Genencor International, Inc.

Danisco US Inc.

Other

Genencor, Inc.

Genimmune N.v.

The Clorox Company

Genecor International, Inc.

Epimmune Inc.

Danisco US Inc., Genencor Division

Scott Douglas Power

David Aaron Estell

Brian Frederick Schmidt

James A Wells

Andrew Shaw

Katherine D Collier

Sandra W Ramer

Richard Ray Bott

Melodie Estabrook

Gudrun Vogtentanz

Robert Mark Caldwell

Brian C Cunningham

Hans De Nobel

Neelam S Amin

Frits Goedegebuur

Anthony G Day

Marc Kolkman

Huaming Wang

Anita Van Kimmenade

William Albert Cuevas

Sang-Kyu Lee

Louise Wallace

Michael C Ward

Colin Mitchinson

Kathleen A Clarkson

Luis Gustavo Cascao-Pereira

Christopher James Murray

Wei Liu

Clement K Choy

Brian E Jones

Ayrookaran J Poulose

Michael D Ward

Benjamin S Bower

Alessandro D Sette

Walter Weyler

Daniel G Yansura

Lilia Maria Babe

Thomas P Graycar

Michael Jay Pepsin

Chris Leeflang

Robert W Chesnut

Jayarama K Shetty

James T Kellis, Jr

Marguerite A Cervin

Karsten Matthias Kragh

Fiona A Harding

Bryan P Fox

Carol A Requadt

Amr R Toppozada

Christopher Charles Barnett

Jeffrey V Miller

Grant C Ganshaw

Mark Joseph Newman

Yiyou Chen

Brian D Livingston

Deborah S Winetzky

Claudine Chang

Robin M Adams

Regina Chin

Gregory L Gray

David Brian Powers

Mansi Goyal

Victoria E Huang

Lawrence M Deyoung

Manley T F Huang

Eugenio Ferrari

Vivek Sharma

Casper Vroemen

Richard J Wiersema

Anna G Stanislowski

Donald E Ward

Leif P Solheim

Mee-Young Yoon

Casper Willem Vroemen

Bradley A Paulson

David E Estell

Ayrookaram J Poulose

Casper Vroeman

Doreen Victoria

Johanna M Van Kimmenade

Louann Carlomagno

Raj Lad

Gudrun Vogentanz

Marc Kolkmam

Karsten Kraugh

Luis G Cascāo-Pereira

Beverley Rider Turnquest

Victoria Huang

Bradley Alan Paulson

William A Cuevas

James T Kellis

Bradley Paulson

Karsten M Kragh

Hybrid alpha-amylases are provided that share a conserved 3D structure in whole or in part with a wild-type Termamyl-like &#x3b1;-amylase, e.g., aamylase. In the hybrid, an N-terminal portion of a Termamyl-like &#x3b1;-amylase is replaced with sequences from an archae &#x3b1;-amylase. The sequence similarity between the two amylase sequences may be less than 60%. Conserving the wild-type 3D structure in the hybrid facilitates obtaining enzymatically active amylases. In one embodiment, one or both amylase sequences contribute residues to the B domain, resulting in particularly advantageous properties. For instance, replacement of the Cabinding site in the B domain of the Termamyl-like &#x3b1;-amylase with a B domain sequence of an archae &#x3b1;-amylase that does not bind Cacan produce a hybrid that is fully active in the absence of Ca.

Hybrid alpha-amylases

Chimeric alpha-amylases having the characteristics of high thermostability and good performance in starch degradation, especially high-temperature liquefaction processes, are provided. The alpha-amylases are chimeras of AmyL and AmyS enzymes, and are useful in starch degradation processes. Methods of making the chimeric enzymes, and methods of using the chimeric alpha-amylases for liquefaction, cleaning starch residue from a surface, and treating woven material to remove coatings. Kits for practicing the methods are provided. Polynucleotides encoding the chimeric amylases, vectors, and expression hosts also are provided.

Chimeric alpha-amylase variants

Alpha-amylases from(AmyE), variants thereof, nucleic acids encoding the same, and host cells comprising the nucleic acids are provided. Methods of using AmyE or variants thereof are disclosed, including liquefaction and/or saccharification of starch. Such methods may yield sugars useful for ethanol production or high fructose corn syrup production. In some cases, the amylases can be used at low pH, in the absence of calcium, and/or in the absence of a glucoamylase.

