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E6412

Sigma-Aldrich

Cellobiohydrolase I from Hypocrea jecorina

greener alternative

0.13 U/mg, recombinant, expressed in corn

Synonym(e):

Cel7A, Cellobiosidase, Cellulase

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100 UNITS
161,00 €

161,00 €

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100 UNITS
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About This Item

EC-Nummer:
3.2.1.91 (BRENDA, IUBMB)
EG-Nummer:
253-465-9
UNSPSC-Code:
12352204
NACRES:
NA.54

161,00 €

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Rekombinant

expressed in corn

Qualitätsniveau

200

Form

liquid

Spezifische Aktivität

0.13 U/mg

Grünere Alternativprodukt-Eigenschaften

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

sustainability

Greener Alternative Product

Grünere Alternativprodukt-Kategorie

Enabling,

Versandbedingung

dry ice

Lagertemp.

−20°C

Verwandte Kategorien

Allgemeine Beschreibung

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.
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. Find details here.

Anwendung

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

Biochem./physiol. Wirkung

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.[1] 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.

Einheitendefinition

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

Physikalische Form

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

Piktogramme

Health hazard
GHS08

Signalwort

Danger

H-Sätze

H334

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number
0000401510
0000385097
0000299837
0000353852
0000353852

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Die Dokumentenbibliothek aufrufen

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
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
Microbial cellulases-Production, applications and challenges.
Sukumaran RK, et al.
J. Sci. Ind. Res., 64(11), 832-844 (2005)
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