Abstract: Compositions comprising cellulase and at least one poly alpha-1,3-glucan ether compound having a degree of substitution with a positively charged organic group of about 0.05-3.0 are disclosed. Such compositions can be dry or aqueous, the latter of which can have a viscosity of at least about 10 cPs. The disclosed composition can be in the form of a personal care product, household product, or industrial product, for example. Also disclosed are a method for preparing an aqueous composition comprising cellulase and a poly alpha-1,3-glucan ether compound, and a method of treating a material such as fabric by contacting it with this aqueous composition.

Abstract: Compositions comprising cellulase and at least one poly alpha-1,3-glucan ether compound having a degree of substitution with a positively charged organic group of about 0.05-3.0 are disclosed. Such compositions can be dry or aqueous, the latter of which can have a viscosity of at least about 10 cPs. The disclosed composition can be in the form of a personal care product, household product, or industrial product, for example. Also disclosed are a method for preparing an aqueous composition comprising cellulase and a poly alpha-1,3-glucan ether compound, and a method of treating a material such as fabric by contacting it with this aqueous composition.

Abstract: The present invention provides a Bacillus sp. subtilisin variant. In addition, the present invention provides compositions comprising this serine protease variant. In some embodiments, the present invention provides laundry and other non-automatic (i.e., hand) dishwashing cleaning compositions comprising this serine protease variant.

Abstract: The present invention provides protease compositions particularly suited for dishwashing applications.

Abstract: 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.

Abstract: The present invention provides methods and compositions for dynamic pH control, particularly in detergent applications. In particularly preferred embodiments, the detergent compositions find use in surface removal of soils from fabrics, including clothing. In some particularly preferred embodiments, the present invention provides combinations of enzymes to provide for dynamic pH control.

Abstract: The present invention provides methods and compositions for the stabilization of oxidase enzymes during storage. In some preferred embodiments, the oxidase is a component of liquid detergent compositions. In some particularly preferred embodiments, the oxidase is stabilized by the addition of a reversible inhibitor of the oxidase to a liquid detergent. In some particularly preferred embodiments, the oxidase is stabilized with bisulfite. In further preferred embodiments, the use of a reversible inhibitor also prevents premature generation of peroxide during storage of liquid detergent. In additional embodiments, liquid detergent formulations comprised of oxidase enzyme, its substrate, and its reversible inhibitor produce active oxygen species (peroxide) upon dilution of the liquid detergent in laundry wash liquor.

Abstract: The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some embodiments, the present invention provides methods and compositions for generation of long chain peracids. Certain embodiments of the present invention find particular use in applications involving cleaning, bleaching and disinfecting.

Abstract: A method is provided for enzymatically modifying a polyester resin, film, fiber, yarn, fabric or textile to modify the characteristics thereof.

Abstract: The present disclosure relates to a device for measuring surface plasmon resonance and fluorescence of a sample, a system for determining the rate of catalytic activity of an enzyme, a method of determining the rate of catalytic activity of an enzyme, and a method of measuring the adsorption and reactivity of a substance, all of which use SPR and SPEF methods simultaneously. This invention also relates generally to systems and methods for measuring diffusion and reactivity of macromolecules on a surface.

Abstract: Novel enzyme variants including protease variants derived from the DNA sequences of naturally-occurring or re-combinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 27, 45, 170, 181, 251 and 271 of Bacillus amyloliquefaciens subtilisin. Additional variants comprising at least one additional substitution at a position selected from 1, 14, 49, 61, 87, 100, 102, 118, 128, 204 and 258 of Bacillus amyloliquefaciens subtilisin are also described.

Abstract: The present invention relates to novel protein variants that exhibit reduced allergenicity when compared to the parental proteins. Also included are DNA molecules that encode the novel variants, host cells comprising the DNA and methods of making proteins less allergenic.

Abstract: The present invention relates to novel protein variants that exhibit reduced allergenicity when compared to the parental proteins. Also included are DNA molecules that encode the novel variants, host cells comprising the DNA and methods of making proteins less allergenic.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue equivalent to positions 7, 23, 26, 28, 29, 30, 31, 47, 66, 69, 73, 82, 85, 88, 90, 92, 93, 105, 113, 139, 148, 149, 150, 151, 178, 200, 201, 231, 233, 267 and/or 273 of Bacillus amyloliquefaciens subtilisin.

Abstract: The present invention provides novel protein variants that exhibit reduced immunogenic responses, as compared to the parental proteins. The present invention further provides DNA molecules that encode novel variants, host cells comprising DNA encoding novel variants, as well as methods for making proteins less allergenic. In addition, the present invention provides various compositions that comprise these proteins that are less immunogenic than the wild-type proteins.

Abstract: An approach for detecting polymers and polymer fragments by analyzing mass analysis data of mixtures that include labeled versions of the polymers is disclosed. A library of polymer fragments is generated based on the possible fragments of a parent polymer. For each fragment in the library, a theoretical mass for both a natural version and a labeled version is generated. The labeled version may be based on a heavier isotope of an element. Data from a mass analysis, such as a mass spectrographic analysis, is received and automatically analyzed to identify whether a mass doublet is observed for each fragment in the library. The mass doublets correspond to the mass peaks of the natural and labeled versions of the fragments in the library. A determination is made whether a particular mass peak is from a labeled parent polymer or whether the particular mass peak is from an unlabeled source.