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Action pattern of polysaccharide lyases on glycosaminoglycans
Glycobiology, 1994 The action pattern of polysaccharide lyases on glycosaminoglycan substrates was examined using viscosimetric measurements and gradient polyacrylamide gel electrophoresis (PAGE). Heparin lyase I (heparinase, EC 4.2.2.7) and heparin lyase II (no EC number) both acted on heparin in a random endolytic fashion.
Robert J Linhardt, Linhardt Robert J
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Analysis of Glycosaminoglycans with Polysaccharide Lyases
Current Protocols in Molecular Biology, 1999 Polysaccharide lyases are a class of enzymes useful for analysis of glycosaminoglycans (GAGs) and the glycosaminoglycan component of proteoglycans (PGs). These enzymes cleave specific glycosidic linkages present in acidic polysaccharides and result in depolymerization.
Robert J Linhardt
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Applied Biochemistry and Biotechnology, 1987
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert J Linhardt +2 more
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Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert J Linhardt +2 more
exaly +3 more sources
Polysaccharide Lyases: Recent Developments as Biotechnological Tools
Critical Reviews in Biotechnology, 2003Polysaccharide lyases, which are polysaccharide cleavage enzymes, act mainly on anionic polysaccharides. Produced by prokaryote and eukaryote organisms, these enzymes degrade (1,4) glycosidic bond by a beta elimination mechanism and have unsaturated oligosaccharides as major products.
Philippe Michaud, J Courtois
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Carbohydrate Research, 2004
A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen G Withers
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A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave ...
Stephen G Withers
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International Journal of Biological Macromolecules, 2021
Alginate and its derivatives are annually produced approximately 30,000 tons or more and are applied to various industries as they are natural polymers. The global market for alginate and its derivatives has been growing steadily. There is little research compared to other enzymes produced through biomass degradation or modification. An alginate lyase,
Hae-Rin, Jeong +4 more
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Alginate and its derivatives are annually produced approximately 30,000 tons or more and are applied to various industries as they are natural polymers. The global market for alginate and its derivatives has been growing steadily. There is little research compared to other enzymes produced through biomass degradation or modification. An alginate lyase,
Hae-Rin, Jeong +4 more
openaire +2 more sources
A Structural Basis for Depolymerization of Alginate by Polysaccharide Lyase Family-7
Journal of Molecular Biology, 2005Alginate lyases depolymerize alginate, a heteropolysaccharide consisting of alpha-L-guluronate and beta-D-mannuronate, through a beta-elimination reaction. Their structure/function relationships are expected to provide information valuable to future industrial alginate processing and drug design for Pseudomonas aeruginosa alginate biofilm-dependent ...
Masayuki, Yamasaki +4 more
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An engineered polysaccharide lyase to combat harmful algal blooms
Biochemical Engineering Journal, 2018Abstract A growing global population and industrialization have come at the cost of induced climate change and pollution of natural resources, resulting in formation of toxic algal blooms in fresh water sources. In the US alone, these blooms cost an estimated $1.5 billion dollars each year to remediate.
Evan Eckersley, Bryan W. Berger
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