Results 51 to 60 of about 6,340 (193)
Capturing single cell genomes of active polysaccharide degraders: an unexpected contribution of Verrucomicrobia. [PDF]
PLoS ONE, 2012 Microbial hydrolysis of polysaccharides is critical to ecosystem functioning and is of great interest in diverse biotechnological applications, such as biofuel production and bioremediation.
Manuel Martinez-Garcia +17 more
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The K5 Lyase KflA Combines a Viral Tail Spike Structure with a Bacterial Polysaccharide Lyase Mechanism [PDF]
Journal of Biological Chemistry, 2010 K5 lyase A (KflA) is a tail spike protein (TSP) encoded by a K5A coliphage, which cleaves K5 capsular polysaccharide, a glycosaminoglycan with the repeat unit [-4)-betaGlcA-(1,4)- alphaGlcNAc(1-], displayed on the surface of Escherichia coli K5 strains.
James Thompson +6 more
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Frontiers in Microbiology, 2019 Studying the physiology and genomics of cultured hydrolytic bacteria is a valuable approach to decipher the biogeochemical cycling of marine polysaccharides, major nutrients derived from phytoplankton and macroalgae.
Hanna Koch +4 more
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Frontiers in Microbiology, 2021 Carbohydrate-active enzymes (CAZymes) are an important feature of bacteria in productive marine systems such as continental shelves, where phytoplankton and macroalgae produce diverse polysaccharides.
Laura A. Wolter +7 more
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Characterization of a Novel PolyM-Preferred Alginate Lyase from Marine Vibrio splendidus OU02
Marine Drugs, 2018 Alginate lyases are enzymes that degrade alginate into oligosaccharides which possess a variety of biological activities. Discovering and characterizing novel alginate lyases has great significance for industrial and medical applications.
Jingjing Zhuang +5 more
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Molecules, 2023 Alginate oligosaccharides (AOs) prepared through enzymatic reaction by diverse alginate lyases under relatively controllable and moderate conditions possess versatile biological activities. But widely used commercial alginate lyases are still rather rare
Hai-Ying Wang +5 more
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A Polysaccharide Lyase from Stenotrophomonas maltophilia with a Unique, pH-regulated Substrate Specificity [PDF]
Journal of Biological Chemistry, 2013 Polysaccharide lyases (PLs) catalyze the depolymerization of anionic polysaccharides via a β-elimination mechanism. PLs also play important roles in microbial pathogenesis, participating in bacterial invasion and toxin spread into the host tissue via degradation of the host extracellular matrix, or in microbial biofilm formation often associated with ...
Logan C. MacDonald, Bryan W. Berger
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A new family of β-helix proteins with similarities to the polysaccharide lyases
Acta Crystallographica Section D Biological Crystallography, 2014 Microorganisms that degrade biomass produce diverse assortments of carbohydrate-active enzymes and binding modules. Despite tremendous advances in the genomic sequencing of these organisms, many genes do not have an ascribed function owing to low sequence identity to genes that have been annotated.
Devin W. Close +2 more
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Foods, 2022 Alginate lyases (ALyases) have been widely applied in enzymatically degrading alginate for the preparation of alginate oligosaccharides (AOS), which possess a range of excellent physiological benefits including immunoregulatory, antivirus, and antidiabetic properties.
Licheng Zhou +6 more
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Frontiers in Microbiology, 2018 Endo-type alginate lyases usually degrade alginate completely into various size-defined unsaturated oligosaccharide products (≥disaccharides), while exoenzymes primarily produce monosaccharide products including saturated mannuronate (M) and guluronate ...
Chune Peng +4 more
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