Topic
Xylanase
About: Xylanase is a research topic. Over the lifetime, 7099 publications have been published within this topic receiving 163793 citations.
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TL;DR: Ten Ascomycetes, seven Fungi Imperfecti and one Oomycete known to occur on submerged wood were tested for their ability to produce amylase, xylanase, cellulases, lipase, polygalacturonase, pectin lyase, protease, chitinase, and polyphenol oxidases, and to form soft-rot cavities on balsa, green ash, and cottonwood.
Abstract: Ten Ascomycetes, seven Fungi Imperfecti and one Oomycete known to occur on submerged wood were tested for their ability to produce amylase, xylanase, cellulases, lipase, polygalacturonase, pectin lyase, protease, chitinase, and polyphenol oxidases. Species were also tested for their ability to degrade lignosols, with and without wood sugars, and indulin, and to form soft-rot cavities on balsa, green ash, and cottonwood. With the exception of Pythium sp., species were generalists with respect to hydrolytic enzymes and could degrade a wide range of substrates. All species produced weak or negative reactions on media containing chitin and lignin derivatives. Although Nectria haematococca, N. lucidum and Heliscus lugdunensis produced strong to moderate positive reactions on xylan, carboxymethylcellulose and Walseth cellulose, they did not form soft-rot cavities. All other species except Pythium sp. produced typical soft-rot cavities.
53 citations
TL;DR: Both enzymes enhanced brightness while reducing chemical demand, but xyl 3 was more effective; Synergism was noted in the prebleaching of softwood but not hardwood pulp, and the presence of pulp increased thermal stability.
53 citations
TL;DR: The enzymatic properties, the participation in hydrolysis of cellooligosaccharides, and the synergism with xylanase make RuBG3A and Ru BG3B very interesting candidates for saccharification of both cellulose and hemicellulose.
Abstract: Two β-glucosidase/xylosidase genes, Rubg3A and Rubg3B, were cloned from yak rumen uncultured microorganisms by metagenome method and function-based screening. Recombinant RuBG3A and RuBG3B purified from Escherichia coli were characterized for enzymatic properties, and they exhibited activity against 4-nitrophenyl-β-d-glucopyranoside and 4-nitrophenyl-β-d-xylopyranoside, suggesting bifunctional β-glucosidase/xylosidase activity. Chromatography analysis showed that they could effectively hydrolyze cellooligosaccharide substrates, indicating the facilitation in saccharification of cellulose. RuBG3A and RuBG3B can also increase the reducing sugar released in xylan hydrolysis to 218% and 169%, respectively, through synergism with xylanase, suggesting their application in hemicellulose saccharification. Molecular modeling and substrate docking showed that there should be one active center responsible for the bifunctional activity in each enzyme, since the active site pocket is substantially wide to allow the entry of both β-glucosidic or β-xylosidic substrates, which elucidated the structure–function relationship in substrate specificities. Therefore, the enzymatic properties, the participation in hydrolysis of cellooligosaccharides, and the synergism with xylanase make RuBG3A and RuBG3B very interesting candidates for saccharification of both cellulose and hemicellulose.
53 citations
TL;DR: The xylanase exhibited direct brightening abilities on bagasse pulp improving brightness by 1.5 points, however, kappa number decreased, indicating the high enzyme efficiency at low doses.
53 citations
TL;DR: An efficient and simple modified method of electroelution is described that can be used as a time-saving method for eluting multiple protein bands and provided that the proteins are highly expressed, they can be purified rapidly and without requiring any prior knowledge of the protein characteristics.
53 citations