WPC decking
❤️ Click here: Decking daske
Prominent regions include structural features, conserved regions, epitopes, domains, motifs, and the like. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid including, for example, unnatural amino acids, etc. The volume of the second compartment is generally small but is sufficient to contain a solid form of the perhydrolase enzyme.
The methods generally comprise synthesizing labeled probes having putative sequences encoding regions of the protein of interest, preparing genomic libraries from organisms expressing the protein, and screening the libraries for the gene of interest by hybridization to the probes. Films can be obtained using methods known in the art, including casting, blow-molding, extrusion, blow extrusion, and the like. It is this ability to transfer oxygen atoms that enables a peracid, for example, peracetic acid, to function as a cleaning, bleaching, and disinfecting agent.
VANJSKE PODNE OBLOGE - DECKING - WPC - Exemplary cleaning components are acid cellulases, acid amylases, acid proteases, acid pectate lyases, and the like. Otporan je na vodu, vlagu i nisku temperaturu.
Poulose Original Assignee Danisco Us Inc. Priority date The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed. A unit -dose package for delivering a perhydrolase enzyme system in a cleaning application, the perhydrolase enzyme system comprising a perhydrolase enzyme component, an acyl substrate component, and a peroxide source component, the package comprising: a first compartment at least partially bounded by a water-soluble material and comprising a first component of the perhydrolase enzyme system; a second compartment at least partially bounded by a water-soluble material and comprising a second component and a third component of the perhydrolase enzyme system; wherein the first component in the first compartment and the second and third components in the second compartment are separated during storage to prevent the formation of peracids, and wherein upon dissolution in an aqueous solution the first compartment and second compartment dissolve simultaneously or sequentially to permit contact of the first, second and third components of the perhydrolase enzyme system to generate peracid. Provisional Patent Application Serial No. Although many hydrolytic enzymes are capable of background levels of perhydrolysis activity only a handful of robust perhydrolase enzymes have been identified. These enzymes preferentially perform perhydrolysis over hydrolysis, making them well suited for use in generating peracids for cleaning, bleaching, and disinfection applications. In one aspect, a unit-dose package for delivering a perhydrolase enzyme system in a cleaning application is provided, the perhydrolase enzyme system comprising a perhydrolase enzyme component, an acyl substrate component, and a peroxide source component, the package comprising: a first compartment at least partially bounded by a water-soluble material and comprising a first component of the perhydrolase enzyme system; a second compartment at least partially bounded by a water-soluble material and comprising a second component and a third component of the perhydrolase enzyme system; wherein the first component in the first compartment and the second and third components in the second compartment are separated during storage to prevent the formation of peracids, and wherein upon dissolution in an aqueous solution the first compartment and second compartment dissolve simultaneously or sequentially to permit contact of the first, second, and third components of the perhydrolase enzyme system to generate peracid. In some embodiments of the unit-dose package of paragraph 1, the first component is the perhydrolase enzyme, the second component is the acyl substrate, and the third component is the peroxide source. In some embodiments of the unit-dose package of paragraph 1, the first component is the acyl substrate, the second component is the perhydrolase enzyme, and the third component is the peroxide source. In some embodiments of the unit-dose package of paragraph 1, the first component is the peroxide source, the second component is the acyl substrate, and the third component is the perhydrolase enzyme. In some embodiments of the unit-dose package of any of the preceding paragraphs, a very low-water, non-aqueous, or non-mixing form of laundry or dishwashing detergent is additionally provided in the first compartment. In some embodiments of the unit-dose package of paragraph 2, the first component is a perhydrolase enzyme provided in liquid or solid form, the second component is an acyl substrate provided in non-aqueous liquid form, and the third component is a peroxide source provided in solid form. In some embodiments of the unit-dose package of paragraph 3, the first component is an acyl substrate provided in non-aqueous liquid form, the second component is a perhydrolase enzyme provided in solid or non-aqueous liquid form, and the third component is the peroxide source provided in solid form. In some embodiments of the unit-dose package of paragraph 4, the first component is a peroxide source provided in solid form, the second component is an acyl substrate provided in non-aqueous liquid form, and the third component is a perhydrolase enzyme provided in solid or non-aqueous liquid form. In some embodiments of the unit-dose package of paragraphs 5-8, the laundry or dishwashing detergent is provided as a non-mixing form selected from the group consisting of a solid, a gel, a paste, or a wax. In some embodiments of the unit-dose package of paragraphs 5-8, the laundry or dishwashing detergent is provided as a very low-water liquid having a water content of less than about 10%. In some embodiments of the unit-dose package of paragraphs 5-8, the laundry or dishwashing detergent is non-aqueous. In some embodiments of the unit-dose package of paragraph 1, a very low- water, non-aqueous, or non-mixing form of laundry or dishwashing detergent is additionally provided in the second compartment. In some embodiments of the unit-dose package of paragraph 12, the first component is a perhydrolase enzyme provided in solid or liquid form, the second component is an acyl substrate provided in non-aqueous form, and the third component is a peroxide source provided in solid form. In some embodiments of the unit-dose package of paragraph 12, the first component is acyl substrate provided in liquid form, the second component is a perhydrolase enzyme provided in solid or non-aqueous liquid form, and the third component is a peroxide source provided in solid form. In some embodiments of the unit-dose package of paragraph 12, the first component is a peroxide source provided in solid or liquid form, the second component is an acyl substrate provided in non-aqueous liquid form, and the third component is a perhydrolase enzyme provided in solid or non-aqueous liquid form. In some embodiments of the unit-dose package of paragraphs 12-15, the laundry or dishwashing detergent is provided as a non-mixing form selected from the group consisting of a solid, a gel, a paste, or a wax. In some embodiments of the unit-dose package of paragraphs 12-15, the laundry or dishwashing detergent is provided as a very low-water liquid having a water content of less than about 10%. In some embodiments of the unit-dose package of paragraphs 12-15, the laundry or dishwashing detergent is non-aqueous. In some embodiments of the unit-dose package of any of the preceding paragraphs, the first compartment is completely bounded by a water-soluble material. In some embodiments of the unit-dose package of any of the preceding paragraphs, the second compartment is completely bounded by a water-soluble material. In some embodiments of the unit-dose