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The present invention provides peptides and supported peptides for treating various diseases and conditions. In particularly preferred embodiments, the present invention provides compositions and methods for personal care. In some embodiments the present invention provides compositions for use in skin and/or hair care, as well as cosmetic compositions. IN alternative particularly preferred embodiments, the present invention provides peptides and supported peptides for treating diseases of the skin, such as rosacea. In some particularly preferred embodiments, the supported peptides of the present invention are anti-VEGF peptides. In alternative particularly preferred embodiments, the anti-VEGF peptides are expressed on a scaffold protein. In some most preferred embodiments, the scaffold protein comprises BBI.

Peptide personal care compositions and methods for their use

An &#x3b1;-amylase from(AmyE) produces significant amounts of glucose from various carbohydrate substrates, including vegetable starch, maltoheptaose, and maltotriose. Among other things, this advantageous property allows AmyE or variants thereof to be used in a saccharification reaction having a reduced or eliminated requirement for glucoamylase. The reduction or elimination of the glucoamylase requirement significantly improves the efficiency of the production of ethanol or high fructose corn syrup, for example.

The present invention relates to modified variant Bowman Birk Protease Inhibitor proteins (BBPIs) that comprise peptides that bind target proteins, and that are further modified to have greater protease inhibitory activity and/or be produced at greater yields than the unmodified BBPIs. The invention encompasses polynucleotide constructs and expression vectors containing polynucleotide sequences that encode the modified variant BBPIs, the transformed host cells that express and produce the modified variant BBPIs, the modified variant BBPI proteins, the compositions comprising the modified variant BBPIs, and the methods for making and using the modified variant BBPIs in personal care.

Modified variant Bowman Birk protease inhibitors

Hybrid alpha-amylases are provided that share a conserved 3D structure in whole or in part with a wild-type Termamyl-like ?-amylase, e.g., aamylase. In the hybrid, an N terminal portion of a Termamyl-like ?-amylase is replaced with sequences from an archae ? amylase. The sequence similarity between the two amylase sequences may be less than 60%. Conserving the wild-type 3D structure in the hybrid facilitates obtaining enzymatically active amylases. In one embodiment, one or both amylase sequences contribute residues to the B domain, resulting in particularly advantageous properties. For instance, replacement of the Ca2+ binding site in the B domain of the Termamyl-like ?-amylase with a B domain sequence of an archae ? amylase that does not bind Ca2+ can produce a hybrid that is fully active in the absence of Ca2+.

The present invention relates to cells that have been genetically manipulated to have an altered capacity to express and/or produce proteins of interest. In particular, the present invention relates to modified host cells of Gram-positive microorganisms, such asspecies that are capable of overexpressing ymaH. The invention encompasses polynucleotide constructs and expression vectors containing polynucleotide sequences that encode YmaH, and the modified host cells comprising them. In particular, the present invention relates to compositions and methods of overexpressing YmaH for enhancing the expression and production of proteins of interest (e.g., proteases) inspecies.

Variants ofsp. TS-23 strain alpha-amylases exhibit improved enzymatic performance, including increased thermostability, reduced calcium dependence, increased washing/cleaning performance, and baking ability. Compositions comprising these variants are useful in methods of starch processing, starch liquefaction, fermatation, starch saccharification, cleaning, laundrying, textile desizing, baking, and biofilm removal.

Modified variant Bowman Birk Protease Inhibitors

Disclosed are compositions comprising variants of alpha-amylase that have alpha-amylase activity and which exhibit altered properties relative to a parent AmyS-like alpha-amylase from which they are derived. The compositions comprise an additional enzyme such as a phytase. Also disclosed are methods of using the compositions, and kits related thereto.

Alpha-amylase variants with altered properties

Variants ofsp. TS-23 strain alpha-amylases exhibit improved enzymatic performance, including increased themostability, reduced calcium dependence, increased washing/cleaning performance, and baking ability. Compositions comprising these variants are useful in methods of starch processing, starch liquefaction, fermatation, starch saccharification, cleaning, laundrying, textile desizing, baking, and biofilm removal.

Described herein are methods for the production of monoclonal antibodies in filamentous fungi host cells. The monoclonal antibodies are expressed as full-length fusion proteins that retain functional antigen binding and antibody-dependent cellular cytotoxicity capabilities. Improvements in the cleavage of the glucoamylase-light chain fusion protein to yield a mature antibody are also provided. The antibodies produced in filamentous fungi show equivalent pharmacokinetic disposition to antibodies produced in mammalian cells.

Production of functional antibodies in filamentous fungi

Growing community of inventors

San Bruno, CA, United States of America

Scott Douglas Power