Results 201 to 210 of about 225,549 (221)
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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 +3 more
semanticscholar +3 more sources
Action pattern of polysaccharide lyases on glycosaminoglycans.
Glycobiology, 1994The 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. Jandik, K. Gu, R. Linhardt
semanticscholar +3 more sources
Improvement of expression level of polysaccharide lyases with new tag GAPDH in E. coli.
Journal of Biotechnology, 2016Escherichia coli (E. coli) is widely used to express a variety of heterologous proteins. Efforts have been made to enhance the expression level of the desired protein. However, problems still exist to regulate the level of protein expression and therefore, new strategies are needed to overcome those issues.
Zhenya Chen +3 more
semanticscholar +3 more sources
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
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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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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The first structure of pectate lyase belonging to polysaccharide lyase family 3
Acta Crystallographica Section D Biological Crystallography, 2001The 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
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Direct Influence of the Conserved Motif in PL7 Family Alginate Lyases on Enzyme Cold Adaptability.
Journal of Agricultural and Food ChemistryAlginate lyase, a vital component of polysaccharide lyases, is instrumental in the efficient degradation of alginate and the production of single oligosaccharides. Although numerous alginate lyases have been characterized, only a few display extreme cold
Zhixiao He +8 more
semanticscholar +1 more source
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
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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
Archives of Biochemistry and Biophysics, 2004
Cells of Bacillus sp. GL1 extracellularly secrete a gellan lyase with a molecular mass of 130 kDa responsible for the depolymerization of a heteropolysaccharide (gellan), although the gene is capable of encoding a huge protein with a molecular mass of 263 kDa.
Osamu, Miyake +5 more
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Cells of Bacillus sp. GL1 extracellularly secrete a gellan lyase with a molecular mass of 130 kDa responsible for the depolymerization of a heteropolysaccharide (gellan), although the gene is capable of encoding a huge protein with a molecular mass of 263 kDa.
Osamu, Miyake +5 more
openaire +2 more sources