package of any of the preceding paragraphs, the first compartment is the water-soluble material bounding the second compartment. In some embodiments of the unit-dose package of any of the preceding paragraphs, the second compartment is the water-soluble material at least partially bounding the first 5 compartment. In some embodiments of the unit-dose package of any of the preceding paragraphs, the first compartment is a film applied to the water-soluble material bounding the second compartment. In some embodiments of the unit-dose package of any of the preceding paragraphs, o the second compartment is a film applied to the water-soluble material bounding the first compartment. In some embodiments the unit-dose package of any of the preceding paragraphs further comprises an additional compartment. In some embodiments of the unit-dose package of paragraph 25, the additional5 compartment comprises a laundry detergent composition, a dishwashing detergent composition, a fabric softener, or a rinsing agent. In some embodiments of the unit-dose package of any of the preceding paragraphs where appropriate , the peroxide source component is and oxidase enzyme and a substrate for the oxidase enzyme, wherein the activity of the oxidase enzyme on the substrate produces o peroxide. In some embodiments of the unit-dose package of any of paragraph 27, the oxidase enzyme and substrate for the oxidase enzyme are present in different compartments. In another aspect, a unit-dose package comprising a water-soluble pouch and a detergent composition is provided, the pouch comprising at least a first compartment and a 5 second compartment, the detergent composition comprising: a from about 5% to about 80% by weight of a surfactant; b from about 1% to about 15% by weight of non-aqueous solvent; c less than 10% by weight of water; and d a perhydrolase enzyme system comprising i a perhydrolase enzyme, ii an acyl substrate, and iii a peroxide source; wherein at least one component selected from i , ii , or iii is separated from at least one other component selected 0 from i , ii , or iii by being present in different compartments of the pouch. In some embodiments, the unit-dose package of paragraph 29 comprises at least a first compartment, a second compartment, and a third compartment, wherein each component selected from i , ii , or iii is separated from each other component by being present in a different compartment of the pouch. In some embodiments of the unit-dose package of preceding paragraphs 29 or 30, the detergent composition further comprises an additional component selected from the group consisting of a chelant, a polymer, a brightener, a fragrance, and a process aid. In some embodiments of the unit-dose package of preceding paragraphs 29-31, the detergent composition further comprises one or more additional enzymes other than the perhydrolase. In some embodiments of the unit-dose package of preceding paragraphs 29-32, the surfactant is an anionic surfactant, a non-ionic surfactant, or combinations thereof. In another aspect, a unit-dose package comprising a water-soluble pouch and a detergent composition is provided, the pouch comprising at least a first compartment and a second compartment, the detergent composition comprising: a a non-phosphorus builder; b a chelating agent; c a perhydrolase enzyme system comprising a perhydrolase enzyme, an acyl substrate, and a peroxide source; wherein at least two components of the perhydrolase enzyme system are present in different compartments of the pouch. In some embodiments of the unit-dose package of paragraph 34, the detergent composition further comprises a cleaning enzyme selected from the group consisting of a protease and an alpha-amylase. In some embodiments, the unit-dose package of paragraphs 34 or 35 further comprises a rinse aid. In another aspect, methods of using the unit dose packages of any of the preceding paragraphs to clean laundry, dishes, toilets, sinks, driveways, decking, and other surfaces is provided. Side views of the unit-dose package are shown in Figures 13 A and 13B and a front view is shown in Figure 13C. The described unit-dose packages utilize water-soluble materials to at least partially define one or more compartments capable of storing a perhydrolase enzyme, an acyl substrate, and source of peroxygen, and preventing these components from reacting until the package is contacted with water. These and other features and advantages of the present compositions and methods are described in detail. Terms not defined should be given their ordinary meanings as using in the relevant art. In addition to the components of the enzymatic bleaching system, the present unit-dose packages can further include detergent compositions, shine agents, fabric softeners, or other components that provide a benefit in the washing or cleaning application. Numerous unit-dose packages can be supplied in a single container e. While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis:hydrolysis ratio, often greater than 1. Such peracid products are able to transfer one of their oxygen atoms to another molecule, such as a soil or stain on a surface. It is this ability to transfer oxygen atoms that enables a peracid, for example, peracetic acid, to function as a cleaning, bleaching, and disinfecting agent. Hydrogen peroxide sources include hydrogen peroxide, itself, as well as molecules that spontaneously, enzymatically, or chemically catalytically produce hydrogen peroxide as a reaction product. Such molecules include, e. For example, an acyl transferase may transfer an acyl group from an acyl substrate to a hydrogen peroxide substrate to form a peracid. In such a reaction, oxygen is reduced to water H 20 or hydrogen peroxide H 20 2. An example of a hydrogen peroxide generating oxidase and its substrate suitable for use herein is glucose oxidase and glucose. Other oxidase enzymes that may be used for generation of hydrogen peroxide include alcohol oxidase, ethylene glycol oxidase, glycerol oxidase, amino acid oxidase, etc. In some embodiments, the hydrogen peroxide generating5 oxidase is a carbohydrate oxidase. The term encompasses textiles made from natural, synthetic e. Textiles may be unprocessed or processed fibers, yarns, woven or knit fabrics, non-wovens, and garments and may be made using a variety of materials, o some of which are mentioned, herein. Examples include cotton and non-cotton cellulosic fibers, yarns or fabrics. Cellulosic fibers may optionally include non-cellulosic fibers. In particular, a material is considered water soluble or dispersible if 1 g of the material is 90% or more dissolved or 0 dispersed in 1 L of 25°C water in 5 min or less, e. The aqueous medium may include any number of dissolved or suspended components, including but not limited to surfactants, salts, buffers, stabilizers, complexing agents, chelating agents, builders, metal ions, additional enzymes and substrates, and the like. Exemplary aqueous media are laundry and dishwashing wash liquors. Materials such as textiles, fabrics, dishes, kitchenware, and other materials may also be present in or in contact with the aqueous medium. Preferred very low- water detergent compositions do not dissolve the water-soluble material used in the unit dose packages described, herein. In some cases, the contents are fully bounded by water-soluble material, meaning that the entire compartment is defined by the water-soluble material, as in the case of a pouch made of water-soluble material. In some cases, the contents are only partially bounded by water- soluble material, meaning that only a portion of the compartment is defined by the water soluble material, and the remainder is defined by water-insoluble material, as in the case of a cup or dish covered by a lid made of water-soluble material. Non-mixing components can also be provided in different phases i. For example, these terms may refer to a material which is substantially or essentially free from components which normally accompany it as found in its native state, such as, for example, an intact biological system. The conventional one- letter or three-letter code for amino acid residues is used herein. The polymer may be linear or branched, it may comprise modified amino acids, and it may be interrupted by non-amino acids. The terms also encompass an amino acid polymer that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as conjugation with a labeling component. