Danisco US Inc.

Dupont Nutrition Biosciences Aps

International N&h Denmark Aps

Igor Nikolaev

Sander Van Stigt Thans

Bradley R Kelemen

Thijs Kaper

Slavko Kralj

Richard Ray Bott

Ronaldus Wilhelmus Hommes

Johannes Franciscus Thomas Van Lieshout

Wolfgang Aehle

Mats Sandgren

Frits Goedegebuur

Suzanne E Lantz

Piet Van Solingen

Gudrun Vogtentanz

David Aaron Estell

Benjamin S Bower

Martijn Scheffers

Casper Vroemen

Harm Jan Mulder

Louise Wallace

Shukun Yu

Jacob Flyvholm Cramer

Jayarama K Shetty

Huaming Wang

Karsten Matthias Kragh

Lilia Maria Babe

Charlotte Horsmans Poulsen

Sung Ho Lee

Jørn Dalgaard Mikkelsen

Rie Mejldal

Jahnavi Chandra Prasad

Ronaldus W J Hommes

Daniel Esteban Torres-Pazmino

Harm Mulder

Maria Foukaraki

Susan Arent Lund

Wilhelmus Van Der Kley

Rikke Hoeegh Lorentsen

Patrick Maria Franciscus Derkx

Paulien Kruithof

Jonathan Caspi

Rene Mikkelsen

Neville Marshall Fish

Peter Edvard Degn

Ronaldus Wilhelmus Joannes Hommes

Jonathan K Lassila

Jorn Dalgaard Mikkelsen

Bart C Koops

Sharief Barends

Jan Hendrik A Van Tuijl

Svend Haaning

Sina Pricelius

Robin Anton Sorg

Hye-Sook Kim

Jens Frisbaek Sorensen

Trine Christensen

Bert Koops

Johan Van Lieshout

Soren Dalsgaard

Wilhelmus Antonious Hendricus Van Der Kley

Suzy Breneman

Johan Franciscus Thomas Van Lieshout

Wilhelmus Van Der Kleij

Nicholai Douglas

Jan Hendrick A Van Tuijl

Karsten Mathias Kragh

Søren Dalsgaard

Engineered robust high Tm-phytase clade polypeptides and fragments thereof are described herein. Also described are methods of making such engineered robust high Tm-phytase clade and fragments thereof and use thereof in enhancing animal performance.

Engineered robust high Tm-phytase clade polypeptides and fragments thereof

The present invention relates to an isolated polypeptide having xylanase activity, selected from the group consisting of:

Polypeptide having xylanase activity

Disclosed are glycosyl hydrolase enzyme variants, particularly variants of certain oxidoreductases of glycosyl hydrolase family 61. Nucleic acids encoding the glycosyl hydrolyase variants, compositions including the glycosyl hydrolase variants, methods of producing the variants, and methods of using the variants are also described.

Variant enzymes

The present invention provides hemicellulytic enzyme variants. Specifically, the present invention provides xylanase variants having one or more modifications as compared to a parent xylanase enzyme resulting in at least one improved property. In addition, the present invention provides compositions comprising a xylanase variant of the invention. The present invention also provides methods of degrading hemicellulotic material, including arabino-xylan using compositions comprising a xylanase variant of the invention.

Composition and methods comprising a xylanase enzyme variant

A GH10 xylanase variant is disclosed herein. This GH10 xylanase variant has increased thermostability compared with a parent GH10 xylanase enzyme comprising at least 90% sequence identity with the amino acid sequence of SEQ ID No. 1 wherein the variant has been modified at two or more of the following positions 7, 33, 79, 217 and 298 corresponding to the amino acid numbering of SEQ ID No. 1.

GH10 family xylanase

Variant Enzymes

Disclosed are a number of homologs and variants ofCe17A (formerlycellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

The present invention relates to polypeptides having glucoamylase activity with improved properties and to compositions comprising these polypeptides suitable for use in the production of a food, beverage (e.g. beer), feed, or biofuel. Also described is an improved and cost-effective process for isolating glucoamylases suitable for large scale protein purification procedures. Furthermore, different methods and uses related to glucoamylases according to the invention are disclosed, such as in a brewing process.

Polypeptides having glucoamylase activity and method of producing the same

The present disclosure relates to cellulase variants. In particular the present disclosure relates to cellulase variants having improved expression, activity and/or stability. Also described are nucleic acids encoding the cellulase variants, compositions comprising the cellulase variants, and methods of use thereof.

Cellulase variants with improved expression, activity and stability, and use thereof

The present disclosure is generally directed to enzymes and in particular beta-glucosidase variants. Also described are nucleic acids encoding beta-glucosidase variants, compositions comprising beta-glucosidase variants, methods of using beta-glucosidase variants, and methods of identifying additional useful beta-glucosidase variants.

Beta-glucosidase I variants with improved properties

The present invention relates to amidase enzymes and a feed or food additive comprising the amidase enzyme capable of degrading ochratoxin.

Food additive comprising an amidase for detoxifying ochratoxin

A method of oxidizing a saccharide, by contacting the saccharide with an alcohol dehydrogenase (ADH) enzyme selected from a quinone redox cofactor-dependent ADH, a nicotinamide adenine dinucleotide (NAD) redox cofactor-dependent ADH, a nicotinamide adenine dinucleotide phosphate (NADP) redox cofactor-dependent ADH, and any combination thereof is described. An oxidized saccharide obtainable by the method and products, in particular food products and paper products, containing the oxidized saccharide, are also described.

Oxidation process

An amino acid sequence is described. The amino acid may comprise a signal sequence that is SEQ ID NO. 1a (or a variant or homologue or derivative or fragment thereof) that is expressed as a fusion protein that comprises a protein of interest. The signal sequence directs secretion of the protein of interest. The protein of interest may be a heterologous protein. Secretion of the fusion protein aids purification.

Proteins

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Noordwijk, Netherlands

Igor Nikolaev