Results 191 to 200 of about 8,211 (214)
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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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Analysis of Glycosaminoglycans with Polysaccharide Lyases
Current Protocols in Molecular Biology, 1999Polysaccharide 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.
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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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Structural analyses of ‘substrate-pH of activity’ pairing observed in Polysaccharide lyases
2023AbstractAnionic polysaccharides found in nature are functionally and structurally diverse, and so are the polysaccharide lyases (PLs) which catalyse their degradation. Atomic superposition of various PL folds according to their cleavable substrate structure confirm the occurrence of structural convergence at PL active sites.
Shubhant Pandey +2 more
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Structural Determinants Responsible for Substrate Recognition and Mode of Action in Family 11 Polysaccharide Lyases [PDF]
Journal of Biological Chemistry, 2009 A saprophytic Bacillus subtilis secretes two types of rhamnogalacturonan (RG) lyases, endotype YesW and exotype YesX, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 YesW and YesX with a significant sequence identity (67.8%) cleave glycoside bonds between rhamnose ...
Bunzo Mikami, Wataru Hashimoto
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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
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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
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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
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Molecular Biotechnology, 2016
A thermostable, alkaline rhamnogalacturonan lyase (RG lyase) CtRGLf, of family 11 polysaccharide lyase from Clostridium thermocellum was cloned, expressed, purified and biochemically characterised. Both, the full-length CtRGLf (80 kDa) protein and its truncated derivative CtRGL (63.9 kDa) were expressed as soluble proteins and displayed maximum ...
Arun, Dhillon +7 more
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A thermostable, alkaline rhamnogalacturonan lyase (RG lyase) CtRGLf, of family 11 polysaccharide lyase from Clostridium thermocellum was cloned, expressed, purified and biochemically characterised. Both, the full-length CtRGLf (80 kDa) protein and its truncated derivative CtRGL (63.9 kDa) were expressed as soluble proteins and displayed maximum ...
Arun, Dhillon +7 more
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