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid including, for example, unnatural amino acids, etc. In additional embodiments, related proteins are provided from the same species. In further embodiments, the term encompasses proteins that are immunologically cross-reactive. The preparation of a protein derivative is preferably achieved by modifying a DNA sequence which encodes for the native protein, transformation of that DNA sequence into a suitable host, and expression of the modified DNA sequence to form the derivative protein. The number of differing amino acid residues may be one or more, for example, 1, 2, 3, 4, 5, 10, 15, 20, 30, 40, 50, or more amino acid residues. In some aspects, related proteins and particularly variant proteins comprise at least 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or even 99% or more amino acid sequence identity. Additionally, a related protein or a variant protein refers to a protein that differs from another related protein or a parent protein in the number of prominent regions. For example, in some embodiments, variant proteins have 1, 2, 3, 4, 5, or 10 corresponding prominent regions that differ from the parent protein. Prominent regions include structural features, conserved regions, epitopes, domains, motifs, and the like. Note that where a particular mutation in a variant polypeptide is specified, further variants of that variant polypeptide retain the specified mutation and vary at other positions not specified. For example, in epitope regions that contain an alpha-helix or a beta-sheet structure, the replacement amino acids in the analogous sequence preferably maintain the same specific structure. The term also refers to nucleotide sequences, as well as amino acid sequences. In some embodiments, analogous sequences are developed such that the replacement amino acids result in a variant enzyme showing a similar or improved function. Thus, where the segment or fragment of interest contains, for example, an alpha-helix or a beta- sheet structure, the replacement amino acids preferably maintain that specific structure. It is not intended that homologs necessarily be evolutionarily related. Thus, it is intended that the term encompass the same, similar, or corresponding enzyme s i. In some embodiments, homologous proteins induce similar immunological response s as a reference protein. In some embodiments, homologous proteins are engineered to produce enzymes with desired activity ies. The degree of homology between sequences may be determined using Clustal W Thompson J. PILEUP creates a multiple sequence alignment from a group of related sequences using progressive, pair- wise alignments. It can also plot a tree showing the clustering relationships used to create the alignment. PILEUP uses a simplification of the progressive alignment method of Feng and Doolittle, Feng and Doolittle 1987 J. The method is similar to that described by Higgins and Sharp Higgins and Sharp 1989 CABIOS 5: 151-153. Useful PILEUP parameters including a default gap weight of 3. Another example of a useful algorithm is the BLAST algorithm, described by Altschul et al. One particularly useful BLAST program is the WU-BLAST-2 program {See, Altschul et al. The BLAST program uses as defaults a word- length W of 11, the BLOSUM62 scoring matrix {See, Henikoff and Henikoff 1989 Proc. USA 89: 10915 alignments B of 50, expectation E of 10, M'5, N'-4, and a comparison of both strands. In some embodiments, the wild-type sequence refers to a sequence of interest that is the starting point of a protein engineering project. The genes encoding the naturally-occurring protein may be obtained in accord with the general methods known to those skilled in the art. The methods generally comprise synthesizing labeled probes having putative sequences encoding regions of the protein of interest, preparing genomic libraries from organisms expressing the protein, and screening the libraries for the gene of interest by hybridization to the probes. Positively hybridizing clones are then mapped and sequenced. Acid enzymes have pH optima of less than 7. All references sited herein are hereby incorporated by reference in their entirety. The unit-dose packages utilize water- soluble materials to at least partially define one or more compartments capable of storing the components of the perhydrolase enzyme system i. The reader will appreciate that the document is organized for ease of reading, and that a description in one section of the document should be read in the context of the document as a whole. It will also be apparent that features discussed with reference to one embodiment can be combined with features discussed with reference to another embodiment. Where the same reference numbers are repeated in different Figures, they should be given the same meaning as in the first Figure in which they appeared. In an alternative embodiments, the unit- dose package 20 includes a compartment 21 that contains components of the perhydrolase system 14, 15, 16 suspended or dispersed in a water-soluble material 22 for dissolution and release of the components upon contact with water 13 Figure 2. In either case, the water soluble material is selected such that it substantially dissolves in 5 min or less, e. In the absence of contact with water the water soluble material should remain intact for at least 6 months to prevent release of the contents of the compartment. This can be accomplished by suspending solid perhydrolase optionally in the form of granules and a solid form of peroxide in liquid acyl substrate see, e. However, it is contemplated that a compartment can be partially bounded by water soluble material and partially bounded by water insoluble material. Dissolution of the soluble material would allow the release of the contents of the compartment, while the insoluble material would remain in the wash liquor for later disposal or recycling. In some embodiments of the two compartment unit-dose package, the perhydrolase enzyme 14 is provided in the first compartment 31 and the acyl substrate 15 and peroxide source 16 are provided in the second compartment 32. The perhydrolase enzyme can be provided in liquid or solid form, as described, herein. The acyl substrate and peroxide source can be provided in a low pH, non-aqueous solution, as described, herein. Alternatively, the acyl substrate can be a liquid and the peroxide source can be provided in solid form, or both the acyl substrate and the peroxide source can be provided in solid form. The acyl substrate can be a liquid, or can be provided in a non-aqueous solution. Alternatively, the acyl substrate can be a solid. The5 perhydrolase enzyme can be provided in the form of a liquid or a solid, and the peroxide source can be provided in solid form. The peroxide source can be a liquid or a solid. The acyl substrate can be a liquid and the perhydrolase enzyme provided in solid form. Alternatively, the acyl substrate and the perhydrolase enzyme can be provided in a non-aqueous solution, or the acyl substrate can be a solid and the perhydrolase enzyme can be provided in liquid form. In yet further