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A New Versatile Microarray-based Method for High Throughput Screening of Carbohydrate-active Enzymes
Carbohydrate-active enzymes have multiple biological roles and industrial applications. Advances in genome and transcriptome sequencing together with associated bioinformatics tools have identified vast numbers of putative carbohydrate-degrading and ...
Silvia Vidal-Melgosa +2 more
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International audienceWe report here the development of a straightforward, sensitive, and quantitative NMR-based method for high-throughput characterization of carbohydrate structure and screening of carbohydrate active enzyme (CAZyme) specificity ...
Stéphane Massou +2 more
exaly +2 more sources
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Role of carbohydrate-active enzymes in mycorrhizal symbioses
Essays in Biochemistry, 2023Abstract Mycorrhizal fungi form mutually beneficial interactions with a wide range of terrestrial plants. During this symbiosis, the associated fungus provides mineral nutrients, such as phosphorus and nitrogen, to its host plant in exchange of photosynthesis-derived carbohydrates.
Gong, Yuhua +3 more
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Carbohydrate-active enzymes (CAZymes) in the gut microbiome
Nature Reviews Microbiology, 2022The 1013-1014 microorganisms present in the human gut (collectively known as the human gut microbiota) dedicate substantial percentages of their genomes to the degradation and uptake of carbohydrates, indicating the importance of this class of molecules.
Jacob F. Wardman +3 more
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Enzyme promiscuity of carbohydrate active enzymes and their applications in biocatalysis
Current Opinion in Structural Biology, 2020The application of biocatalysis for the synthesis of glycans and glycoconjugates is a well-established and successful strategy, both for small and large scale synthesis. Compared to chemical synthesis, is has the advantage of high selectivity, but biocatalysis had been largely limited to natural glycans both in terms of reactivity and substrates.
Edward, Pallister +2 more
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New technologies based on microarray methods have begun to feature widely in carbohydrate chemistry and biology. These ‘glycoarray’ techniques, which in a number of cases emulate what has been achieved with DNA microarrays, allow for high throughput ...
David A Russell, Robert A Field
exaly +2 more sources
Why are there so many carbohydrate-active enzyme-related genes in plants?
Plants contain far more carbohydrate-active enzyme-encoding genes than any other organism sequenced to date. The extremely large number of glycosidase and glycosyltransferase-related genes in plant genomes can be explained by the complex structure of the
Pedro M Coutinho +2 more
exaly +1 more source
Building mutational bridges between carbohydrate-active enzymes
Current Opinion in Biotechnology, 2022The commercial value of specialty carbohydrates and glycosylated compounds has sparked considerable interest in the synthetic potential of carbohydrate-active enzymes (CAZymes). Protein engineering methods have proven to be highly successful in expanding the range of glycosylation reactions that these enzymes can perform efficiently and cost ...
Jorick, Franceus +2 more
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Polymeric Iminosugars Improve the Activity of Carbohydrate-Processing Enzymes
Bioconjugate Chemistry, 2015Multivalent iminosugars have recently emerged as powerful tools to inhibit the activities of specific glycosidases. In this work, biocompatible dextrans were coated with iminosugars to form linear and ramified polymers with unprecedently high valencies (from 20 to 900) to probe the evolution of the multivalent inhibition as a function of ligand valency.
Brissonnet, Yoan +10 more
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Interaction of carbohydrates with alcohol dehydrogenase: Effect on enzyme activity
Journal of Bioscience and Bioengineering, 2015Alcohol dehydrogenase was covalently conjugated with three different oxidized carbohydrates i.e., glucose, starch and pectin. All the carbohydrates inhibited the enzyme. The inhibition was studied with respect to the inhibition rate constant, involvement of thiol groups in the binding, and structural changes in the enzyme. The enzyme activity decreased
Jadhav, Swati B. +6 more
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