E6412
Cellobiohydrolase I from Hypocrea jecorina
0.13 U/mg, recombinant, expressed in corn
Synonym(s):
Cel7A, Cellobiosidase, Cellulase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
recombinant
expressed in corn
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
shipped in
dry ice
storage temp.
−20°C
Related Categories
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.
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.
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.
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
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
Microbial cellulases-Production, applications and challenges.
Sukumaran RK, et al.
J. Sci. Ind. Res., 64(11), 832-844 (2005)
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
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