embodiments, both compartments contain components of the perhydrolase system suspended or dispersed in a water-soluble material, rather than having one or more compartments at least partially bounded by water-soluble material not shown. This embodiment of the two compartment unit-dose package has the general appearance of a single-compartment package. The film can take the form or a coating, design, label, or logo, and may be applied by spraying, brushing, printing including inkjet printing , and the like. The volume of the second compartment is generally small but is sufficient to contain a solid form of the perhydrolase enzyme. The reader will appreciate that such a film applied to the unit-dose package shown in previous Figure 7A would effectively create a three compartment unit-dose package, although it would superficially have the appearance of a single compartment package. The arrangement of the three compartments is generally not critical. This arrangement allows maximum flexibility with respect to solid and liquid forms of any of the components. This configuration is useful for additional functionality to the unit-dose container, for example, including a laundry or dishwashing component in a fourth compartment, isolated from the components of the perhydrolase system. This may be accomplished by 5 forming a barrier in a single container package, e. The compartments can share a common barrier, as illustrated in Figure 8 and 12, or can have their own barriers of water soluble material, as illustrated in Figures 3-6, 10, and 11. The compartments need not be the same size but should rather be optimized and minimized to suit the contents of each chamber. The water-soluble material used to make the package can be of uniform thickness, such that each o component of the package is released at substantially the same time following contact with aqueous medium. Alternatively, the thickness of the water soluble material can vary, such that the contents of one compartment are released before the contents of another compartment. Different compartments can also be bounded by different water soluble materials, to affect different rates of release of the contents of the compartments, for example in response to 5 temperature or pH. For example, a small round, triangular, heart-shaped, or otherwise styled compartment can be attached to a pillow-shaped compartment. Compartments can also be shaped like company trademarks. Different compartments can o contain different dyes to further contribute to the overall design and appearance of the unit-dose package. Small compartments can be stacked on top of large compartments, or multiple compartments can be arranged in a rosette arrangement. However, in some embodiments of the unit-dose package, it may be desirable to provide an enclosure 121 for the water soluble packages 120, e. The enclosure should be mesh or perforated such that it includes a sufficient number of openings 122 to permit water 13 to contact the soluble package to promote dissolution and the release of the components of the perhydrolase system. The mesh or perforated enclosure may be reusable, for example, the end user could open the enclosure to insert a fresh dissolving package, or the manufacturer could collect used enclosures for remanufacture. Alternatively or additionally, the enclosures can be made of a recyclable material. The mesh or perforated enclosure may also be coated, printed including inkjet 5 printing , painted, or otherwise include an active component, including a component of the perhydrolase system. The enclosure 130 includes a casing 131 with a mesh or perforated face 132 having a plurality of openings 133. Although two compartments are shown, the present embodiment can be used with one, two, three, or more compartments, as described, above. In some embodiments, a compartment 139 can be partially bounded by the casing 131, in which case water-soluble material 134 need only be present behind the perforated face 132 Figure 13B. An optional second compartment 138 is shown, which is completely bounded by5 water soluble material 134. Side views of the unit-dose package are shown in Figures 13A and 13B and a front view is shown in Figure 13C. In some embodiments, the handle includes a hook 143, such that the unit-dose package can be suspended i. In related embodiments, the unit-dose package 150 5 is provided in a mesh or perforated enclosure 151, which is attached to string, rope, chain, or other elongated flexible structure 152, optionally with an attachment loop 153, which allows the unit-dose package to be tied or suspended above the bucket, sink, toilet cistern or bowl, dishwasher basket, washing machine drum, or other vessel while the package is dissolving Figure 15. In some embodiments, the perhydrolase system is used to clean, bleach, or disinfect 0 the vessel itself such as the washing machine or dishwasher , while in some embodiments the system is used to produce a peracid solution for use in bleaching, cleaning, or disinfecting other objects, e. Preferably, the unit-dose package can be reused by periodically adding a new unit dose package to the assembly. This embodiment is reminiscent of a swimming pool chlorine dispenser. Additional compartments can be attached to any of the aforementioned unit-dose packages, and such compartments can include solid, gel, paste, wax, or liquid forms of complete laundry or dishwashing detergent compositions, prewash compositions, fabric softeners, anti-spotting additives, fragrances, and the like. By varying the water-soluble material used to form these additional packages, or by varying the thickness of the films of these additional packages, it is possible to control the order in which different components contained within the unit-dose packaging are released, for example in response to temperature or pH. The water soluble material used to contain the components of the perhydrolase enzyme system is thicker, or of a different material than the water soluble material used to contain the laundry or dishwashing detergent composition, such that the laundry or dishwashing detergent composition is released first into the wash liquor, allowing the surfactants and enzymes present in the laundry or dishwashing detergent composition to begin cleaning laundry or dishes before the perhydrolase enzyme system components are released and begin to produce peracid. This arrangement delays the production of peracid in the wash liquor, which peracid may react unfavorably with components of the laundry or dishwashing detergent composition. Exemplary cleaning components are acid cellulases, acid amylases, acid proteases, acid pectate lyases, and the like. The water soluble material used to contain the components of the perhydrolase enzyme system and laundry or dishwashing detergent composition is thinner, or of a different material than the water soluble material used to contain the cleaning component with improved performance at low pH, such that the laundry or dishwashing detergent composition and perhydrolase enzyme system components are released, first, allowing the perhydrolase enzyme system to lower the pH of the wash liquor before the cleaning component that has improved performance at low pH is released. The water soluble material used to contain the components of the perhydrolase enzyme system and laundry or dishwashing detergent composition is thinner, or of a different material than the water soluble material used to contain the catalase, such that the laundry or dishwashing detergent composition and 5 perhydrolase enzyme system components are released, first, allowing peracid formation and cleaning to take place before catalase is released near the end of the cleaning cycle to destroy residual hydrogen peroxide. This embodiment is especially