Results 21 to 30 of about 4,548 (168)
Molecular Plant-Microbe Interactions, 2001 The ability of the enterobacterium Erwinia chrysanthemi to induce pathogenesis in plant tissue is strongly related to the massive production of plant-cell-wall-degrading enzymes (pectinases, cellulases, and proteases).
William Nasser +3 more
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Allergies, 2022 Pectate-lyase allergens, the group 1 of allergens from Cupressaceae pollen, consist of glycoproteins exhibiting an extremely well-conserved three-dimensional structure and sequential IgE-binding epitopes.
Annick Barre +5 more
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Evaluation of the potential of free and immobilized thermophilic bacterial enzymes in the degradation of agro-industrial wastes [PDF]
Archives of Biological Sciences, 2015 Agro-industrial wastes are potential starting materials for the production of useful value-added compounds, including prebiotic oligosaccharides. In this paper, we evaluated the potential of thermophilic bacterial pectin- and xylan-degrading ...
Kieraite Ieva +3 more
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Identification and Characterisation of a Pectinolytic Enzyme from Paenibacillus xylanolyticus
BioResources, 2014 Pectinolytic enzymes play an important role in the processing of lignocellulosic materials because of their ability to improve the access of cellulases to their substrate by removing pectins. The strain Paenibacillus xylanolyticus 2-6L3 was isolated from
Simona Giacobbe +5 more
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Structure of pectate lyase A: comparison to other isoforms [PDF]
Acta Crystallographica Section D Biological Crystallography, 2002 Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E.
Thomas, Leonard M. +3 more
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Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin [PDF]
Microbiology, 1995 Phytopathogenic Erwinia bacteria cause tissue maceration by secretion of pectinolytic enzymes such as pectate lyase (PL). Sequencing of overlapping genomic fragments from Erwinia carotovora subsp. atroseptica established the organization of a 7.5 kbp region encoding PL isoenzymes.
S, Bartling, C, Wegener, O, Olsen
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Molecular Plant-Microbe Interactions, 2002 Root-knot nematodes (Meloidogyne javanica) are obligate sedentary endoparasites that must penetrate the host root to initiate their life cycle. Many enzymes are secreted by the nematode to facilitate host penetration; required enzymes may include pectate
Elizabeth A. Doyle, Kris N. Lambert
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Abundance and genetic diversity of microbial polygalacturonase and pectate lyase in the sheep rumen ecosystem. [PDF]
PLoS ONE, 2012 Efficient degradation of pectin in the rumen is necessary for plant-based feed utilization. The objective of this study was to characterize the diversity, abundance, and functions of pectinases from microorganisms in the sheep rumen.A total of 103 unique
Peng Yuan +8 more
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Molecular Plant-Microbe Interactions, 2001 Colletotrichum gloeosporioides is an important pathogen of tropical and subtropical fruits. The C. gloeosporioides pelB gene was disrupted in the fungus via homologous recombination. Three independent isolates, GD-14, GD-23, and GD-29, did not produce or
Nir Yakoby +5 more
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Molecular Plant-Microbe Interactions, 2007 Pseudomonas viridiflava is a common pathogen of Arabidopsis thaliana in wild populations, yet very little is known about mechanisms of resistance and virulence in this interaction. We examined the induced defense response of A.
Katrin Jakob +2 more
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