Cleansing composition comprising amylase variants with high stability in the presence of a chelating agent

Abstract

The present invention relates to cleaning compositions comprising variants of an alpha-amylase with greater stability against chelating agents compared to its original enzyme, and to a cleaning process comprising such compositions.

Description

Cleaning composition comprising amylase variants with high stability in the presence of a chelating agent. Field of the invention The present invention, as defined by the claims, relates to cleaning compositions comprising variants of an alpha-amylase that have improved stability against chelating agents with respect to their parent enzyme. Background of the invention Alpha-amylases (alpha-1, 4-glucan-4-glucanohydrolases, EC3.2.1.1) constitute a group of enzymes that catalyze the hydrolysis of starch and other linear and branched oligosaccharides and polysaccharides with 1, 4-glycosidic linkages. Among the first bacterial alpha-amylases used was an alpha-amylase from B. licheniformis, also called Termamyl, which has been extensively characterized and its crystal structure determined. Alkaline amylases, such as the alpha-amylase derived from Bacillus sp. described in WO 95 / 26397, constitute a particular group of alpha-amylases that are useful in detergents. Many of these known bacterial amylases have been modified to improve their functionality in a specific application. Alpha-amylase variants and compositions comprising them have been described, for example, in WO 99 / 23211 A1, WO 2009 / 061379 A1, and WO 02 / 092797 A2. Termamyl and many other highly effective alpha-amylases required calcium for their activity. In the crystal structure of Termamyl, four calcium atoms were found to be bound to the alpha-amylase structure, coordinated by negatively charged amino acid residues. In other alpha-amylases, the number of calcium ions bound to the structure may differ. This calcium requirement is a disadvantage in applications where strong chelating agents are present, such as in detergents and cleaning compositions. As mentioned previously, it is well known that several enzymes depend on calcium or other metal ions such as magnesium or zinc for both activity and stability. Therefore, developing enzymes that are stable and exhibit good efficacy in detergents and cleaning compositions containing chelating agents presents a challenge. Chelating agents are incorporated to reduce water hardness during washing, protect bleaching agents that may also be present, and have a direct effect on the removal of some stains. The stability of a calcium-dependent enzyme in a detergent can sometimes be improved by adding calcium to the detergent, but this often destroys the stain-removing effect. Furthermore, adding calcium to a liquid detergent can introduce formulation problems, specifically affecting the detergent's physical stability. Summary of the invention Therefore, it would be beneficial to provide alpha-amylase compositions and variants that are stable against chelating agents and that preferably have a maintained or increased clearing capacity compared to the parental alpha-amylase. Therefore, in a second aspect, the invention relates to a cleansing composition according to claim 1. The cleansing composition comprises a variant of a parental alpha-amylase, wherein the parental alpha-amylase is an alpha-amylase having the amino acid sequence shown in sec. 6 Id. and the variant has amylolytic activity. The variant has the amino acid sequence shown in sec. 6 Id. with one of the sets of mutations listed in claim 1. 1. The composition further comprises at least one cleaning aid and at least one chelating agent wherein said chelating agent at a concentration of less than 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured at 21 °C and pH 8.0. In a second aspect, the invention relates to a method of washing clothes, comprising washing a garment with a composition according to the first aspect of the invention, preferably at a temperature of 30 °C or less, or more preferably, at a temperature of 20 °C or less. Detailed description of the invention Definitions Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC3.2.1.1) are a group of enzymes that catalyze the hydrolysis of starch and other linear and branched oligosaccharides and polysaccharides with 1,4-glycosidic linkages. Known alpha-amylases are obtained from a wide range of organisms, including bacteria, such as species of the genus Bacillus, for example, Bacillus licheniformis; fungal species, such as Aspergillus oryzae (TAKA-amylase) or Aspergillus niger; plants, such as barley; and mammals. Natural enzyme: The term "natural" alpha-amylase denotes an alpha-amylase expressed by a naturally occurring microorganism, such as a bacterium, yeast, or filamentous fungus. The terms "natural enzyme" and "parental enzyme" may be used interchangeably when the parental enzyme is not a variant enzyme. Variant enzyme: The term "variant" is defined herein as a polypeptide having alpha-amylase activity comprising an alteration, such as a substitution, insertion, and / or deletion, of one or more amino acid residues at one or more specific positions in the parental or natural amylase. Preferably fewer than 50 modifications, more preferably fewer than 30 modifications. The altered alpha-amylase is obtained by human intervention through modification of the parental alpha-amylase. The variants used within the scope of the present invention, as defined in the claims, are listed in claim 1. Parent enzyme: The term "parental" alpha-amylase, as used herein, means an alpha-amylase that is modified to produce the variant alpha-amylases of the present invention. This term also refers to the polypeptide against which a variant of the invention is compared. The parent may be a naturally occurring ("wild type") polypeptide, or it may even be a variant thereof, prepared by any suitable means. For example, the parental protein may be a variant of a naturally occurring polypeptide that has been modified or altered in its amino acid sequence. Therefore, the parental alpha-amylase may have one or more amino acid substitutions, deletions, and / or insertions. Thus, the parental alpha-amylase may be a variant of a parental alpha-amylase.A parental variant can also be an allelic variant, which is a polypeptide encoded by any two or more alternative forms of a gene that occupies the same chromosomal locus. Improved property: The expression "improved property" is defined in this document as a feature associated with an improved variant compared to the parental alpha-amylase.These improved properties include, but are not limited to, increased amylolytic activity, for example, when measured in an EnzChek assay or the PNP-7 assay as described in the examples section of this specification; greater cleaning capacity, such as soiling effectiveness, for example, effectiveness against starch-containing stains; stain removal; prevention of graying; stability, for example, thermostability, pH stability, or stability in the presence of detergent-enhancing additives, including chelating agents; stability in powder, liquid, or gel detergent formulations or dishwashing compositions; temperature-dependent effectiveness and altered activity profile; pH activity; substrate specificity; product specificity; and chemical stability.The cleaning and / or dishwashing power can be measured as described later in the "Materials and Methods" section of this application. Preferably, variants of the invention include a combination of improved properties, such as improved stability, improved cleaning power, improved dishwashing power, and / or improved detergent activity. Improved stability includes both stability during storage in a concentrated detergent product and stability in the diluted detergent during washing. The improved properties include increased cleaning or dishwashing power at low temperatures. Activity: In the present context, the term "activity" is amylolytic activity, measured by the number of 1,4-alpha-D-glycosidic bonds hydrolyzed in polysaccharides containing three or more D-glucose units with 1,4-alpha linkages, such as starch, per unit time and per unit of enzyme protein under specified conditions; for example, the activity obtained under specified conditions per ml of enzyme sample per g of an enzyme protein. Activity can be measured in, for example, the EnzChek assay or the PNP-G7 assay as described later in "Materials and Methods." In this application, the term "activity" is used interchangeably with "amylolytic activity." The term "specific activity" is frequently used to describe the maximum activity obtained per ml (g) of enzyme protein. Improved Chemical Stability: The term "improved chemical stability" is defined herein as a variant enzyme that retains enzymatic activity after an incubation period in the