useful when the unit-dose package is dissolved in a bucket for cleaning, e. In one example, the indicator system is conventional pH paper contained within the housing, which paper remains captive in the housing after the water soluble material 5 has dissolved. In other embodiments, a colored pH sensitive indicator is included in a compartment in the unit-dose package, or in a separate water soluble package, for the purpose of indicating when a preselected amount of peracid has been generated. In some embodiments, the perhydrolase enzyme comprises, consists of, or consists essentially of an amino acid sequence that is at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99. In some embodiments, the perhydrolase enzyme is from a microbial source, such as a bacterium or fungus. An exemplary enzyme is derived from Mycobacterium smegmatis. Patent Publications US2008145353 and US2007167344, which are incorporated by reference. In some embodiments, the perhydrolase enzyme comprises, consists of, or consists essentially of an amino acid sequence that is at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99. In some embodiments, the perhydrolase enzyme comprises any one or any combination of substitutions of amino acids selected from Ml, K3, R4, 15, L6, C7, D10, Sl l, L12, T13, W14, W16, G15, V17, P18, V19, D21, G22, A23, P24, T25, E26, R27, F28, A29, P30, D31, V32, R33, W34, T35, G36, L38, Q40, Q41, D45, L42, G43, A44, F46, E47, V48, 149, E50, E51, G52, L53, S54, A55, R56, T57, T58, N59, 160, D61, D62, P63, T64, D65, P66, R67, L68, N69, G70, A71, S72, Y73, S76, C77, L78, A79, T80, L82, P83, L84, D85, L86, V87, N94, D95, T96, K97, Y99F100, R101, R102, P104, L105, D106, 1107, A108, L109, G110, Mi l l, S112, V113, LI 14, V115, T116, Q117, V118, L119, T120, S 121, A122, G124, V125, G126, T127, T128, Y129, P146, P148, W149, F150, 1153, F154, 1194, and F196. Patent Application Publication Nos. Members of the CE-7 esterase family share a conserved signature motif Vincent et al. SEQ ID NO: 3 , the cephalosporin C deacetylase from Bacillus subtilis subsp. SEQ ID NO: 6 , the acetyl xylan esterase from Bacillus pumilus PS213 SEQ ID NO: 7 , the acetyl xylan esterase from Clostridium thermocellum ATCC 27405. SEQ ID NO: 8 , the acetyl xylan esterase from Thermotoga neapolitana SEQ ID NO: 9 , the cephalosporin C deacetylase from Bacillus subtilis ATCC 29233. SEQ ID NO: 10 , the acetyl xylan esterase from Thermotoga maritima or variants, thereof SEQ ID NO: 11. Exemplary variants of this enzyme include C277V, C277A, C277S, and C277T, which are described in U. In some embodiments, the perhydrolase enzyme has a perhydrolysis:hydrolysis ratio greater than 1. In some embodiments, the perhydrolysis:hydrolysis ratio is greater than 1. In some embodiments, the perhydrolase enzyme is provided at a molar ratio with respect to the amount of dye on the textile. Liquid forms of the perhydrolase enzyme include stabilized, nonaqueous formulations that do not dissolve the soluble material in which the perhydrolase enzyme is contained. An exemplary formulation is described in U. The formulation provides perhydrolase in a non-aqueous liquid phase {i. The polymer is insoluble in the carrier fluid but soluble in water. The liquid phase comprises less than 5%, less than 1%, or even less than 0. An advantage of this polymeric formulation is that an acyl substrate can be mixed with the encapsulated enzyme to produce a stable, non-reactive, co-formulated perhydrolase-substrate liquid mixture, which is suitable for use in many embodiments of the present unit-dose dissolving packages. In some embodiments, the polymeric matrix contains one or more filler or extender e. Such polysaccharides may for example include material produced by the organisms from which the enzymes o themselves have been produced, and may remain as contaminants in the partially purified enzyme preparations even though they do not have, themselves have useful enzymatic activity. Alternatively or additionally, such polysaccharides may be added separately, in amounts up to about 1 to 5% by weight or more of the slurry. Such amounts may be comparable with those of the enzymes themselves. In some embodiments, the polysaccharides are present or added 5 before spray-drying. Other exemplary polymers are arabinogalactans, xylogalalctans, and, generally, acid polysaccharides. Some or all of the proteins or peptides may be present in a fermentation broth, cell media, or partially-purified protein preparations, and may remain as contaminants in o the partially purified enzyme preparations even though they do not have, themselves have useful enzymatic activity. Alternatively or additionally, such polysaccharides may be added separately, in amounts up to about 1 to 5% by weight or more of the slurry. Such amounts may be comparable with those of the enzymes themselves. In particular embodiments, spray-drying is used. In various embodiments, the amount of enzyme encapsulated in the polymeric matrix is about 0. In various embodiments, the particles are about 0. The monolith can have any shape, from that of a thin flake to a more globular form, and it may be freely suspended or have a tendency to settle unless agitated or shaken. In some embodiments, an enzyme powder is formed by spray drying or lyophilizing the perhydrolase enzyme. The amount of enzyme present in the powder is preferably from about 5 weight percent wt % to about 75 wt based on the dry weight of the enzyme powder. A preferred weight percent range of the enzyme in the enzyme powder is from about 10 wt to 50 wt%, and a more preferred weight percent range of the enzyme in the enzyme powder is from about 20 wt to 33 wt. In one aspect, the excipient is provided in an amount in a range of from about 95 wt to about 25 wt based on the dry weight of the enzyme powder. A preferred wt % range of excipient in the enzyme powder is from about 90 wt to 50 wt%, and a more preferred wt % range of excipient in the enzyme powder is from about 80 wt to 67 wt. Exemplary excipients are oligosaccharides and surfactants. In a preferred embodiment, the oligosaccharide excipient is maltodextrin. Oligosaccharide-based excipients also include, but are not limited to, water-soluble non-ionic cellulose ethers, such as hydroxymethyl-cellulose and hydroxypropylmethylcellulose, and mixtures thereof. In yet a further embodiment, the excipient is selected from, but not limited to, one or more of the following compounds: trehalose, lactose, sucrose, mannitol, sorbitol, glucose, cellobiose, a-cyclodextrin, and carboxymethylcellulose. Preferably, the surfactant is a polyoxyethylene sorbitan fatty acid ester, with polysorbate 80 being more preferred. The buffer may be present in an amount in a range of from about 0. The buffer may be present in a more preferred range of from 5 about 0. Granules, including multi-layered granules, may be produced by a variety of fabrication techniques including: rotary atomization, wet granulation, dry granulation, spray drying, disc granulation, extrusion, pan coating, spheronization, drum granulation, fluid-bed agglomeration, high-shear granulation, fluid-bed spray coating, crystallization, precipitation, emulsion gelation, spinning disc atomization and other casting approaches, and prill processes. Such processes are known in the art and are described in U. W09932595 describe suitable materials for the core. In some embodiments, the core comprises one or more water soluble or dispersible agent s. Suitable water soluble agents include, but are not limited to, inorganic salts e. Suitable dispersible agents include, but are not limited to, clays, nonpareils combinations of sugar and starch; e. W09932595 describe suitable materials for the coating layer. In some embodiments, the coating layer comprises one of more of the