Carbohydrate-degrading Enzymes
Carbohydrate-degrading Enzymes - Related Videos
06:51
High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
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Cited by 5 •
2016
A high-throughput assay for enzyme screening is described. This multiplexed ready-to-use assay kit comprises of pre-chosen Chromogenic Polymer Hydrogel (CPH) substrates and complex Insoluble Chromogenic Biomass (ICB) substrates. Target enzymes are polysaccharide degrading endo-enzymes and proteases.
03:27
Insoluble Chromogenic Biomass-Based Enzyme Screening: An Assay to Evaluate the Degradation Activity of Plant Biomass-Degrading Enzymes
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2025
This video demonstrates an assay to screen enzymes effective in degrading complex polysaccharides in plant biomass using insoluble chromogenic biomass or ICB. The enzymes hydrolyze ICB to release soluble dye-linked oligosaccharides, and the enzyme activity is assessed by colorimetric analysis of the reaction product.
03:49
Chromogenic Polymer Hydrogel-Based Enzyme Screening Assay: A High Throughput Method to Screen the Carbohydrate-Active Enzymes Using Synthetic Substrates
0 Views •
2025
In this video, we demonstrate a high throughput assay for carbohydrate-active enzyme screening using insoluble chromogenic polymer hydrogel substrates. The enzyme degrades these substrates into a soluble colored product that can be quantified by measuring the color intensity of the product.
02:23
Performing Thin-Layer Chromatography to Assess Bacterial Exopolysaccharide Degradation
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2026
Source: Hu, Y., et al. Analysis of Interactions between Endobiotics and Human Gut Microbiota Using In Vitro Bath Fermentation Systems. J. Vis. Exp. (2019)This video demonstrates the use of thin-layer chromatography (TLC) to assess the degradation of exopolysaccharides (EPS) by human fecal microbiota. EPS fragments in fermentation supernatants are separated based on size and polarity using TLC, then visualized as colored bands following carbohydrate-specific staining.
14:37
High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles
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Cited by 7 •
2012
In this article, a high throughput method is presented for the synthesis of oligosaccharides and their attachment to the surface of polyanhydride nanoparticles for further use in targeting specific receptors on antigen presenting cells.
FAQs
Substrate specificity arises from the fit between an enzyme’s active site and particular carbohydrate structures. This selectivity determines which glycosidic bonds can be hydrolyzed and therefore which products form. In practice, matching the enzyme to the substrate helps researchers target starch, cellulose, pectin, or related materials while reducing reactions on unsuitable carbohydrate components.
These conditions influence how effectively the enzyme catalyzes glycosidic-bond hydrolysis and how much product is generated. Changes in pH or temperature can alter enzyme performance, while substrate composition affects which carbohydrate structures are available for reaction. Controlling these variables is therefore important when comparing experiments or seeking consistent yields from biological materials.
The enzymes differ primarily in the carbohydrate materials they act on. Amylases are associated with starch, cellulases with cellulose, and pectinases with pectin. Selecting among them allows researchers to examine or process distinct components of biological material, including storage carbohydrates and plant cell-wall constituents, rather than treating all complex carbohydrates as equivalent substrates.
The resulting mixture of oligosaccharides and monosaccharides can provide information about how a substrate was broken down and which carbohydrate structures were accessible. Product patterns help researchers analyze carbohydrate composition and investigate enzyme function. They can also indicate how effectively a selected enzyme converted a biological material under the tested reaction conditions.
A practical workflow begins by identifying the sample’s carbohydrate composition and selecting an enzyme with suitable substrate specificity. Researchers then control relevant reaction conditions, including pH, temperature, and substrate composition, before evaluating the sugars released. This approach supports both sample preparation and comparison of product yields across enzymes or experimental conditions.
They are useful when researchers need to modify, prepare, or analyze carbohydrate-rich biological materials. Enzymatic treatment can support biomass processing, food studies, and fermentation research by converting complex substrates into smaller sugars. The released products may help researchers assess material conversion and examine how carbohydrate availability relates to biological or processing outcomes.
Cell-wall studies can use enzyme selectivity to examine components such as cellulose and pectin, while metabolism research can track the smaller sugars generated from larger carbohydrates. These applications connect enzyme activity with substrate structure and microbial use of carbohydrates. As a result, the technique helps investigate both plant material organization and carbohydrate-processing functions in biological systems.