presence of a chemical or chemicals, whether naturally occurring or synthetic, that reduce the enzymatic activity of the precursor enzyme. Improved chemical stability may also result in variants that can better catalyze a reaction in the presence of such chemicals. In one particular aspect of the invention, improved chemical stability is improved stability in a detergent, particularly a liquid detergent. Improved detergent stability is, in particular, improved stability of alpha-amylase activity when an alpha-amylase variant of the present invention is blended into a liquid detergent formulation comprising a chelating agent; the liquid may also include gels or a paste.Liquid detergent formulation can refer to concentrated detergent that is added during an automatic laundry or dishwashing process, or a diluted detergent such as a washing solution, i.e., an aqueous solution to which the concentrated detergent is added. In the present invention, the liquid detergents are particularly useful as liquid laundry detergents. Stability: The term "stability" includes stability during storage and stability during use, for example, during a washing process, and reflects the stability of the amylase over time, for example, how much activity is retained when the amylase is kept in solution, particularly in a detergent solution. For example, the alpha-amylase variant may have a residual activity, i.e., the level of retained activity, above 70% after 18 hours at 31 °C. Stability is influenced by many factors, for example, pH, temperature, detergent composition (e.g., the amount and type of detergent booster additive, surfactants, etc.). Amylase stability is measured using the EnzCheck test or the PNP-G7 test described in "Materials and Methods." Improved stability: The term "improved stability" is defined herein as a variant enzyme exhibiting greater stability than that of the parental alpha-amylase, for example, having a residual activity greater than 70% or having at least a 10 pp improvement in residual activity compared to the parental enzyme after 18 hours at pH 8 in the presence of (1.5 w / v) DTPA at 31 °C when measured in the EnzCheck assay as described in "Materials and Methods". The improvement in percentage points (pp) in the residual activity of the variant compared to the parental enzyme is calculated as the difference between the residual activity of the variant and that of the parental enzyme as described in "Materials and Methods". Detergency Boosters. Detergency boosters can be classified using the test described by MK Nagarajan et al., JAOCS, vol. 61, no. 9 (September 1984), pp. 1475–1478 to determine the minimum level of detergency booster required to reduce water hardness at pH 8 from 2.0 mM (as CaCO3) to 0.10 mM in solution. The detergency booster can be, in particular, a chelating agent that forms water-soluble complexes, for example, with calcium and magnesium ions. Chelating agents, or chelating agents, are chemical substances that form molecules with specific metal ions, inactivating the ions so they cannot react with other elements. They are therefore binding agents that suppress chemical activity by forming chelates. Chelation is the formation or presence of two or more separate bonds between a ligand and a single central atom. The ligand can be any organic compound, a silicate, or a phosphate. In this context, the term "chelating agents" encompasses chelating agents, complexing agents, or sequestering agents, which form water-soluble complexes with metal ions such as calcium and magnesium. The chelation effect describes the enhanced affinity of chelating ligands for a metal ion compared to the affinity of a collection of similar non-chelating ligands for the same metal.Chelating agents have the ability to bind with metal ions, particularly calcium ions (Ca2+), and have been widely used in detergents and general washing compositions, such as laundry or dishwashing liquids. However, chelating agents themselves have been shown to inhibit enzyme activity. The term "chelating agent" is used interchangeably with "complexing agent," "chelating agent," or "chelant" in this application. Since most alpha-amylases are sensitive to calcium, the presence of chelating agents can affect enzyme activity. The calcium sensitivity of alpha-amylases can be determined by incubating a given alpha-amylase in the presence of a strong chelating agent and analyzing the impact of this incubation on the activity of the alpha-amylase in question. A calcium-sensitive alpha-amylase will lose a significant portion or all of its activity during incubation. Characterization of Chelating Agents As mentioned, the chelation effect describes the enhanced affinity of chelating ligands for a metal ion compared to the affinity of a collection of similar non-chelating ligands for the same metal. However, the strength of this chelation effect can be determined by various types of assays or measurement methods, thus differentiating or classifying chelating agents according to their chelating effect (or strength). In a preferred assay, chelating agents can be characterized by their ability to reduce the concentration of free calcium ions (Ca2+) from 2.0 mM to 0.10 mM or less at pH 8.0, for example, using a test based on the method described by MKNagarajan et al., JAOCS, vol. 61, no. 9 (September 1984), pp. 1475-1478. Example 2a describes an example of characterizing chelating agents using the method based on Nagarajan et al.Preferably, the chelating agent required according to the invention comprises chelating agents capable of reducing the concentration of free calcium ions from 2.0 mM to 0.1 mM or less to a concentration of less than 10 mM, preferably less than 9.5 mM, preferably less than 9 mM, preferably less than 8.5 mM, preferably less than 8 mM, preferably less than 7.5 mM, preferably less than 7 mM, preferably less than 6.5 mM, preferably less than 6 mM, preferably less than 5.5 mM, preferably less than 5 mM, preferably less than 4.5 mM, less than 4 mM, preferably less than 3.5 mM, preferably less than 3 mM, preferably less than 2.5 mM, preferably less than 2 mM, preferably less than 1.5 mM or preferably less than 1 mM, when measured at pH 8.0 at 21°C. Preferably, the chelating agent according to the invention comprises chelating agents capable of reducing the concentration of free calcium ions from 2.0 mM to 0.1 mM to a concentration of less than 10 mM, preferably less than 9.5 mM, preferably less than 9 mM, preferably less than 8.5 mM, preferably less than 8 mM, preferably less than 7.5 mM, preferably less than 7 mM, preferably less than 6.5 mM, preferably less than 6 mM, preferably less than 5.5 mM, preferably less than 5 mM, preferably less than 4.5 mM, less than 4 mM, preferably less than 3.5 mM, preferably less than 3 mM, preferably less than 2.5 mM, preferably less than 2 mM, preferably less than 1.5 mM or preferably less than 1 mM, when measured in 80 mM potassium chloride and EPPS (acid 4-(2-hydroxyethyl)piperazine-1-propanesulfonic acid) 49 mM, at pH 8 at 21 °C.In a specific preferred embodiment, the chelating agent is able to reduce the concentration of free calcium ions from 2.0 mM to 0.1 mM when measured in 80 mM potassium chloride and 49 mM EPPS, at pH 8 and 21 °C and using a calcium ion selective electrode for the determination of free calcium concentration, as described in "Materials and Methods".Therefore, preferably, the chelating agents comprise chelating agents capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM to a concentration below 10 mM, preferably below 9.5 mM, preferably below 9.0 mM, preferably below 8.5 mM, preferably below 8.0 mM, preferably below 7.5 mM, preferably below 7.0 mM, preferably below 6.5 mM, preferably below 6.0 mM, preferably below 5.5 mM, preferably below 5.0 mM, preferably below 4.5 mM, preferably below 4.0 mM, preferably below 3.5 mM, preferably below 3.0 mM, preferably below 2.5 mM, preferably below 2.0 mM, preferably below 1.5 mM or preferably below 1 mM, when tested at pH 8.0 and 21°C, as described in "Materials and Methods". In a particularly preferred embodiment, the chelating agents are capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured in 80 mM potassium chloride and 49 mM EPPS at pH 8 and 21 °C to a concentration of 9 mM to 0.5 mM, preferably from 9 mM to 1 mM, preferably from 8 mM to 1 mM, preferably from 7 mM to 1 mM, preferably from 6 mM to 1 mM, preferably from 5 mM to 1 mM, preferably from 4 mM to 1 mM, preferably from 3 mM to 1 mM, preferably from 2 mM to 1 mM, preferably from 9.0 mM to 1.5 mM, preferably from 8.0 mM to 1.5 mM, preferably from 7.0 mM to 1.5 mM, preferably from 6.0 mM to 1.5 mM, preferably from 5.0 mM to 1.5 mM, preferably from 4.0 mM to 1.5 mM, preferably from 3.0 to 1.5 mM, preferably from 2.5 mM to 1.0 mM, preferably from 2.0 mM to 1.1 mM, preferably from 1.85 mM to 1.0 mM. The reduction in the