the adsorption of fusion protein of fungal family 1 CBD from Trichoderma reesei
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
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