Unilever Patent Holdings B.v.

Lever Brothers Company, Division of Conopco, Inc.

Bac IP B.v.

Conopco, Inc.

Lever Brothers Company

Internationale Octrooi Maatschappij 'octropa' Bv

Unilever Home and Personal Care Usa, Division of Conopco, Inc.

Van Den Bergh Foods Co., Division of Conopco, Inc.

Internationale Otrool Maatschappij 'octropa' B.v.

Cornelis T Verrips

Adrianus M Ledeboer

Jan Maat

Daniel Convents

Leon Gerardus Frenken

Luppo Edens

Christiaan Visser

Leon Gerardus Joseph Frenken

Ton Swarthoff

Raymond Hamers

John D Marugg

Johannes M Verbakel

Cornelis P Hollenberg

Zbigniew A Janowicz

Sandra Bezemer

Holger York Toschka

Roelf J Planta

Maria T Lopes

Marco F Giuseppin

Cecile Hamers-Casterman

Leo G Frenken

Leon G J Frenken

Michael M Harmsen

Jannetje Wilhelmina Bos

Richard H Van Der Linden

Franciscus Maria Klis

Ronald Hage

Paul James Davis

Charles Craig Nunn

Cornelis Johannes Leenhouts

Steven Howell

Neil James Parry

Maarten Robert Egmond

Amir Maximiliaan Batenburg

Bernard Lucas Feringa

Rudolf J Martens

Walter M Verhue

Mark John Berry

Johannes A Van Den Berg

Rudolf Willem Van Drunen

Johannes Joseph Wilhelmus De Haard

Pieter De Geus

Monique Van Der Heiden

Marcel Van Der Helm

Serge Vm Muyldermans

Annelies Smits

Dirk Herman Hondmann

Johannes Gerardhus Roelfes

Serge V M Muyldermans

Maarten P Schreuder

Johannes Joseph Wilhelmus deHaard

Robert Klok

Richard Hendricus Jacobus Van Der Linden

Michael Marie Harmsen

Maria Y Toonen

Thomas Stewart Beggs

Marco L Giuseppin

Todd Domke

Leon Gerardus J Frenken

Gerard Tuynenburg Muys

Roger Theophile Sylvain Van Gorp

Renee Van Rhee

Pim Unilever Research Vlaardingen Hermans

J J W Unilever Research Vlaardingen De Haard

Ilse Unilever Research Vlaardingen Landa

The use of VHHs in the preparation of products to provide stability of antibody specificity under destabilizing conditions whereby normally lower eukaryotes or traditional antibodies are killed or inactivated.

Products comprising inactivated yeasts or moulds and active VHH-type antibodies

A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an example DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin of Camelidae and is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the generaor, or a yeast, preferably belonging to the yeast genera, or. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody ex Camelidae can be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised in Camelidae against transition state molecules. The functionalized antibody or fragment thereof can comprise a fusion protein of both a heavy chain immunoglobulin from Camelidae or a fragment thereof and another polypeptide, e.g., an enzyme, preferably an oxido-reductase. Also provided are new products obtainable by a process as described, and compositions containing a product produced by a process as described, which composition may contain a new product as provided.

Prosuction of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae

A method of inhibiting viral infection using a monovalent antigen binding protein comprising a single domain binding unit capable of binding to a virus is described. Preferably the protein is a heavy chain variable domain derived from an immunoglobulin naturally devoid of light chains. Food, pharmaceutical and cosmetic products comprising such proteins are also described together with a method for selecting inhibiting proteins from a large population of mainly containing non-inhibiting, but infectious agent binding fragments.

Inhibition of viral infection using antigen-binding proteins

A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an expressible DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin ofand is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the generaoror a yeast, preferably belonging to the yeast genera. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody excan be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised inagainst transition state molecules. The functionalized antibody or fragment thereof can comprise a fusion protein of both heavy chain immunoglobulin fromor a fragment thereof and another polypeptide, e.g., an enzyme, preferably an oxido-reductase. Also provided are new products obtainable by a process as described, and compositions containing a product produced by a process as described, which composition may contain a new product as provided.

Production of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae

There is provided a targeted bleaching composition comprising an organic substance which forms a complex with a transition metal, the complex catalyzing bleaching of a substrate by a precursor selected from atmospheric oxygen and/or a peroxyl species. The complex is bound to a recognizing portion having a high binding affinity for stains present on fabrics.

Targeted moieties for use in bleach catalysts

New products are provided comprising inactivated lower eukaryotic cells, preferably yeasts or molds, having at the outer surface functionally active antibodies or functionally active fragments thereof. Preferred antibody fragments are the variable domains of Camelidae heavy chain antibodies, which are surprisingly stable against physical and chemical decontamination regimes and do not loose their activity when they are immobilized on the glucan layer of the cell wall which is present in a variety of lower eukaryotes. The new products are preferably in the field of food products, personal care products, and animal feed products.

Products comprising inactivated yeasts or moulds provided with active antibodies

There is provided a detergent composition comprising one or more surfactants and a compound capable of binding to colored substances which may occur as stains on fabrics.

Detergent compositions

There is provided a bleaching enzyme capable of generating a bleaching chemical and having a high binding affinity for stains present on fabrics. Furthermore, there is provided an enzymatic bleaching composition comprising the bleaching enzyme and a surfactant and a process for bleaching stains present of fabrics.

Bleaching enzymes

There is provided a detergent composition comprising one or more surfactants and a compound capable of binding to coloured substances which may occur as stains on fabrics.

Immobilized proteins with specific binding capacities and their use in

There is provided an enzymatic bleach composition comprising one or more surfactants and an enzyme of extracellular origin, capable of oxidizing substrates by the build-in of one or more oxygen atoms into the substrate using molecular oxygen, in particular a dioxygenase from extracellular origin, and a process for bleaching stains present on fabrics comprising treating the stained fabrics with said composition.

Enzymatic bleach composition

A process is disclosed for preparing a protein by a eukaryote transformed by multicopy integration of an expression vector into the genome of a yeast, such as Saccharomyces, Hansenula, and Kluyveromyces, or of a mould such as Aspergillus, Rbizopus and Trichoderma, the expression vector containing both an 'expressible gene' encoding the protein and a so-called 'deficient selection marker meeded for the growth of the yeast or mould in a specific medium', such as the LEU2d, TRP1d or URA3d gene, in combination witha ribosomal DNA sequence, resulting in stable high copy integration of 100-300 copies per cell. This multicopy integration results in an increased production of the desired protein, which can be guar .alpha.-galactosidase, an oxidase or a hydrolytic enzyme such as a lipase.

Process for preparing a protein by a fungus transformed by multicopy

There is provided an enzymatic oxidation process wherein a substance which is to be oxidised is reacted with (a) an enzyme exhibiting peroxidase activity and a source of hydrogen peroxide or an enzyme exhibiting oxidase activity on phenolic compounds and (b) a compound which enhances the oxidation activity of the enzyme, characterized in that the compound specifically binds the substance which is to be oxidized. Furthermore, there is provided an enzymatic stain bleaching or anti dye-transfer composition comprising: (a) an enzyme exhibiting peroxidase activity and a source of hydrogen peroxide or an enzyme exhibiting oxidase activity on phenolic compounds and (b) a compound which enhances the oxidation activity of the enzyme and which is capable of binding selectively to a stain chromophore or textile dye in solution.

Enzymatic oxidation process

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Maassluis, Netherlands

Cornelis T Verrips