Novozymes

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.

Methods for producing fermentation products

Abstract: The invention relates to methods for treating pre-treated lignocellulose-containing material comprising the steps of: a) subjecting a slurry comprising pre-treated lignocellulose-containing material to agitation in the presence of one or more chemicals and/or one or more enzymes; b) subjecting said slurry to liquid-solid separation; c) recycling at least a portion of the liquid to the agitated slurry; d) optionally transferring solids-containing material for downstream processing.

Method for enzymatic treatment of wool

Abstract: A method of producing wool or animal hair material with improved properties such as shrink-proofed (anti-felting tendency), increased whiteness, improved dyeability, increased softness and/or reduced pilling tendency, the method comprising the steps of treating wool, wool fibres or animal hair material in a process selected from the group consisting of plasma treatment processes and the Delhey process, and subjecting the wool or animal hair material to a treatment with a proteolytic enzyme (a protease), preferably a serine protease, more preferably a subtilisin, in an amount effective for improving the properties.

Structural Basis for Substrate Recognition by Erwinia Chrysanthemi Gh30 Glucuronoxylanase.

Abstract: Xylanase A from the phytopathogenic bacterium Erwinia chrysanthemi is classified as a glycoside hydrolase family 30 enzyme (previously in family 5) and is specialized for degradation of glucuronoxylan. The recombinant enzyme was crystallized with the aldotetraouronic acid β-d-xylopyranosyl-(14)-[4-O-methyl-α-d-glucuronosyl-(12)]-β-d-xylopyranosyl-(14)-d-xylose as a ligand. The crystal structure of the enzyme–ligand complex was solved at 1.39 A resolution. The ligand xylotriose moiety occupies subsites −1, −2 and −3, whereas the methyl glucuronic acid residue attached to the middle xylopyranosyl residue of xylotriose is bound to the enzyme through hydrogen bonds to five amino acids and by the ionic interaction of the methyl glucuronic acid carboxylate with the positively charged guanidinium group of Arg293. The interaction of the enzyme with the methyl glucuronic acid residue appears to be indispensable for proper distortion of the xylan chain and its effective hydrolysis. Such a distortion does not occur with linear β-1,4-xylooligosaccharides, which are hydrolyzed by the enzyme at a negligible rate. Database Structural and experimental data are available in the Protein Data Bank database under accession number 2y24 [45].

Chemical respiratory allergy: opportunities for hazard identification and characterisation. The report and recommendations of ECVAM workshop 60.

Abstract: Kimber, Ian Agius, Raymond Basketter, David A Corsini, Emanuela Cullinan, Paul Dearman, Rebecca J Gimenez-Arnau, Elena Greenwell, Leona Hartung, Thomas Kuper, Frieke Maestrelli, Piero Roggen, Erwin Rovida, Costanza European Centre for the Validation of Alternative Methods Consensus Development Conference England Alternatives to laboratory animals : ATLA Altern Lab Anim. 2007 May;35(2):243-65.