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Enzyme Activity Measurement for Cellulose 1,4-Beta-Cellobiosidase (Non-Reducing End)

Creative Enzymes is proud to offer various enzyme activity assays for customers, such as rapid routine quantification or custom activity tests. We are committed to being the most reliable provider specialized in enzymatic activity measurement in the global market. Extensive experiences, state-of-the-art technology, and high customer satisfaction help us gain a good reputation. Here, we announce the most accurate enzyme activity assay for cellulose 1,4-beta-cellobiosidase (non-reducing end).

Cellulose 1,4-beta-cellobiosidase (non-reducing end) is a retaining exo-cellulase that hydrolyzes the β-1,4-linkages of a cellulose chain from its reducing end to release β-cellobiose as the main product. The enzyme is designated as EC 3.2.1.91 and also known as 4-β-D-glucan cellobiohydrolase (non-reducing end) or cellobiohydrolases. The crystal structure of the catalytic domain of cellobiohydrolase revealed a long cellulose-binding tunnel that could provide a large number of interactions for a single cellulose chain. The cellobiohydrolases belong to the glycosyl hydrolase family 7 (GH-7), which contain enzymes that seem to be especially important in the hydrolysis of highly crystalline cellulose and are found only in the fungal kingdom. The best known GH-7 cellobiohydrolase is the Cel7A from the mesophilic fungus Trichoderma reesei. Functionally, cellobiohydrolase plays a pivotal role in paper, detergent and textile industry. It is especially important in hydrolyzing cellulose to soluble sugars, which requires the cooperative action of three groups of cellulolytic enzymes, endo-β-1,4-glucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) and β-glucosidases (EC 3.2.1.21). The synergy of these enzyme was found naturally in microbes that reside in rotting wood by producing a wide range of hydrolytic enzymes to degrade recalcitrant cellulosic structures. Cellulose itself is a chemically simple polymer, consisting of β-1,4-linked D-glucosyl units, and cannot be selectively hydrolyzed by chemical means or efficiently digested by human. Therefore, cellobiohydrolase has gained growing interests from environmental and chemical industries for its potential use in utilization of biomass, recycling wastes, and environment friendly production of valuable chemicals.

Creative Enzymes performs the highly customizable enzymatic activity measurement for cellobiohydrolase. The activity of cellobiohydrolase is determined through reliable spectrophotometric assays. We deliver the test results in the shortest span of time from the date of order placement. The unique advantage on our spectrophotometric analysis allows us to exceed competitors and assures the accuracy of the test results. Creative Enzymes is the best partner for enzyme activity assays and always support diverse and unique customers in various research activities.

The crystal structure of cellulose 1,4-beta-cellobiosidase from Trichoderma Harzianum Figure: The crystal structure of cellulose 1,4-beta-cellobiosidase from Trichoderma Harzianum.
PDB: 2Y9N