following materials: an inorganic salt e. In one embodiment, the coating layer comprises sugars, such as sucrose. In one embodiment, the coating layer comprises a polymer such as polyvinyl alcohol PVA. Suitable PVA for incorporation in the coating layer s of the multi-layered granule include partially hydrolyzed, fully hydrolyzed and intermediately hydrolyzed having low to high degrees of viscosity. In one embodiment the core is coated with at least two coating layers. In another embodiment the core is coated with at least three coating layers. In a further embodiment the core is coated with at least four coating layers. In one embodiment, at least one coating layer is an enzyme coating layer. In some embodiments the core is coated with at least two enzyme layers. In another embodiment the core is coated with at least three enzyme layers. In some embodiments, the enzyme layer comprises at least one enzyme. In some embodiments the enzyme layer comprises at least two enzymes. In some embodiments, the enzyme layer comprises at least three enzymes. In addition to one or more perhydrolases, the coating s may further include, e. Foamblast 882 ® is available from Emerald Foam Control, LLC. Foamblast 882 ® is a defoamer which is made with food grade ingredients. In a particular embodiment, the outer coating layer of a multi-layered granule comprises an inorganic salt e. Where reactive components of the perhydrolase system, or other reactive components, are included in the same granule, the different components can be separated by an intermediate layer to prevent reaction between the components. Such a layer may be referred to as a reaction barrier. Preferred water soluble materials include, for example, polyvinyl acetate, methyl cellulose waxes and the like, sodium chloride, sucrose, magnesium sulfate, ammonium sulfate, hydroxypropyl methyl cellulose, ethyl cellulose, carboxy methyl cellulose, acacia gum, polyvinylpyrrolidone, mono and diglycerides, polyethylene glycol, non-ionic surfactants, starch, hydroxypropyl starch, hydroxyethyl starch and other modified starches. See, for example, U. In some embodiments, the multi-layered granules are produced using a fluid-bed spray coating process. The first coating layer is applied to the core then the second coating layer is applied to the first coating layer and then the third coating layer is applied to second coating layer. The first coating layer is applied to the core then the second coating layer is applied to the first coating layer and then the third coating layer is applied to second coating layer. In some embodiments, the granules are formulated so as to contain an enzyme protecting agent and a dissolution retardant material i. The acyl substrate may be a mono-, di-, tri-, or multivalent ester, or a mixture thereof. For example, the acyl substrate may be a carboxylic acid and a single alcohol monovalent, e. In some embodiments, the acyl substrate is a polymeric ester, for example, a partially acylated acetylated, propionylated, etc. In some embodiments, the acyl substrate is an ester of one or more of the following: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, caprylic acid, nonanoic acid, decanoic acid, dodecanoic acid, myristic acid, palmitic acid, stearic acid, oleic acid, monoacetin, monopropionin, dipropionin, tripropionin, monobutyrin, dibutyrin, glucose pentaacetate, xylose tetraacetate, acetylated xylan, acetylated xylan fragments, P-D-ribofuranose-l,2,3,5-tetraacetate, tri-O-acetyl-D-galactal, tri-O-acetyl-glucal, propylene glycol diacetate, ethylene glycol diacetate, monoesters or diesters of 1,2-ethanediol, 1,2-propanediol, 1,3-propanediol, 1,2- butanediol, 1,3-butanediol, 2,3-butanediol, 1,4-butanediol, 1,2-pentanediol, 2,5-pentanediol, 1,6- pentanediol, 1,2-hexanediol, 2,5-hexanediol, or 1,6-hexanediol. In some embodiments, triacetin, tributyrin, and other esters serve as acyl donors for peracid formation. In some embodiments, the acyl substrate is propylene glycol diacetate, ethylene glycol diacetate, or ethyl acetate. In one embodiment, the acyl substrate is propylene glycol diacetate. The amount of substrate used for color modification may be adjusted depending on the number carboxylic acid ester moieties in the substrate molecule. In some embodiments, the concentration of carboxylic acid ester moieties in the final aqueous medium e. Exemplary concentrations of carboxylic acid ester moieties include about 60 mM, about 80 mM, about 100 mM, about 120 mM, about 140 mM, about 160 mM, about 180 mM, and about 200 mM. Exemplary amounts of ester substrate include about 30 mM, about 40 mM, about 50 mM, about 60 mM, about 70 mM, about 80 mM, about 90 mM, and about 100 mM. The skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent ester substrates based on the number of carboxylic acid esters moieties per molecule. Exemplary liquids are PGDA, triacetin, and other substrates listed herein, which are liquids at the temperature at which an end user is likely to use the present unit-dose packaged peracid generating system. Liquid substrates are preferably provided in non-aqueous form, or can be added to the same chamber as a very low water or non-aqueous detergent. In some embodiments, the acyl substrate is a solid, which includes gums resulting from hygroscopic solid acyl substrates. Exemplary liquids are 2,2-dimethyl-l,3-propanediol, paranitrophenyl acetate, glucose pentaacetate, and other substrates listed herein, which are solids at the temperature at which an end user is likely to use the present unit-dose packaged peracid generating system. In some embodiments, the carboxylic acid ester moieties of the ester substrate are provided at about 20 to about 20,000 times the molar amount of dye. As before, the skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent acyl substrates based on the number of carboxylic acid esters moieties per molecule. In some embodiments, the acyl substrate is provided in a molar excess with respect to the perhydrolase enzyme. The skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent acyl substrates based on the number of carboxylic acid esters moieties per molecule. In some embodiments, the peroxide source is hydrogen peroxide. In some embodiments, the peroxide source is a compound that generates peroxide upon addition to water. The compound may be a solid or a liquid. Such compounds include adducts of hydrogen peroxide with various inorganic or organic compounds, of which the most widely employed is sodium carbonate per hydrate, also referred to as sodium percarbonate. Examples of inorganic perhydrate salts are perborate, percarbonate, perphosphate, persulfate and persilicate salts. Inorganic perhydrate salts are normally alkali metal salts. Additional hydrogen peroxide sources include adducts of hydrogen peroxide with zeolites, urea hydrogen peroxide, and carbamide peroxide. For certain perhydrate salts, preferred forms are granular compositions involving a coating, which provides better storage stability for the perhydrate salt in the granular product. Suitable coatings comprise inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures thereof, or organic materials such as waxes, oils, or fatty soaps. In one embodiment, the enzymatic hydrogen peroxide generation system comprises an oxidase and its substrate. Suitable oxidase enzymes include, but are not limited to: glucose oxidase, sorbitol oxidase, hexose oxidase, choline oxidase, alcohol oxidase, glycerol oxidase, cholesterol oxidase, pyranose oxidase, carboxyalcohol oxidase, L-amino acid oxidase, glycine oxidase, pyruvate oxidase, glutamate oxidase, sarcosine oxidase, lysine oxidase, lactate oxidase, vanillyl oxidase, glycolate oxidase, galactose oxidase, uricase, oxalate oxidase, and xanthine oxidase. For example, lactate oxidases