concentration of free calcium ions from 2.0 mM Ca2+ to 0.10 mM corresponds to a reduction in water hardness from 200 ppm (as CaCO3 in the form of Ca(HCO3)2 in the presence of acidic CO2) to 10 ppm. The minimum level of detergency booster additive is calculated based on the sodium salt of the chelating agent relative to 100% dry chelating agent. The chelating effect of the chelating agent can also be measured relative to citrate. The citrate concentration capable of reducing the amount of free calcium ions from 2.0 mM to 0.10 mM is assigned a value of 1, and the results of the chelating agents are compared to this value. The preferred chelating agent according to the invention is capable of reducing the free calcium concentration from 2.0 mM to 0.10 mM to a concentration less than 0.9, such as less than 0.8, less than 0.7, less than 0.6, less than 0.5, less than 0.4, less than 0.3, less than 0.2, and less than 0.1 times lower compared to the citrate concentration, when measured at pH 8.0 and 21 °C.The preferred chelating agent according to the invention is capable of reducing the concentration of free calcium from 2.0 mM to 0.10 mM to a concentration less than 0.9, such as less than 0.8, such as less than 0.7, such as less than 0.6, such as less than 0.5, such as less than 0.4, such as less than 0.3, such as less than 0.2, such as less than 0.1 times lower compared to the citrate concentration, when measured at pH 8.0 at 21 °C using a calcium ion selective electrode for the determination of the free calcium concentration when measured in 80 mM potassium chloride and 49 mM EPPS at 21 °C and pH 8.0. In a particularly preferred embodiment, the chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a chelating agent concentration of less than 1.0 to 0.1, such as less than 0.9 to 0.1, such as less than 0.8 to 0.1, such as less than 0.7 to 0.1, such as less than 0.6 to 0.1, such as less than 0.5 to 0.1, such as less than 0.4 to 0.1, such as less than 0.35 to 0.1, such as less than 0.3 to 0.1 times lower compared to the citrate concentration capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM, when measured at pH 8.0 and 21 °C. A further embodiment of the invention relates to a cleaning composition comprising a variant as defined in the claims of a parental alpha-amylase, wherein the variant alpha-amylase comprises a substitution in one or more positions selected from the group consisting of 193, 195, 197, 198, 200, 203, 206, 210, 212 and 213, using the numbering according to Seq. No. 6, and further comprising at least one chelating agent, wherein said chelating agent at a concentration of less than 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured at 21 °C and pH 8.0; and a cleaning adjuvant. In a preferred embodiment of the invention, the cleaning composition comprises a variant as defined by the claims of a parental alpha-amylase, wherein the variant comprises a substitution at one or more positions in the range of 193 to 213, using the numbering according to Seq. No. 6, and further comprises at least one chelating agent, wherein said chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a chelating agent concentration less than 0.9 times the citrate concentration capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM, when measured at 21 °C and pH 8; and a cleaning adjuvant. Therefore, the chelating agent according to the invention is able to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM, a concentration lower than the citrate concentration required to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM under the same conditions. Alternatively, the strength of the complex formed between the chelating agent and metal ions, such as calcium and / or magnesium, is expressed as the log K value (equilibrium, binding, dissociation, or stability constant). This constant can be measured at a specific pH, temperature, and ionic strength. As mentioned previously, the strength of the complex formed between the chelating agent and the metal ions, for example, calcium and / or magnesium, can be expressed as the log K value (equilibrium, binding, dissociation, or stability constant). This constant can be measured by isothermal titration calorimetry (ITC) as described in A. Nielsen et al., Anal. Biochem. Vol. 314, (2003), pp. 227–234. From the K value, log K can be calculated as the base-10 logarithm of the K value. The log K value measured by this method will depend on the temperature, pH, and ionic strength; therefore, when comparing K values, it is important that they be determined under similar, preferably identical, conditions. Furthermore, introducing a reference standard, such as citrate, can reduce the impact of variations in the experiments. Preferably, log K is determined as described in "Materials and Methods" of this application.Therefore, in one embodiment of the invention, the chelating agent in the composition according to the invention has a log K value of at least 3, such as at least 4, such as at least 5, such as at least 6, such as at least 7, such as at least 8, such as at least 9, such as at least 10, such as at least 11, when log K is measured at pH 10 and 19 °C as described in "Materials and Methods". The log K value of the chelating agent in the compositions according to the invention may also be in the range 3-11, such as 3-10, such as 3-9, such as 3-8, such as 4-11, such as 5-11, such as 6-11, such as 4-10, such as 5-10, such as 4-9, such as 5-9, such as 4-8, especially 5-8.Preferably, the log K of the chelating agent in the composition according to the invention is a factor of at least 1, such as at least 1.33, such as at least 1.67, such as at least 2, such as at least 2.33, such as at least 2.67, such as at least 3, such as at least 3.33, such as at least 3.67 times the log K of citrate determined as described in Example 2b. The chelating agent in the compositions according to the invention can also be in the range of a factor of 1-3, 67, such as 1-3, 33, such as 1-3, 00, such as 1-2, 67, such as 1, 33-3, 67, such as 1, 33-3, 33, such as 1, 33-3, 00, such as 1, 33-2, 67, such as 1, 67-3, 67, such as 1, 67-3, 33, such as 1, 67-3, in particular 1, 67-2, 67 times the log K of citrate determined as described in "Materials and Methods". Useful chelating agents may include, but are not limited to, the following: N-(1,2-dicarboxyethyl)-D,L-aspartic acid (IDS), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), -alanine-N,N-diacetic acid (-ALDA), serine-N, N-diacetic acid (SEDA), isoserine-N, N-diacetic acid (ISDA), phenylalanine-N, N-diacetic acid (PHDA), anthranilic acid-N, N-diacetic acid (ANDA), sulfanilic acid-N, N-diacetic acid (SLDA), taurine-N, N-diacetic acid (TUDA), sulfomethyl-N,N-diacetic acid (SMDA), N-(hydroxyethyl)-ethylidenediaminetriacetate (HEDTA), diethanolglycine (DEG),aminotris (methylenephosphonic acid) (ATMP) ., The preferred chelating agent may contain an amino group and may be, for example, an amino-polycarboxylate or a phosphonate. It may be a monomeric molecule comprising one, two, or three amino groups (typically secondary or tertiary amino groups), and may contain two, three, four, or five carboxyl groups, or even more. Chelating agents may or may not contain phosphorus. There are many ways to group chelating agents; one way is as follows: Chelating agents are, or are based on, carboxylate groups such as EDTA (ethylenediamine tetraacetate), NTA (2,2',2"-nitrilotriacetate), citrate, 2-hydroxypropane-1,2,3-tricarboxylate, DTPA (diethylenetriaminepentaacetic acid), MGDA (methylglycinediacetic acid or NN-bis(carboxymethyl)alanine), EGTA (ethylene glycol tetraacetic acid), EDDS (ethylenediamine-NN-disuccinic acid), GLDA (L-glutamic acid, N,N-diacetic acid), polycarboxylates such as PAA [poly(acrylic acid)], PAA / PMA [copoly(acrylic acid / malic acid)], or mixtures thereof. Chelating agents containing phosphorus can be polyphosphates or phosphonates, such as sodium tripolyphosphate (STP), HEDP (1-hydroxyethylidene-1,1-diphosphonic acid), EDTMP (ethylenediaminetetra(methylenephosphonic acid), EDTMPA (ethylenediaminetetramethylenetetraphosphonic acid), DTPMP (diethylenetriaminepenta(methylenephosphonic acid), DTMPA (diethylenetriaminepenta(methylenephosphonic acid)). Chelating agents can contain nitrogen, as in EDTA, NTA, DTPA, PDTA, GLDA, MGDA, EDDS, EDTMP, EDTMPA, and DTPMP, or ASMA, ASDA, ASMP, IDA, SMAS, SEAS, SMGL, SEGL, MIDA, ALDA, SEDA, ISDA, PHDA, ANDA, SLDA, TUDA, SMDA. HEDTA, DEG, ATMP, or mixtures thereof. Therefore, preferred chelating agents may include, but are not limited to, the following: ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentamethylenephosphonic acid (DTMPA, DTPMP), hydroxyethanediphosphonic acid (HEDP), ethylenediamine N,N'-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), diethylenetriaminepentacetic acid (DTPA), propylendiaminetetraacetic acid (PDTA), 2-hydroxypyridin-N-oxide (HPNO), ethylglycinediacetic acid (MGDA), glutamic acid, N,N-diacetic acid (N,N-dicarboxymethyl glutamic acid tetrasodium salt (GLDA)), and nitrilotriacetic acid (NTA), or mixtures thereof. The chelating agents may be present in their acid form or as a salt. Preferably, the chelating agents may be present as sodium, ammonium, or potassium salts. The chelating agent may be present in the composition in an amount of 0.0001% by weight to 20% by weight, preferably 0.01 to 10% by weight, more preferably 0.1 to 5% by weight. Parental alpha-amylase: In principle, parental alpha-amylase can be any alpha-amylase for which a variant with improved stability during storage or use is desired, for example, during washing or in a starch hydrolysis process. Therefore, improved stability can be observed as a reduced loss of amylolytic activity during storage or as increased activity and performance during use. Known alpha-amylases are derived from a wide range of organisms, including bacteria, such as those from species of the genus Bacillus, for example, Bacillus licheniformis; fungal species, such as Aspergillus oryzae (TAKA-amylase) or Aspergillus niger; plants, such as barley; and mammals. Parental alpha-amylase can, in principle, be any alpha-amylase regardless of its origin.According to the present invention, the parental alpha-amylase is an alpha-amylase having the amino acid sequence shown in Seq. No. 6. It is well known that a number of alpha-amylases produced by Bacillus spp. are highly identical at the amino acid level. Due to the substantial identity found among these alpha-amylases, they are considered to belong to the same class of alpha-amylases, specifically the "Termamyl-type alpha-amylases" class. Therefore, in the present context, the term "Termamyl-like alpha-amylase" means an alpha-amylase, especially Bacillus alpha-amylase, which, at the amino acid level, has substantial identity, i.e., at least 60%, with the alpha-amylase from B. licheniformis having the amino acid sequence shown in Section Id. No. 20 (Termamyl™), in the present specification. Termamyl-type alpha-amylases Table 1 below shows the identity of a number of known Bacillus alpha-amylases: Table 1 For example, the alpha-amylase from B. licheniformis comprising the amino acid sequence shown in Seq. Id. No. 20 (commercially available as Termamyl™) has been found to be approximately 81% homologous to the alpha-amylase from B. amyloliquefaciens comprising the amino acid sequence shown in Seq. Id. No. 14 (BAN) and approximately 65% ​​homologous to the alpha-amylase from B. stearothermophilus comprising the amino acid sequence shown in Seq. Id. No. 16 (BSG). Other homologous alpha-amylases include SP722 and SP690 described in WO 95 / 26397 and further represented in Seq. Id. No. 6 and Seq. Id. No. 7. No. 12, respectively, in the present report. Other amylases are alpha-amylase AA560 derived from Bacillus sp. and shown in section Id. No. 10, and alpha-amylase SP707 or No. 707 derived from Bacillus sp., shown in section Id. No. 8 and described by Tsukamoto et al., Biochemical and Biophysical Research Communications, 151 (1988) , pp. 25-31. Another homolog is the alpha-amylase KSM AP1378 described in id. of sec. n.o 18 en WO 97 / 00324 (of KAO Corporation) . Another additional homolog is SPO.7-7 with the id. of sec. No. 22. Another suitable original amylase is Id. of sec. n.°: 2 of K 38 or the amylase of B.circulans with the Id. of sec. n.°: 4 and the Id. of sec. n.°: 24, described in W02005 / 001064. Other interesting alpha-amylases include the alpha-amylase produced by the B. licheniformis strain described in EP 0252666 (ATCC 27811), and the alpha-amylases identified in WO 91 / 00353 and WO 94 / 18314. Other commercial alpha-amylases of the Termamyl type are included in products sold under the following trade names: Optitherm™ and Takatherm™ (Solvay); Maxamyl™ (marketed by Gist-brocades / Genencor), Spezym AA™ and Spezyme Delta AA™ (marketed by Genencor), and Keistase™ (marketed by Daiwa), Dex lo, GC 521 (marketed by Genencor) and Ultraphlow (from Enzyme Biosystems), Purastar™ ST 5000E, PURASTRA™ HPAM L, POWERASE™, Spezyme FRED, GC358, ClearFlow AA (from Danisco.), or alpha-amylase TS-23 (Seq. Id. No.: 26 (Lin et al., J.App.Microbiol.1997, 82, 325-334). Non-Termamyl-type alpha-amylase can be, for example, a fungal alpha-amylase, a mammalian or plant alpha-amylase, or a bacterial alpha-amylase (other than a Termamyl-type alpha-amylase). Specific examples of such alpha-amylases include TAKA alpha-amylase from Aspergillus oryzae, acid alpha-amylase from A. niger, alpha-amylase from Bacillus subtilis, porcine pancreatic alpha-amylase, and a barley alpha-amylase. All of these alpha-amylases have elucidated structures that are markedly different from the structure of a typical Termamyl-type alpha-amylase, as discussed herein. The fungal alpha-amylases mentioned above, that is, those obtained from A. niger and A. oryzae, are highly identical at the amino acid level and are generally considered to belong to the same alpha-amylase family. The fungal alpha-amylase derived from Aspergillus oryzae is marketed under the trade name Fungamyl™. As described in the present memory, the parental alpha-amylases have an amino acid sequence that differs (for example, by insertion or substitution) in one or more amino acids, preferably in ten amino acids, more preferably in nine, eight, seven, six, preferably in five amino acids, more preferably in four amino acids, even more preferably in three amino acids, with maximum preference in two amino acids, and even with maximum preference in one amino acid with respect to the mature polypeptide of Id. of sec. no. 6. The parental alpha-amylase may be an alpha-amylase that exhibits immunological cross-reactivity with an antibody against an alpha-amylase having one of the amino acid sequences selected from the group consisting of sec. no. 6. In a preferred embodiment, the parental alpha-amylase is one in which the antibody against the parental alpha-amylase exhibits an affinity or avidity for an alpha-amylase having one of the amino acid sequences shown in sec. no. 6 in a competitive assay technique such as, for example, ELISA or BiaCore, respectively, or exhibits affinity or avidity comparable to that of the parental alpha-amylase, and in which the antibody against the alpha-amylase having one of the amino acid sequences shown in sec. no. 6°: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24 or 26 exhibits in said competitive assay technique an affinity or avidity for the parental alpha-amylase comparable to the affinity or avidity for the alpha-amylase having one of the amino acid sequences shown in Seq. ID No. 6. In other embodiments, the parental alpha-amylase is one having an affinity or avidity that is at least 70%, preferably at least 75%, preferably at least 80%, preferably at least 85%, preferably at least 90%, preferably at least 95%, preferably at least 100%, preferably at least 110%, preferably at least 120%, especially preferably at least 125% of the affinity or avidity of the alpha-amylase having one of the amino acid sequences shown in Seq. ID No. 6. No.: 6. The parental alpha-amylase may also be an alpha-amylase encoded by a DNA sequence that hybridizes with the DNA sequence encoding the alpha-amylases specified above, which are evident from Section ID No. 6 of this application. Therefore, this specification describes a variant alpha-amylase of a parental alpha-amylase, wherein the parental alpha-amylase: (A) is obtained from a strain of B. licheniformis, Bacillus sp. or KSM API378; (B) is selected from the group having amino acid sequences as shown in the Seq. ID No.: 6; In one respect, the parental polypeptide having amylolytic enhancement activity is a polypeptide comprising an amino acid sequence having at least 60% identity with the mature polypeptide of Id. sec. no. 6; When a particular variant of a parental alpha-amylase is (conventionally) referred to as referring to the modification (e.g., deletion or substitution) of specific amino acid residues in the amino acid sequence of a specific alpha-amylase, it should be understood that variants of another alpha-amylase modified at the equivalent position or positions (as determined from the best possible alignment of amino acid sequences between the respective amino acid sequences) are thereby encompassed. In one particular aspect of the invention, the parental alpha-amylase is a variant of a naturally occurring alpha-amylase prepared by any suitable means. For example, the parental alpha-amylase may be a variant of a naturally occurring alpha-amylase that has been modified or altered in its amino acid sequence. The parental alpha-amylase may be a substantially homologous parental alpha-amylase that may have one or more (several) amino acid substitutions, deletions, and / or insertions. These changes are preferably