Results 181 to 190 of about 23,515 (209)

Characterization of an organic solvent-tolerant polysaccharide lyase from Microbulbifer thermotolerans DAU221

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
openaire   +4 more sources

An engineered polysaccharide lyase to combat harmful algal blooms

Biochemical Engineering Journal, 2018
Abstract 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
openaire   +3 more sources

A Structural Basis for Depolymerization of Alginate by Polysaccharide Lyase Family-7

Journal of Molecular Biology, 2005
Alginate 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
openaire   +4 more sources

Polysaccharide lyases

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.
R J, Linhardt   +2 more
openaire   +2 more sources

Polysaccharide Lyases: Recent Developments as Biotechnological Tools

Critical Reviews in Biotechnology, 2003
Polysaccharide 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.
P, Michaud   +3 more
openaire   +2 more sources

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.
K A, Jandik, K, Gu, R J, Linhardt
openaire   +2 more sources

The first structure of pectate lyase belonging to polysaccharide lyase family 3

Acta Crystallographica Section D Biological Crystallography, 2001
The crystal structure of a highly alkaline low molecular weight pectate lyase (Pel-15) was determined at 1.5 A resolution by the multiple isomorphous replacement (MIR) method. This is the first pectate lyase structure from polysaccharide lyase family 3.
M, Akita   +4 more
openaire   +2 more sources

Study of a novel glycoconjugate, thiopeptidoglycan, and a novel polysaccharide lyase, thiopeptidoglycan lyase

International Journal of Biological Macromolecules, 2011
A typical filamentous bacterium, Sphaerotilus natans, secretes a thiolic glycoconjugate which is assembled into a microtube, so called sheath. The glycoconjugate is known to consist of a pentasaccharide-dipeptide repeating unit, but its chemical structure has not been completely elucidated.
Keiko, Kondo   +8 more
openaire   +2 more sources

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