from Lactobacillus species known to create peroxide from lactic acid and oxygen may be used. One advantage of such a reaction is the enzymatic generation of acid {e. Such a reduction in pH is also brought about directly by the production of peracid. In some embodiments, the oxidase enzyme is in the same compartment as the perhydrolase enzyme, acyl substrate, or source of peroxygen. In some embodiments, the substrate for the oxidase enzyme is in the same compartment as the perhydrolase enzyme, acyl substrate, or source of peroxygen. In some embodiments, hydrogen peroxide is provided at about 10 to about 1,000 times the molar amount of dye. Exemplary amounts of hydrogen peroxide include about 30 mM, about 40 mM, about 50 mM, about 60 mM, about 70 mM, about 80 mM, about 90 mM, and about 100 mM. In some embodiments, the hydrogen peroxide is provided at about 10 to about 10,000 times the molar amount of dye. The water-soluble material should begin to dissolve, such that the package begins to substantially release its contents within a few minutes of being contacted with water. Preferably, the contents of the package are substantially released in 5 min or less, 4 min or less, 3 min or less, 2 min or less, 1 min or less, or even 30 sec or less, 5 after contact with water. The mixture is then filtered through a sintered-glass filter with a o pore size of no more than about 50 μιη. The filtrate is collected and the water is removed by any conventional method {e. Then, the percentage solubility or dispersibility can then be calculated. Films can be obtained using methods known in the art, including casting, blow-molding, extrusion, blow extrusion, and the like. The films may optionally be stretched during formation of the packaging or during filing and sealing of the packaging with the aforementioned contents. Stretching the films makes the final packaging more compact. More preferably the polymer is selected from polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose sodium, dextrin, ethylcellulose, hydroxyethyl cellulose, hydroxypropyl methylcellulose, maltodextrin, polymethacrylates, and mixtures thereof, most preferably polyvinyl alcohols, polyvinyl alcohol copolymers, hydroxypropyl methyl cellulose HPMC , and mixtures thereof. Blends of polymers can be used to achieve the desired dissolution rate and storage stability, and different polymers can be used for different compartments of the packaging. Another preferred film is known under the trade reference PT-75, sold by Aicello Chemical Europe GmbH, Carl-Zeiss-Strasse 43, 47445 Moers, DE. The resulting film preferably is formulated to be insoluble at a pH greater than about 9. The resulting film also preferably has sufficient wet strength to withstand agitation in an automatic washing apparatus for the intended use during pre-rinse phases of washing. Preferably, the PVOH is fully hydrolyzed e. The polysaccharide obtained by more extensive deacetylation of chitin is chitosan. Both chitin and chitosan are insoluble in water, dilute aqueous bases, and most organic solvents. However, unlike chitin, chitosan is soluble in dilute aqueous acids, usually carboxylic acids, as the chitosonium salt. Chitosan is available in different molecular weights and is generally regarded as non-toxic and biodegradable. The degree of acetylation has a significant effect on the amine group pKa, and hence solubility behavior, and the rheological properties of the polymer. The amine group on the mostly deacetylated polymer has a pKa in the range of 5. At low pH, the polymer is soluble, with the sol-gel transition occurring at approximate pH 7. As the degree of acetylation increases, the pH above which the film dissolves increases. The degree of acetylation of the chitosan is preferably about 65% or less, or 70% or less, for example in ranges such as about 50% to about 65%, about 55% to about 65%, or about 60% to about 65%, to provide a film with a pH solubility trigger of about 9. This material can be obtained by a reacetylation reaction, using acetic anhydride, of commercially available 85% to 95% deacetylated chitosan in aqueous acetic acid, by methods known in the art. An average molecular weight of about 150,000 Da to about 190,000 Da is preferred. The weight ratio of PVOH to chitosan is about 12: 1 to about 3: 1, or about 8: 1 to about 10: 1, for example about 9: 1. Boric acid preferably is used in an amount in a range of about 0. For example, it may be beneficial to add plasticizers for example glycerol, ethylene glycol, diethylene glycol, propylene glycol, sorbitol and mixtures thereof , additional water, disintegrating aids, lubricants, release agents, fillers, extenders, crosslinking agents, antiblocking agents, antioxidants, detackifying agents, antifoams, nanoparticles such as layered silicate-type nanoclays e. For example, the unit-dose package may include a scaffold structure to which the water soluble material attaches, or an enclosure that surrounds the compartment s bounded by water-soluble material. The insoluble material is preferably a low cost, recyclable, polymeric material, such as polyethylene terephthalate, polyethylene, polyvinyl chloride, polypropylene, polycarbonate, and the like, although it could in theory be wood or metal. Particularly where the unit-dose container is intended for laundry use, the surface of the insoluble material should be smooth and free from sharp corners, which could damage clothing. Exemplary detergent compositions include laundry detergent compositions and dishwashing compositions, including automatic dishwashing compositions. As described in detail, herein, the detergent compositions may be included in the one or more compartments of the unit dose package that also include one or more components of the perhydrolase system, or may be included in one or more additional compartments of the unit dose package that do not include any of the components of the perhydrolase system. Alternatively, components of the detergent compositions may provided in different compartments, such that some components of the detergent composition are included in the one or more compartments of the unit dose package that also include one or more components of the perhydrolase system, and other components of the detergent composition are included in one or more additional compartments of the unit dose package that do not include any of the components of the perhydrolase system. Many of the exemplary detergent formulations are already intended to be provided in multiple-compartment format, making them well-suited for inclusion in the present unit dose packages along with components of the perhydrolase system. Because they are conventional detergent compositions, many of them include bleaching agents, typically a percarbonate source and a bleach booster. In preferred embodiments of present compositions and methods, the perhydrolase system partially or completely replaces these conventional bleaching agents. Unless otherwise indicated, all numbers refer to the wt of components. In the following tables, the reference to enzymes or enzyme preparation includes all enzymes known to be useful in detergent compositions but excluding perhydrolase enzymes. Automatic Dishwashing ADW Detergent Compositions Formulation 1 2 3 4 Level Level Level Level Ingredient %wt %wt %wt %wt Solid ADW detergent composition STPP 35 0 0 56 Carbonate 24 45 40 18. Unit Dose Laundry Del tergent Compositions Ingredients 1 2 3 4 5 Alkylbenzene sulfonic acid C 11- 13, 23. Multi-compartment formulations Composition 1 2 Compartment A B C A B C Volume of each compartment 40 ml 5 ml 5 ml 40 ml 5 ml 5 ml Active material in Wt. Dry detergent compositions Particulate composition 5 6 7 8 STPP 60 60 61 61 HEDP 1 1 1 1 TERMAMYL® 1. Dry detergent compositions Solid composition 1 2 3 4 Ci 4AO 5 5 C 16AO 5 5 SLF18 5 5 STPP 55 55 56 56 HEDP 1 1 1 1 Enzyme 2. Dry and liquid detergent compositions Solid Composition Level %wt STPP 40 Carbonate 24 Silicate 7 TAED 0. Liquid detergent compositions Raw materials Formula 1 Formula 2 Formula 3 Formula 4 Formula 5 Formula 6 Formula 7 % vvt % vvt % vvt % vvt % vvt % vvt % vvt PEG 1500 5. Liquid detergent compositions Composition 1 2 3 Sodium carbonate 8 8 8 Sodium percarbonate 11 11 11 Trisodium citrate 40 40 41. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Liquid detergent compositions 1 2 3 4 Cleaning agent A; pH 20°C 6. Multiple-compartment liquid detergent compositions 2 3c Compartment A B A B A B 32 g 4 g 32 g 4 g 32 g 4 g Ingredient name WT WT WT WT WT WT Linear alkyl benzene 14. Multiple-compartment liquid detergent compositions Ingredient name Compartment 1 Compartment 2 Linear alkyl benzene sulfonic 10 14. Solid detergent compositions Ingredient 1 2 3 4 5 6 7 Transition -Metal 0. Liquid detergent compositions wt% 1 2 3 4 5 6 Linear alkylbenzenesulfonate 8 7. Liquid detergent compositions wt% 1 2 3 4 5 6 AES C12-15 alkyl ethoxy 1. Liquid detergent compositions wt% 1 2 3 4 5 6 AE3S 2. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 LAS 12. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 LAS 22. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 AES 8. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 AES 2. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 AES 8. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 AES 0. Liquid Detergent Compositions Ingredient 1 2 3 4 5 6 AES 2. Liquid Detergent Compositions Ingredients 1 2 3 4 5 6 AES 11. In some embodiments, the unit-dose packages are for laundry application, particularly machine wash laundry application in top-loading and front-loading washing machines. In such applications, the unit dose packages are added to the washing machine as it is l o filing with water or after it is filled with water. Where the unit dose package does not include a laundry detergent composition, it can be added separately. Ideally, clothes are added to the washing machine after the unit dose package has dissolved and all perhydrolase components and detergent components have dispersed in the wash liquor, although it is appreciated and contemplated that many consumers follow a less regimented protocol. A feature of the present 15 unit dose packages is that a finite amount of time and an adequate amount of water is required to dissolve the package and form peracid in the wash liquor, therefore adding the unit dose package on top of clothes to be washed, or adding clothes to be washed and the unit dose package simultaneous to the washing machine is unlikely to cause unwanted bleaching. In such applications, the unit dose packages are added to the detergent dispenser of the dishwasher, or placed on a rack within the dishwasher prior to beginning a typical automatic wash cycle. Where the unit dose package does not 5 include a dishwashing detergent composition, it can be added separately. Where the unit dose package does not include a o detergent composition, it can be added separately. Exemplary items to be cleaned include, but are not limited to, clothes, dishes, driveways, decks, tires, animal facilities, hospital floors, medical equipment, and other surfaces. In some embodiments, the unit-dose packages are used to clean, bleach, or disinfect washing machines or dishwashers themselves. In such cases, the housing can be recovered from the vessel after the unit dose package has dissolved or after the wash application is complete. In some embodiments, the housing is attached to a handle, rod, hook, string, rope, chain, or other structure to impart functionality. The following examples are intended to further illustrate, but not limit, the compositions and methods. Therefore, the description should not be construed as limiting the scope of the invention. Serine proteases of bacillus species 2013-12-13 2015-06-18 Danisco Us Inc. Kgaa Washing or cleaning product with reduced surfactant content 2015-06-17 2016-12-22 Danisco Us Inc. Bacillus gibsonii-clade serine proteases 2015-11-05 2017-05-11 Danisco Us Inc Paenibacillus sp. Enzyme-containing granules coated with hydrolyzed polyvinyl alcohol or copolymer thereof 1986-11-19 1995-02-14 Genencor, Inc. Lipase from Pseudomonas mendocina having cutinase activity 1992-08-14 1997-12-10 Genencor International GmbH Novel enzyme granulates 1997-12-20 1999-07-01 Genencor International, Inc. Granule with hydrated barrier material 1994-11-18 2001-01-17 Genencor International, Inc. Coated enzyme granules 2000-10-13 2001-05-08 Colgate Palmolive Company Automatic dishwashing cleaning system 1996-05-13 2001-06-19 Genencor International, Inc. Perhydrolase 2002-03-06 2005-06-30 Reckitt Benckiser N. Warewashing composition comprising zinc and aluminum ions for use in automatic dishwashing machines 2005-12-13 2009-01-01 Dicosimo Robert Production Of Peracids Using An Enzyme Having Perhydrolysis Activity 2001-12-20 2009-03-24 Reckitt Benckiser Inc. Dupont De Nemours And Company Multi-component peracid generation system 2001-03-16 2010-05-13 Conopco, Inc. Dust free particulate enzyme formulation 1986-06-09 1991-07-09 The Clorox Company Enzymatic peracid bleaching system 1986-11-19 1992-04-28 The Clorox Company Enzymatic peracid bleaching system with modified enzyme 1986-11-19 1995-02-14 Genencor, Inc. Enzyme-containing granules coated with hydrolyzed polyvinyl alcohol or copolymer thereof 1992-08-14 1997-12-10 Genencor International GmbH Novel enzyme granulates 1994-11-18 2001-01-17 Genencor International, Inc. Coated enzyme granules 1996-05-13 2001-06-19 Genencor International, Inc. Enzyme granulate for washing and cleaning 1997-01-13 2003-01-07 Ecolab Inc. Alkaline detergent containing mixed organic and inorganic sequestrants resulting in improved soil removal 1997-12-20 1999-07-01 Genencor International, Inc. Granule with hydrated barrier material 1999-01-08 2003-03-18 Genencor International, Inc. Unit dose cleaning product 2001-03-16 2010-05-13 Conopco, Inc. Unit dose products 2001-12-20 2009-03-24 Reckitt Benckiser Inc. Container 2002-03-06 2005-06-30 Reckitt Benckiser N. Du Pont De Nemours And Company Production of peracids using an enzyme having perhydrolysis activity 2005-12-13 2008-07-24 Dicosimo Robert Production of Peracids Using An Enzyme Having Perhydrolysis Activity 2005-12-13 2009-01-01 Dicosimo Robert Production Of Peracids Using An Enzyme Having Perhydrolysis Activity 2005-12-13 2007-06-21 E. Dupont De Nemours And Company Multi-component peracid generation system 2008-10-03 2011-11-22 E. Serine proteases of bacillus species 2013-12-13 2015-06-18 Danisco Us Inc. Kgaa Washing or cleaning product with reduced surfactant content 2015-06-17 2016-12-22 Danisco Us Inc. Bacillus gibsonii-clade serine proteases 2015-11-05 2017-05-11 Danisco Us Inc Paenibacillus sp.
Montaza drvene terase
Provisional Patent Application Serial No. Multiple-compartment liquid detergent compositions 2 3c Compartment A B A B A B 32 g 4 g 32 g 4 g 32 g 4 g Ingredient name WT WT WT WT WT WT Linear alkyl benzene 14. The aqueous medium may include any number of dissolved or suspended components, including but not limited to surfactants, salts, buffers, stabilizers, complexing agents, chelating agents, builders, metal ions, additional enzymes and substrates, and the like. In one example, the indicator system is conventional pH paper contained within the housing, which paper remains captive in the housing after the water soluble material 5 has dissolved. Prirodna patina drveta nastaje već nakon kratkog vremena po montaži. In preferred embodiments of present compositions and methods, the perhydrolase system partially or completely replaces these conventional bleaching agents.