inority in nature, i.e., conservative amino acid substitutions as described below and other substitutions that do not significantly affect the three-dimensional folding or activity of the protein or polypeptide; small deletions, typically of one to approximately 30 amino acids; and small amino-terminal or carboxy-terminal extensions, such as an amino-terminal methionine residue, a small linking peptide of up to approximately 20-25 residues, or a small extension that facilitates purification (an affinity tag), such as a polyhistidine tail, or protein A (Nilsson et al., 1985, EMBO J. 4: 1075; Nilsson et al., 1991, Methods Enzymol.198: 3. See also, in general, Ford et al., 1991, Protein Expression and Purification 2: 95-107. Although the changes described above are preferably minor in nature, these changes can also be substantial, such as the fusion of larger polypeptides of up to 300 amino acids or more as amino-terminal or carboxy-terminal extensions. When a particular variant of a parental alpha-amylase (variant of the invention) is referred to (conventionally) as referring to the modification (e.g., deletion or substitution) of specific amino acid residues in the amino acid sequence of a specific parental alpha-amylase, it should be understood that variants of another parental alpha-amylase modified at the equivalent position or positions (as determined from the best possible alignment of amino acid sequences between the respective amino acid sequences) are thereby encompassed. Homology (sequence identity) Homology can be determined as the degree of identity between two sequences, indicating that the first sequence is derived from the second. For the purposes of the present invention, the degree of sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970 J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 3.0.0 or higher. The optional parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 substitution matrix (the EMBOSS version of BLOSUM62). The Needle output labeled as "highest identity" (obtained using the -nobrief option) is used as the percentage identity and is calculated as follows: (Identical residues x 100) / (Alignment length - Total number of gaps in the alignment) For the purposes of the present invention, the degree of sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, mentioned above) as applied in the Needle program of the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, mentioned above), preferably version 3.0.0 or later. The optional parameters used have a gap opening penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL substitution matrix (EMBOSS version of NCBI NUC4.4). The Needle result labeled "highest identity" (obtained using the "nobrief" option) is used as the percent identity and is calculated as follows: (Identical deoxyribonucleotides x 100) / (Alignment length - Total number of gaps in the alignment) Sequence homology or identity can also be determined as the degree of identity between two sequences, indicating that the first sequence is derived from the second. Homology can be adequately determined using software programs known in the field, such as GAP, provided in the GCG software package. Therefore, Gap GCGv8 can be used with the default scoring matrix for identity and the following default parameters: a gap introduction penalty of 5, 0, and a gap extension penalty of 0, 3, respectively, for nucleic acid sequence comparisons, and a gap introduction penalty of 3, 0, and a gap extension penalty of 0, 1, respectively, for protein sequence comparisons.GAP uses the method of Needleman and Wunsch, (1970), J.Mol. Biol. 48, pp.443-453, to make alignments and to calculate the identity. A structural alignment between, for example, Termamyl and an alpha-amylase can be used to identify equivalent / corresponding positions in other alpha-amylases. One method for obtaining such structural alignment is to use the Pile Up program of the GCG software package using default gap penalty values, i.e., a gap introduction penalty of 3, 0 and a gap extension penalty of 0, 1. Other structural alignment methods include hydrophobic cluster analysis (Gaboriaud et al., (1987), FEBS LETTERS 224, pp. 149-155) and reverse chain formation (Huber, T; Torda, AE, PROTEIN SCIENCE vol. 7, no. 1 pp. 142-149 (1998)). The properties of alpha-amylases, i.e., immunological cross-reactivity, can be analyzed using an antibody against, or reactive with, at least one epitope of the relevant Termamyl-type alpha-amylase.The antibody, which can be monoclonal or polyclonal, can be produced using methods known in the art, for example, as described by Hudson et al., Practical Immunology, third edition (1989), Blackwell Scientific Publications. Cross-reactivity can be determined using assays known in the art, such as Western blot or radial immunodiffusion, as described by Hudson et al., 1989. Methods for preparing alpha-amylase variants Several methods for introducing mutations into genes are known in this technique. After a brief description of cloning DNA sequences encoding alpha-amylase, methods for generating mutations at specific sites within the alpha-amylase coding sequence will be described. Cloning a DNA sequence that codes for an alpha-amylase The DNA sequence encoding a parental alpha-amylase can be isolated from any cell or microorganism that produces the alpha-amylase in question, using various well-established methods. First, a genomic DNA and / or cDNA library must be constructed using chromosomal DNA or messenger RNA from the organism that produces the alpha-amylase under study. Then, if the amino acid sequence of the alpha-amylase is known, known homologous, labeled oligonucleotide probes can be synthesized to identify alpha-amylase-encoding clones from a library prepared from the organism in question. Alternatively, a labeled oligonucleotide probe containing sequences homologous to a known alpha-amylase gene could be used to identify alpha-amylase-encoding clones, using low-restriction hybridization and washing conditions. Another method for identifying clones that encode alpha-amylase would involve inserting fragments of genomic DNA into an expression vector, such as a plasmid, transforming alpha-amylase-negative bacteria with the resulting DNA library, and then placing the transformed bacteria on agar containing a substrate for alpha-amylase, thereby allowing the identification of clones that express alpha-amylase. Alternatively, the DNA sequence encoding the enzyme can be prepared synthetically using established standard methods, e.g., the phosphoramidite method described by SL Beaucage and MH Caruthers, (1981) Tetrahedron Letters 22: 1859 or the method described by Matthes et al. (1984), EMBO J.380.- 805. In the phosphoramidite method, oligonucleotides are synthesized, e.g., in an automated DNA synthesizer, purified, paired, ligated, and cloned into suitable vectors. Finally, the DNA sequence can be of mixed genomic and synthetic origin, of mixed synthetic and cDNA origin, or of mixed genomic and cDNA origin, prepared by ligating fragments of synthetic, genomic, or cDNA origin (as appropriate, fragments corresponding to various parts of the complete DNA sequence), according to standard techniques. The DNA sequence can also be prepared by polymerase chain reaction (PCR) using specific primers, for example, as described in US patent 4,683,202 or in R.K. Isolauri et al. (1988), Science vol. 239, 4839, pp. 487–491. Site-directed mutagenesis Once a DNA sequence encoding alpha-amylase has been isolated and desirable mutation sites have been identified, mutations can be introduced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites; the mutant nucleotides are inserted during oligonucleotide synthesis. In one specific method, a single-stranded DNA gap, bridging the alpha-amylase-coding sequence, is created in a vector carrying the alpha-amylase gene. The synthetic nucleotide containing the desired mutation is then paired with a homologous portion of the single-stranded DNA. The remaining gap is then filled with DNA polymerase I (Klenow fragment), and the construct is ligated using T4 ligase. A specific example of this method is described in Morinaga et al. 1984 Biotechnology 2, pp. 636–639. In US-4,760.Section 025 describes the introduction of oligonucleotides encoding multiple mutations by making minor alterations to the cassette. However, an even wider variety of mutations can be introduced at any time using the Morinaga method, because a multitude of oligonucleotides of varying lengths can be introduced. Another method for introducing mutations into DNA sequences encoding alpha-amylase is described in Nelson and Long (1989). This involves the three-step generation of a PCR fragment containing the desired mutation, using a chemically synthesized DNA strand as one of the primers in the PCR reactions. From the PCR-generated fragment, a DNA fragment