The Procter Gamble Company

Danisco US Inc.

Genencor International, Inc.

Hiroshi Oh

Andrew Shaw

David Aaron Estell

Eugene Steven Sadlowski

Ayrookaran J Poulose

Brian E Jones

Sang-Kyu Lee

Louise Wallace

Ronaldus W J Hommes

Steven Daryl Smith

William Michael Scheper

Vladimir Gartstein

Marc Kolkman

Chris Leeflang

Robb Richard Gardner

Wolfgang Aehle

Ronaldus Wilhelmus Joannes Hommes

Wilhelmus A H Van Der Kley

Leonardus P M Van Marrewijk

Mark Robert Sivik

Gregory Scot Miracle

Jeffrey John Scheibel

Richard Ray Bott

John Christian Haught

Gregory Marshall Whited

Michael Stanford Showell

Jeffrey Scott Dupont

Walter Weyler

Arseni Valerevich Radomyselski

Neelam S Amin

Sandra W Ramer

Victor Manuel Arredondo

Marc Eric Gustwiller

Klaus Liebeton

David Lee Daugherty

Edward M Concar

Dorothy A Hall

Matthew G Boston

Johan Smets

Faiz Feisal Sherman

Kenneth Nathan Price

Marguerite A Cervin

Nicholas David Vetter

Ming Tang

John August Wos

Charles Raymond Degenhardt

Pierre Daniel Verstraete

Qing Chen

William Richard Mueller

Matthew Grant Boston

Sergiy Minko

Jeffrey Jon Hopkins

Wilhelmus A H Van Der Kleij

Suxuan Gong

Timothy Bates

Mikhail Motornov

Robert Lupitskyy

Olivier Fasbender

Maguerite A Cervin

Leo Van Marrewijk

Lucia Mendez-Mata

Jeffrey John Hopkins

Tim Bates

Brian Edward Jones

Ronald Hommes

Mike Stanford Showell

Neelem S Amin

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained fromsp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from. In still further preferred embodiments, the neutral metalloprotease is a variant of theneutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the theneutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting.

Use and production of storage-stable neutral metalloprotease

A personal care composition comprises a personal care adjunct ingredient, an anti-dandruff agent, and cationic co-polymer disposed on an outer surface of the anti-dandruff agent. The cationic co-polymer has a viscosity of at least 0.09 poise and comprises monomers selected from the group consisting of acrylamide ('AAM'), dimethyl acrylamide ('DMAA'), acrylamidopropyl trimethylamonium chloride (&#x201c;APTAC&#x201d;), methacrylamidopropyl trimethylammonium chloride (&#x201c;MAPTAC&#x201d;), and combinations thereof.

Personal care compositions comprising anti-dandruff agents

A consumer product composition comprises a consumer product adjunct ingredient, a microcapsule, and deposition polymer disposed on an outer surface of the microcapsule. The deposition polymer has a Water Uptake Value (WUV) of at least about 2 grams per gram, as determined according to the WATER UPTAKE VALUE TEST METHOD. The microcapsule comprises a shell material encapsulating a core material, wherein the shell material comprises a polyacrylate and the core material comprises a benefit agent.

Consumer product compositions comprising microcapsules

The present invention relates to a method of making an amino silicone nanoemulsions. More specifically, the present invention relates to a method of making an amino silicone nanoemulsions that may be used to protect surfaces from being soiled or wetted.

Method of making an amino silicone nanoemulsion

The present invention relates to amino silicone nanoemulsions. More specifically, the present invention relates to amino silicone nanoemulsions that may be used to protect surfaces from being soiled or wetted.

Amino silicone nanoemulsion

A foam manipulation stabilizing composition for use in consumer products includes a plurality of surface-modified particles in combination with at least one surfactant. The particles have an average particle size greater than 100 nm up to about 50 &#x3bc;m and a hydrophobicity measured by a contact angle between about 20&#xb0; to 140&#xb0;. The ratio of particles-to-surfactant may be between about 1:20 to about 20:1. The surface modification may include grafting pH or temperature switching functional groups to the particles or to a composition, such as a polymer, coated on the particle. A method for reducing the level of foam in a rinse solution is also described.

Foam manipulation compositions containing fine particles

The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions for generation of peracids. The present invention finds particular use in applications involving cleaning, bleaching and disinfecting.

Perhydrolase

A cleaning composition may comprise a pH-switchable sudsing system and a cleansing system. The pH-switchable sudsing system may comprise a primary sudsing agent in combination with a pH-switchable co-surfactant. The pH-switchable co-surfactant is selected from diamine molecules having a general formula RR&#x2014;N&#x2014;R&#x2014;N(CH)X, where Ris a linear or branched Cto Chydrocarbyl, Ris a linear or branched Cto Chydrocarbyl, Ris a linear or branched Cto Chydrocarbylene, and X is a counteranion. The tertiary amine nitrogen of the pH-switchable co-surfactant has a pKvalue. When the tertiary amine nitrogen is unprotonated, the pH-switchable co-surfactant may provide a suds-boosting effect in washing solutions at a washing pH above the pK. When the tertiary amine nitrogen is protonated, the pH-switchable co-surfactant may provide a suds-reducing benefit in rinse waters at a rinse pH below the pK.

Cleaning compositions comprising pH-switchable amine surfactants

The present invention provides novel Micrococcineae spp serine proteases having multiple substitutions. In particular, the present invention provides serine proteases having multiple substitutions, DNA encoding these proteases, vectors comprising the DNA encoding the proteases, host cells transformed with the vector DNA, and enzymes produced by the host cells. The present invention also provides cleaning compositions (e.g., detergent compositions), animal feed compositions, and textile and leather processing compositions comprising these serine protease variants. In particularly preferred embodiments, the present invention provides mutant (i.e., variant) proteases derived from the wild-type proteases described herein. These variant proteases also find use in numerous applications.

Multiple mutation variants of serine protease

The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained fromsp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from. In still further preferred embodiments, the neutral metalloprotease is a variant of theneutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of theneutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting.

Thermostable neutral metalloproteases

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Cincinnati, OH, United States of America

Hiroshi Oh