Results 151 to 160 of about 6,770 (172)
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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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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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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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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
2023Abstract Anionic 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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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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Applied Biochemistry and Biotechnology, 2013
Polysaccharide lyases (PLs) are enzymes that cleave glycosidic linkages in hexuronate polysaccharides, such as homogalacturonan (HG), using a β-elimination mechanism. Traditionally, PL activities on HG have been associated with catalytic calcium cofactors, unusually high pH optima, and arginine Brønstead bases.
D Wade, Abbott +3 more
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Polysaccharide lyases (PLs) are enzymes that cleave glycosidic linkages in hexuronate polysaccharides, such as homogalacturonan (HG), using a β-elimination mechanism. Traditionally, PL activities on HG have been associated with catalytic calcium cofactors, unusually high pH optima, and arginine Brønstead bases.
D Wade, Abbott +3 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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Polyuronic acid degradation by polysaccharide lyase family 7
Acta Crystallographica Section A Foundations and Advances, 2022M. Vuillemin +12 more
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Bioprocess and Biosystems Engineering
Enhancing the stability and the reusability of ulva polysaccharide lyase (UPL) is crucial for the efficient production of reducing sugars from ulva polysaccharides, which are vital for their broad applications in functional foods. In this study, we innovatively developed a self-immobilized UPL by fusing the enzyme with ferritin, leading to the ...
Qing, Yang +11 more
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Enhancing the stability and the reusability of ulva polysaccharide lyase (UPL) is crucial for the efficient production of reducing sugars from ulva polysaccharides, which are vital for their broad applications in functional foods. In this study, we innovatively developed a self-immobilized UPL by fusing the enzyme with ferritin, leading to the ...
Qing, Yang +11 more
openaire +2 more sources