carrying the mutation can be isolated by cleaving it with restriction endonucleases and reinserted into an expression plasmid. Random mutagenesis Random mutagenesis is properly performed as localized or region-specific random mutagenesis in at least three parts of the gene that translates to the amino acid sequence shown in question, or within the entire gene. Random mutagenesis of a DNA sequence encoding a parental alpha-amylase can be conveniently performed using any method known in the technique. In relation to the foregoing, an additional aspect of the present invention relates to a method for generating a variant of a parental alpha-amylase, for example, wherein the variant has an altered starch affinity with respect to the parental one, the method comprising: (a) subjecting a DNA sequence encoding the original alpha-amylase to random mutagenesis, (b) express the mutated DNA sequence obtained in step (a) in a host cell, and (c) drying host cells that express an alpha-amylase variant that has an altered affinity for starch with respect to the original alpha-amylase. Step (a) of the preceding method of the invention is preferably carried out using doped primers. For example, random mutagenesis can be performed by using a physical or chemical mutagenic agent, by using a suitable oligonucleotide, or by subjecting the DNA sequence to PCR-induced mutagenesis. Furthermore, random mutagenesis can be performed by using any combination of these mutagenic agents. The mutagenic agent can be, for example, an agent that induces transitions, transversions, inversions, mixing, deletions, and / or insertions. Examples of a suitable physical or chemical mutagenic agent for the present purpose include ultraviolet (UV) irradiation, hydroxylamine, N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), O-methyl-hydroxylamine, nitrous acid, ethylmethanesulfonate (EMS), sodium bisulfite, formic acid, and nucleotide analogues. When such agents are used, mutagenesis is typically carried out by incubating the DNA sequence encoding the parental enzyme to be mutagenized in the presence of the chosen mutagenic agent under conditions suitable for mutagenesis, and selecting the mutated DNA that has the desired properties. When mutagenesis is carried out using an oligonucleotide, the oligonucleotide may be doped or supplemented with the three non-parental nucleotides during oligonucleotide synthesis at the positions to be changed. Doping or supplementation may be done in such a way as to avoid codons for undesired amino acids.The doped or supplemented oligonucleotide can be incorporated into the DNA encoding the alpha-amylase enzyme using any published technique, for example, PCR, LCR, or any DNA polymerase and ligase, as deemed appropriate. Preferably, doping is carried out using constant random doping, in which the percentage of the natural strain and the mutation at each position is predefined. Furthermore, doping can be directed to a preference for the introduction of certain nucleotides and, thus, a preference for the introduction of one or more specific amino acid residues. Doping can be done, for example, to allow the introduction of 90% of the natural strain and 10% of the mutation at each position. An additional consideration in selecting a doping scheme is based on the genetic and structural constraints of the protein.The doping scheme can be carried out using the DOPE program, which, among other things, ensures that the introduction of stop codons is avoided. When using PCR-generated mutagenesis, either a chemically treated or untreated gene encoding a parental alpha-amylase is PCR-treated under conditions that increase erroneous nucleotide incorporation (Deshler 1992, Genetic Analysis: Biomolecular Engineering, 9 (4), pp. 103-106; Leung et al., 1989 Technique, vol. 1, pp. 11-15). A mutator strain of E. coli (Fowler et al., 1974, Molec. Gen. Genet., 133, pp.17.- 191), S. cerevisiae or any other microbial organism can be used for random mutagenesis of DNA encoding alpha-amylase by, for example, transforming a plasmid containing the original glycosidase into the mutant strain, growing the mutant strain with the plasmid and isolating the mutated plasmid from the mutant strain.The mutated plasmid can be subsequently transformed into the expression organism. The DNA sequence to be mutagenic may conveniently be present in a cDNA library prepared from an organism expressing the parental alpha-amylase. Alternatively, the DNA sequence may be present in a suitable vector, such as a plasmid or a bacteriophage, which can then be incubated with, or otherwise exposed to, the mutagenic agent. The DNA to be mutagenized may also be present in a host cell, either integrated into the cell's genome or contained in a vector. Finally, the DNA to be mutagenized may be in isolated form. It is understood that the DNA sequence to be randomly mutagenic is preferably a cDNA or a genomic DNA sequence.In some cases, it may be convenient to amplify the mutated DNA sequence before carrying out the expression step (b) or the analysis step (c). Such amplification can be performed using methods known to the art, with PCR amplification using oligonucleotide primers prepared based on the DNA or amino acid sequence of the parental enzyme being the currently preferred method. After incubation with, or exposure to, the mutagenic agent, the mutated DNA is expressed by culturing a suitable host cell carrying the DNA sequence under conditions that allow expression to occur. The host cell used for this purpose can be one that has been transformed with the mutated DNA sequence, optionally present in a vector, or one that carried the DNA sequence encoding the parental enzyme during the mutagenesis treatment.Examples of suitable host cells are as follows: gram-positive bacteria such as Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaens, Bacillus collus, Bacillus collus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, Streptomyces lividans or Streptomyces murinus; and gram-negative bacteria, such as E. coli. The mutated DNA sequence may further comprise a DNA sequence encoding functions that permit expression of the mutated DNA sequence. Localized random mutagenesis Random mutagenesis can be favorably localized to a portion of the parental alpha-amylase in question. This can be advantageous, for example, when certain regions of the enzyme have been identified as particularly important for a specific property of the enzyme, and modifying them is expected to yield a variant with improved properties. Such regions can typically be identified once the tertiary structure of the parental enzyme has been elucidated and is related to the enzyme's function. Localized or region-specific random mutagenesis is conveniently carried out using PCR-generated mutagenesis techniques as described above or any other suitable technique known to the art. Alternatively, the DNA sequence encoding the portion of the DNA sequence to be modified can be isolated, for example, by insertion into a suitable vector, and this portion can then be mutagenic using any of the mutagenesis methods described above. Alternative methods for providing alpha-amylase variants Alternative methods for providing variants of the invention include the gene transposition method known in the art, including the methods, for example, described in WO 95 / 22625 (from Affymax Technologies NV) and WO 96 / 00343 (from Novo Nordisk A / S). Expression of alpha-amylase variants According to the invention, a DNA sequence encoding the variant produced by the methods described above, or by any alternative method known in the art, can be expressed, in enzyme form, using an expression vector that typically includes control sequences encoding a promoter, operator, ribosome binding site, translation start signal, and, optionally, a repressor gene or various activator genes. The recombinant expression vector carrying the DNA sequence encoding an alpha-amylase variant of the invention can be any vector suitable for recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced. Therefore, the vector can be a self-replicating vector, that is, a vector that exists as an extrachromosomal entity, whose replication is independent of chromosomal replication, for example, a plasmid, a bacteriophage, or an extrachromosomal element, a minichromosome, or an artificial chromosome. Alternatively, the vector can be one that, when introduced into a host cell, integrates into the host cell's genome and replicates along with the chromosome(s) into which it has been integrated. In the vector, the DNA sequence must be operationally linked to a suitable promoter sequence. The promoter can be any DNA sequence that exhibits transcriptional activity in the chosen host cell and can be obtained from genes encoding homologous or heterologous proteins for the host cell. Examples of suitable promoters for directing