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
Sinônimo(s):
Cel7A, Cellobiosidase, Cellulase
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About This Item
Preço e disponibilidade não estão disponíveis no momento.
Produtos recomendados
recombinante
expressed in corn
Formulário
liquid
atividade específica
0.13 U/mg
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Condições de expedição
dry ice
temperatura de armazenamento
−20°C
Categorias relacionadas
Descrição geral
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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Aplicação
Cellobiohydrolase I can be used in combination with endocellulases and b-glucosidase to produce glucose from cellulose.
Ações bioquímicas/fisiológicas
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.
Definição da unidade
Unit Definition: A unit will turn over 1 nmole of methyl-umbelliferyl beta-D cellobioside per min at pH 5 at 50° C.
forma física
Provided as an ammonium sulfate precipitate with the source as recombinant maize.
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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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
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
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
Microbial cellulases-Production, applications and challenges.
Sukumaran RK, et al.
J. Sci. Ind. Res., 64(11), 832-844 (2005)
Artigos
Uncover more about glycosaminoglycans and proteoglycans including the structure of glycosaminoglycans (GAGs), the different types of GAGs, and their functions.
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