Institution
Novozymes
Company•Copenhagen, Denmark•
About: Novozymes is a company organization based out in Copenhagen, Denmark. It is known for research contribution in the topics: Nucleic acid & Polynucleotide. The organization has 2506 authors who have published 2828 publications receiving 89266 citations. The organization is also known as: Novo Enzymes A/S & Novozymes A/S.
Topics: Nucleic acid, Polynucleotide, Fermentation, Lipase, Cellulase
Papers published on a yearly basis
Papers
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07 Jul 1999TL;DR: In this paper, a process for preparing tobacco, which process comprises the steps of treating a tobacco material with a phenol oxidising enzyme, such as by extracting tobacco with a solvent to provide an extract and a residue; and treating the extract with an oxidizing enzyme such as a laccase.
Abstract: A process for preparing tobacco, which process comprises the steps of treating a tobacco material with a phenol oxidising enzyme, such as by extracting tobacco with a solvent to provide an extract and a residue; and treating the extract with a phenol oxidising enzyme such as a laccase. An improved tobacco product having a reduced amount of phenolic compounds. This is an alternative or a supplement to a process in which the phenolic compounds are adsorbed onto the insoluble carrier polyvinylpolypyrrolidone (PVPP). In preferred embodiments, the process includes further steps of removing the oxidised phenolic compound, adding adsorbents such as bentonite; removing and/or inactivating the enzyme; and concentrating the extract. Preferred phenol oxidising enzymes are peroxidases and laccases. The thus treated extract is advantageously re-combined with the tobacco residue and further processed to provide a tobacco article for smoking.
114 citations
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12 Oct 1999TL;DR: In this article, the reduction of allergenicity by N-glycosylation of proteins is discussed, and the present invention relates to the field of immunology, in particular allergicity.
Abstract: The present invention relates to the field of immunology, in particular allergenicity. More specifically it relates to the reduction of allergenicity by the in vivo N-glycosylation of proteins.
114 citations
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TL;DR: Five structures of wild-type and mutant forms of Cel6A from Humicola insolens in complex with nonhydrolyzable thio-oligosaccharides are presented, dissecting the structural accommodation of a processing substrate chain through the active center during hydrolysis.
113 citations
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TL;DR: Global gene expression patterns of Bacillus subtilis in response to subinhibitory concentrations of protein synthesis inhibitors (chloramphenicol, erythromycin, and gentamicin) were studied by DNA microarray analysis.
Abstract: Global gene expression patterns of Bacillus subtilis in response to subinhibitory concentrations of protein synthesis inhibitors (chloramphenicol, erythromycin, and gentamicin) were studied by DNA microarray analysis. B. subtilis cultures were treated with subinhibitory concentrations of protein synthesis inhibitors for 5, 15, 30, and 60 min, and transcriptional patterns were measured throughout the time course. Three major classes of genes were affected by the protein synthesis inhibitors: genes encoding transport/binding proteins, genes involved in protein synthesis, and genes involved in the metabolism of carbohydrates and related molecules. Similar expression patterns for a few classes of genes were observed due to treatment with chloramphenicol (0.4x MIC) or erythromycin (0.5x MIC), whereas expression patterns of gentamicin-treated cells were distinct. Expression of genes involved in metabolism of amino acids was altered by treatment with chloramphenicol and erythromycin but not by treatment with gentamicin. Heat shock genes were induced by gentamicin but repressed by chloramphenicol. Other genes induced by the protein synthesis inhibitors included the yheIH operon encoding ABC transporter-like proteins, with similarity to multidrug efflux proteins, and the ysbAB operon encoding homologs of LrgAB that function to inhibit cell wall cleavage (murein hydrolase activity) and convey penicillin tolerance in Staphylococcus aureus.
113 citations
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TL;DR: The immobilized enzyme was found to be stabilized compared to the free enzyme, and the performance of the biocatalyst was evaluated by the degradation of phenolic compounds including phenol, p-chlorophenol and catechol.
113 citations
Authors
Showing all 2507 results
Name | H-index | Papers | Citations |
---|---|---|---|
Jens Nielsen | 149 | 1752 | 104005 |
Gary K. Schoolnik | 81 | 233 | 27782 |
Lubbert Dijkhuizen | 75 | 424 | 21761 |
Bauke W. Dijkstra | 72 | 256 | 19487 |
Michel Vert | 69 | 333 | 17899 |
Henning Langberg | 60 | 242 | 11999 |
Harinderjit Gill | 59 | 319 | 12978 |
John M. Woodley | 58 | 420 | 13426 |
Lei Cai | 57 | 374 | 16689 |
Anette Müllertz | 57 | 274 | 10319 |
Peter J. Punt | 52 | 154 | 8846 |
Svein Jarle Horn | 51 | 123 | 9511 |
Martin Hofrichter | 50 | 158 | 7387 |
Eva Stoger | 49 | 127 | 8367 |
Luciano Saso | 45 | 325 | 7672 |