transcription of the DNA sequence encoding an alpha-amylase variant of the invention, especially in a bacterial host, include the E. coli lac operon promoter, the Streptomyces coelicolor agarase dagA gene promoter, the Bacillus licheniformis alpha-amylase (amyL) gene promoter, the Bacillus stearothermophilus maltogenic amylase (amyM) gene promoter, the Bacillus amyloliquefaciens alpha-amylase (amyQ) gene promoter, the Bacillus subtilis xylA and xylB gene promoter, and so on.For transcription in a fungal host, examples of useful promoters are those obtained from the gene encoding TAKA amylase from A. or and zae, aspartic proteinase from Rhizomucor miehei, neutral alpha-amylase from A. niger, acid-stable alpha-amylase from A. niger, glucoamylase from A. niger, lipase from Rhizomucor miehei, alkaline protease from A. or and zae, triose phosphate isomerase from A. or and zae, or acetamidase from A. nidulans. The expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, polyadenylation sequences operatively connected to the DNA sequence encoding the alpha-amylase variant of the invention. The termination and polyadenylation sequences may be suitably obtained from the same sources as the promoter. The vector may also comprise a DNA sequence that allows the vector to replicate in the host cell in question. Examples of such sequences are the origins of replication of the plasmids pUC19, pACYC177, pUB110, pE194, pAMB1, and pIJ702. The vector may also comprise a selectable marker, for example, a gene whose product complements a defect in the host cell, such as the dal genes of B. subtilis or B. licheniformis, or one that confers antibiotic resistance, such as resistance to ampicillin, kanamycin, chloramphenicol, or tetracycline. Furthermore, the vector may comprise Aspergillus selection markers such as amdS, argB, niaD, and sC, a marker that confers hygromycin resistance, or selection may be achieved by cotransformation, for example, as described in WO 91 / 17243. Although intracellular expression can be advantageous in some respects, for example, when certain bacteria are used as host cells, extracellular expression is generally preferred. In general, the Bacillus alpha-amylases mentioned herein comprise a preregion that allows the secretion of the expressed protease into the culture medium. If desired, this preregion can be replaced by a different preregion or signal sequence obtained by substituting the DNA sequences encoding the respective preregions. The procedures used to ligate the DNA construct of the invention encoding an alpha-amylase variant, the promoter, the terminator, and other elements, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to those skilled in the art (see, for example, Sambrook et al., Molecular Cloning: A Laboratory and Manual, 2nd ed., Cold Spring Harbor, 1989). A cell comprising a DNA construct or an expression vector, as defined above, is advantageously used as a host cell in the recombinant production of an alpha-amylase variant for use in the invention. The cell can be conveniently transformed with the DNA construct of the present invention, which encodes the variant, by integrating the DNA construct (in one or more copies) into the host chromosome. This integration is generally considered advantageous because the DNA sequence is more likely to be stably maintained in the cell. The integration of the DNA constructs into the host chromosome can be carried out using conventional methods, for example, by homologous or heterologous recombination. Alternatively, the cell can be transformed with an expression vector as described above in relation to different host cell types. The cell can be a cell from a higher organism, such as a mammal or an insect, but preferably it is a microbial cell, for example, a bacterial or fungal cell (including yeasts). Examples of suitable bacteria are gram-positive bacteria such as Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, or Streptomyces lividans or Streptomyces murinus, or gram-negative bacteria, such as E. coli. Transformation of bacteria can be carried out, for example, by protoplast transformation or by using competent cells in a manner known per se. The yeast organism can be favorably selected from a species of Saccharomyces or Schizosaccharomyces, for example, Saccharomyces cerevisiae. The filamentous fungus can advantageously belong to a species of Aspergillus, for example, Aspergillus oryzae or Aspergillus niger. The fungal cells can be transformed by a process involving protoplast formation and transformation followed by cell wall regeneration in a manner known per se. A suitable procedure for the transformation of Aspergillus host cells is described in EP 238023. A suitable method for producing an alpha-amylase variant for use in the invention comprises culturing a host cell in the manner described above under conditions favorable for the production of the variant and recovering the variant from the cells and / or culture medium. The medium used to culture the cells may be any conventional medium suitable for culturing the host cell in question and obtaining expression of the alpha-amylase variant of the invention. Suitable media are commercially available from suppliers or may be prepared according to published recipes (e.g., as described in the American Type Culture Collection catalogs). The alpha-amylase variant secreted by host cells can be conveniently recovered from the culture medium using well-known procedures that include separating the cells from the medium by centrifugation or filtration, and precipitating the protein components from the medium using a salt such as ammonium sulfate, followed by chromatographic procedures such as ion-exchange chromatography, affinity chromatography, or similar techniques. Conventions for variant designation Using the numbering system that originates from the amino acid sequence of alpha-amylase described in Seq. No. 6 aligned with the amino acid sequence of a number of other alpha-amylases, it is possible to indicate the position of an amino acid residue in an alpha-amylase in regions of structural homology. In describing the various alpha-amylase variants of the present invention, the nomenclature described below has been adapted for ease of reference. In all cases, the single-letter or triplet amino acid abbreviation accepted by the IUPAC is used. In this specification and claims, conventional one-letter and three-letter codes are used for amino acid residues. For ease of reference, the alpha-amylase variants of the invention are described using the following nomenclature: Original amino acid(s): position(s): of the substituted amino acid(s). According to this nomenclature, for example, the substitution of alanine by asparagine at position 30 is shown as: Ala30Asn or A30N An alanine deletion at the same position is shown as: A30* or A30* and the insertion of an additional amino acid residue after position 30, such as lysine, is shown as: Ala30AlaLys or A30AK A deletion of a consecutive sequence of amino acid residues, such as amino acid residues 30-33, is indicated as (30-33)* or (A30-N33). The deletion of a single amino acid residue can be described simply as 30*. When a specific alpha-amylase contains a "deletion" compared to other alpha-amylases and an insertion is made at that position, this is indicated as: *36Asp or *36D for the insertion of an aspartic acid at position 36. Multiple mutations can be separated by plus signs or a space, that is: Ala30Asn + Glu34Ser or A30N+E34S Ala30Asn Glu34Ser or A3ONE34S which represent mutations at positions 30 and 34 that replace alanine and glutamic acid with asparagine and serine, respectively. Alternatively, multiple mutations can be separated by commas or semicolons, i.e.: Ala30Asn, Glu34Ser or A30N, E34S Even more simplified multiple mutations can be separated by a space, for example, Ala30Asn Glu34Ser or A30NE34S Alternatively, multiple mutations can be separated by commas or semicolons. When one or more alternative amino acid residues can be inserted at a given position, it is indicated as A30N, E or A30N or A30E Alternatively, one or more alternative amino acid residues may be inserted at a given position; this is indicated as: A30 [N, E] or A30 [NE], alternatively A30 {N, E} or A30 (NE} For simplicity, the alternative amino acid that could be substituted at a given position can be indicated as: A30 N, E, H, L or V Furthermore, when a suitable position for modification is identified herein without any specific modification being suggested, it should be understood that any amino acid residue may be substituted for the amino acid residue present at that position. Therefore, for example, when a modification of alanine at position 30 is mentioned but not specified, it should be understood that the alanine may be removed or substituted by any other amino acid, i.e., any of the following: