This product is provided as a slurry containing 10 mg of enzyme in saturated ammonium sulfate precipitate. It is supplied at 100 units, with a concentration of 0.13 units per 1 mg of protein at 10 mg per ml.
E6412
Cellobiohydrolase I from Hypocrea jecorina
0.13 U/mg, recombinant, expressed in corn
Synonyme(s) :
Cel7A, Cellobiosidase, Cellulase
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100 UNITS
170,00 $
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100 UNITS
170,00 $
About This Item
170,00 $
Veuillez contacter notre Service Clients pour connaître la disponibilité de ce produit.
Produits recommandés
Produit recombinant
expressed in corn
Forme
liquid
Activité spécifique
0.13 U/mg
Caractéristiques du produit alternatif plus écologique
Design for Energy Efficiency
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sustainability
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Autre catégorie plus écologique
Conditions d'expédition
dry ice
Température de stockage
−20°C
Catégories apparentées
Description générale
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.
Actions biochimiques/physiologiques
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.
Définition de l'unité
Unit Definition: A unit will turn over 1 nmole of methyl-umbelliferyl beta-D cellobioside per min at pH 5 at 50° C.
Forme physique
Provided as an ammonium sulfate precipitate with the source as recombinant maize.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
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
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
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
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
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