Abstract: Disclosed herein are compositions and methods to target enzymatic peracid production to a target surface. The peracid benefit agent produced by the targeted perhydrolytic enzyme can be use for a variety of applications such as bleaching, whitening, disinfecting, destaining, deodorizing, and combinations thereof. Specifically, a fusion protein comprising a perhydrolytic enzyme and at least one peptidic component having affinity for a target surface (excluding body surfaces and oral care surfaces) is used in combination with a suitable substrate and a source of peroxygen to enzymatically produce a peracid on or near the surface of the target material. In a preferred aspect, the target surface is a cellulosic material.

Abstract: Disclosed herein are compositions and methods for delivering substrates for a depilatory product using an enzymatically generated peracid. More specifically, a two component system is provided comprising (a) a first non-aqueous composition comprising a solid source of peroxygen, an ester substrate, and an optional organic cosolvent and (b) an aqueous component having a pH of at least 4 comprising an enzyme catalyst having perhydrolytic activity and a buffer. The perhydrolytic enzyme catalyst may be in the form of a fusion protein comprising a perhydrolytic enzyme coupled through an optional peptide linker to a peptidic component having affinity for hair.

Abstract: Disclosed herein are compositions and methods to treat hair with a peracid-based benefit agent. The peracid benefit agent can be used for hair bleaching, hair weakening, hair removal, hair waiving, hair straightening or any combination thereof. The peracid may be enzymatically generated from a carboxylic acid ester substrate using an enzyme having perhydrolytic activity (perhydrolase) in the presence of a source of peroxygen. A fusion protein comprising the perhydrolase coupled to a hair-binding domain, either directly or through an optional linker, may be used to target the perhydrolytic activity to the hair surface.

Abstract: An acid-cleavable peptide linker comprising aspartic acid and proline residues is disclosed. The acid-cleavable peptide linker provides an altered sensitivity to acid-hydrolytic release of peptides of interest from fusion peptides of the formula PEP1-L-PEP2. The inventive linker, L, is described in various embodiments, each of which provides substantially more rapid acid-release of peptides of interest than does a single aspartic acid-proline pair. In an additional aspect, a method of increasing the stability of an acid cleavable linkage to acid hydrolysis is also provided.

Abstract: An L-arabinose inducible expression system comprising a mutant arabinose promoter. This system exhibits an increase in heterologous protein production upon induction with L-arabinose and comprises a mutant araB promoter and an AraC transcription binding region. This system retains the tight regulatory control characteristic of the wild type arabinose operon.

Abstract: The invention relates to the recombinant expression of a peptide of interest in the form of a fusion protein comprising a solubility tag. The fusion protein comprises at least two portions separated by a cleavable peptide sequence wherein one portion is devoid of cysteine residues and the second portion comprises an effective number of cross-linkable cysteine residues. After cell lysis and isolation of the fusion protein, the fusion protein is subsequently cleaved into a mixture of first and second portions. Oxidative cross-linking is used to selectively precipitate one of the two portions to facilitate simple and effective separation of the peptide of interest.

Abstract: The invention relates to the recombinant expression of a peptide of interest in the form of a fusion protein comprising a solubility tag. The fusion protein comprises at least two portions separated by a cleavable peptide sequence wherein one portion is devoid of cysteine residues and the second portion comprises an effective number of cross-linkable cysteine residues. After cell lysis and isolation of the fusion protein, the fusion protein is subsequently cleaved into a mixture of first and second portions. Oxidative cross-linking is used to selectively precipitate one of the two portions to facilitate simple and effective separation of the peptide of interest.

Abstract: Oral care compositions, oral care systems, oral surface-binding peptides, and a method for applying particles to an oral surface are provided. The oral care system comprises at least one peptidic component comprising a first binding element having affinity for an oral surface and a second binding element having affinity for a ligand property of a particle.

Abstract: The present invention relates to compositions and systems comprising peptide-based reagents for delivery of cosmetic benefit agents to human hair, human skin, or human nail.

Abstract: Peptide tags, referred to here as inclusion body tags, are disclosed useful for the generation of insoluble fusion peptides. The fusion peptides comprise at least one inclusion body tag operably linked to a peptide of interest. Expression of the fusion peptide in a host cell results in a product that is insoluble and contained within inclusion bodies in the cell and/or cell lysate. The inclusion bodies may then be purified and the protein of interest may be isolated after cleavage from the inclusion body tag.

Abstract: A process of in vivo labeling and identifying recombinantly produced peptides or proteins within an unpermeabilized prokaryotic host cell. Recombinant prokaryotic cells expressing a fusion peptide comprising at least one tetracysteine tag were labeled in vivo using a biarsenical labeling reagent. A fluorescent activated cell sorter was used to identify and select subpopulations of fluorescent cells wherein the amount of fusion peptide in the cell was proportional to the amount of fluorescence detected.

Abstract: Peptide tags, referred to here as inclusion body tags, are disclosed useful for the generation of insoluble fusion peptides. The fusion peptides comprise at least one inclusion body tag operably linked to a peptide of interest. Expression of the fusion peptide in a host cell results in a product that is insoluble and contained within inclusion bodies in the cell and/or cell lysate. The inclusion bodies may then be purified and the protein of interest may be isolated after cleavage from the inclusion body tag.

Abstract: An L-arabinose inducible expression system comprising a mutant arabinose promoter. This system exhibits an increase in heterologous protein production upon induction with L-arabinose and comprises a mutant araB promoter and an AraC transcription binding region. This system retains the tight regulatory control characteristic of the wild type arabinose operon.

Abstract: Peptide tags, referred to here as inclusion body tags, are disclosed useful for the generation of insoluble fusion peptides. The fusion peptides comprise at least one inclusion body tag operably linked to a peptide of interest. Expression of the fusion peptide in a host cell results in a product that is insoluble and contained within inclusion bodies in the cell and/or cell lysate. The inclusion bodies may then be purified and the protein of interest may be isolated after cleavage from the inclusion body tag.

Abstract: A process of in vivo labeling and identifying recombinantly produced peptides or proteins within an unpermeabilized prokaryotic host cell. Recombinant prokaryotic cells expressing a fusion peptide comprising at least one tetracysteine tag were labeled in vivo using a biarsenical labeling reagent. A fluorescent activated cell sorter was used to identify and select subpopulations of fluorescent cells wherein the amount of fusion peptide in the cell was proportional to the amount of fluorescence detected.

Abstract: The invention relates to the recombinant expression of a peptide of interest in the form of a fusion protein comprising a solubility tag. The fusion protein comprises at least two portions separated by a cleavable peptide sequence wherein one portion is devoid of cysteine residues and the second portion comprises an effective number of cross-linkable cysteine residues. After cell lysis and isolation of the fusion protein, the fusion protein is subsequently cleaved into a mixture of first and second portions. Oxidative cross-linking is used to selectively precipitate one of the two portions to facilitate simple and effective separation of the peptide of interest.

Abstract: Peptide tags, referred to here as inclusion body tags, are disclosed useful for the generation of insoluble fusion peptides. The fusion peptides comprise at least one inclusion body tag operably linked to a peptide of interest. Expression of the fusion peptide in a host cell results in a product that is insoluble and contained within inclusion bodies in the cell and/or cell lysate. The inclusion bodies may then be purified and the protein of interest may be isolated after cleavage from the inclusion body tag.