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Institution

Novozymes

CompanyCopenhagen, 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.


Papers
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Patent
07 Jul 1999
TL;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

Patent
12 Oct 1999
TL;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

Journal ArticleDOI
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

Journal ArticleDOI
Janine T. Lin1, Mariah Connelly1, Chris Amolo1, Suzie Otani1, Debbie Yaver1 
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

Journal ArticleDOI
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

NameH-indexPapersCitations
Jens Nielsen1491752104005
Gary K. Schoolnik8123327782
Lubbert Dijkhuizen7542421761
Bauke W. Dijkstra7225619487
Michel Vert6933317899
Henning Langberg6024211999
Harinderjit Gill5931912978
John M. Woodley5842013426
Lei Cai5737416689
Anette Müllertz5727410319
Peter J. Punt521548846
Svein Jarle Horn511239511
Martin Hofrichter501587387
Eva Stoger491278367
Luciano Saso453257672
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20229
202181
202070
201998
2018102
2017135