R, N, D, A, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, V. Furthermore, "A30X" means any of the following substitutions: A30R, A30N, A30D, A30C, A30Q, A30E, A30G, A30H, A30I, A30L, A30K, A30M, A30F, A30P, A30S, A30T, A30W, A30Y, or A30 V; abbreviated: A30R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, V. Or, for example, A30 [R, N, D, C, Q, E, G, H, I, L, K, M, F, P, S, T, W, Y, V] An expert in the technique would know that using a numbering system, for example, according to seq. id. no. 6, means using seq. id. no. to counteract, not that the parental enzyme is necessarily seq. id. no. 6, but simply that the positions to be altered are defined according to seq. id. no. 6. Therefore, another way to describe specific substitutions is to indicate the amino acid to be altered with an X. Thus, X30N means that any amino acid present at position 30 could be substituted by N, indicating that a different alpha-amylase can be used as the parental alpha-amylase. Therefore, the nomenclature "X30N" or "X30V" means that any amino acid that can be in position 30 in the parental alpha-amylase is substituted by an asparagine or a valine. Characteristics of amino acid residues Charged amino acids: Asp, Glu, Arg, Lys, His Negatively charged amino acids (with the most negative residue first): Asp, Glu Positively charged amino acids (with the most positive residue first): Arg, Lys, His Neutral amino acids: Gly, Ala, Val, Leu, Ile, Phe, Tyr, Trp, Met, Cys, Asn, Gin, Ser, Thr, Pro Hydrophobic amino acid residues (with the most hydrophobic residue listed last): Gly, Ala, Val, Pro, Met, Leu, Ile, Tyr, Phe, Trp, Hydrophobic amino acids (with the most hydrophobic residue listed last): Thr, Ser, Cys, Gin, Asn This nomenclature is particularly relevant for modifications that involve substituting, inserting, or deleting amino acid residues that share specific common properties. Such modifications are referred to as conservative amino acid modifications. Examples of conservative modifications include basic amino acids (arginine, lysine, and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, and valine), aromatic amino acids (phenylalanine, tryptophan, and tyrosine), and small amino acids (glycine, alanine, serine, threonine, and methionine). Amino acid modifications that generally do not alter specific activity are known in the art and have been described, for example, by H. Neurath and R.L. Hill, 1979, in The Proteins, Academic Press, New York.The exchanges that take place most frequently are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly and the reverses (Taylor, 1986, Journal of Theoretical Biology 119: 205-218. Useful variants in the invention Preferred variants comprise an alteration or alterations in one or more, or one or more amino acid residues in the region 193 to 213 of the parental alpha-amylase. In a particularly preferred embodiment of the variant comprising at least one, at least two, or at least three deletions in the amino acid region 181, 182, 183, or 184 and further an alteration in one or more, or one or more amino acid residues in the region 193 to 213, wherein the numbering corresponds to the mature polypeptide of Seq. No. 6, i.e., using the numbering according to Seq. No. 6. The inventors have discovered that these alterations provide variants that have greater stability in compositions comprising a chelating agent, especially when the chelating agents are capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM to a concentration below 10 mM, preferably below 9.5 mM, preferably below 9.0 mM.preferably less than 8.5 mM, preferably less than 8.0 mM, preferably less than 7.5 mM, preferably less than 7.0 mM, preferably less than 6.5 mM, preferably less than 6.0 mM, preferably less than 5.5 mM, preferably less than 5.0 mM, preferably less than 4.5 mM, less than 4.0 mM, preferably less than 3.5 mM, preferably less than 3.0 mM, preferably less than 2.5 mM, preferably less than 2.0 mM, preferably less than 1.5 mM or preferably less than 1 mM, when measured at 21 °C and pH 8.0, as described later in "Materials and Methods". A first aspect of the invention relates to a cleaning composition according to claim 1. The cleaning composition comprises a variant, as defined in the claims, of a parental alpha-amylase, wherein the parental alpha-amylase is an alpha-amylase having the amino acid sequence shown in sec. 6 and the variant has amylolytic activity. The variant has the sequence shown in sec. 6 with one of the sets of mutations listed in claim 1. The composition further comprises at least one cleaning adjuvant and at least one chelating agent, wherein said chelating agent at a concentration of less than 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured at 21 °C and pH 8.0. Also described herein is a cleaning composition comprising a variant as defined in the claims of a parental alpha-amylase, wherein the variant comprises a substitution in one or more positions in the range of 193 to 213, using the numbering according to Section Id. No. 6, and optionally further comprising at least one chelating agent, wherein said chelating agent at a concentration of less than 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured at 21 °C and pH 8.0, and a cleaning adjuvant. A second aspect provides a method of washing clothes, comprising washing a garment with a composition according to the first aspect of the invention, preferably at a temperature of 30 °C or less, or more preferably, at a temperature of 20 °C or less. The cleaning composition of the present invention comprises a chelating agent at a concentration of less than 10 mM that is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured in 80 mM potassium chloride and 49 mM EPPS at 21 °C and pH 8.0. This document also describes a cleaning composition, in which the chelating agent at a concentration of less than 10 mM is able to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured in the test described in "Materials and Methods". Therefore, in a preferred aspect of the invention, the variant comprises at least one substitution, as defined in claim 1, at one or more positions in the range corresponding to positions 193 to 213 of the mature polypeptide of sec. no. 6. The terms "using the numbering according to" or "corresponding to" refer to the numbering system used in this application, and the two expressions are used interchangeably herein. Therefore, position 195 is the amino acid corresponding to position 195 in sec. no. 6. It is therefore understood that variants of other parental alpha-amylases modified at the equivalent position or positions (as determined from the best possible alignment of amino acid sequences between the respective amino acid sequences) are thus encompassed. Where deletions are present, counting is carried out as if no deletions were present. Preferably, variants comprising alterations in one or more of the above-identified positions have greater stability in detergent, preferably in liquid detergent, compared to the parental alpha-amylase. The inventors have discovered that these variants have improved stability compared to the parental alpha-amylase in compositions comprising a chelating agent, wherein said chelating agent at a concentration below 10 mM is able to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM, at 21 °C and pH 8.0, as described in "Materials and Methods". Also described, but not forming part of the claimed invention, is a method for preparing a polypeptide comprising: (a) provide an amino acid sequence of a parental polypeptide having amylase activity; (b) select one or more amino acids occupying one or more positions corresponding to positions 195, 197, 198, 200, 203, 206, 210, 212, 213, 243 and also select one or more positions corresponding to positions 116, 118, 129, 133, 134, 142, 146, 147, 149, 151, 152, 169, 174, 186, 235, 244, 303, 320, 339, 359, 418, 431, 434, 447, 458 of the mature polypeptide of Id. of sec. no.: 6; (c) modify the sequence by substituting or removing the selected amino acid residue or by inserting one or more amino acid residues downstream and adjacent to the selected amino acid residue; (d) produce a variant polypeptide having the modified sequence; (e) test the variant polypeptide for amylase activity and stability; and (f) Selecting a variant polypeptide having amylase activity and greater stability relative to the original polypeptide in the presence of a chelating agent wherein said chelating agent at a concentration below 10 mM is able to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM at 21 °C and pH 8.0. Preferably, the variants comprise alterations in three positions, more preferably four positions, even more preferably five positions, and most preferably six positions. In a particularly preferred embodiment, the variant comprises at least one, at least two, or at least three deletions in the amino acid region of 181, 182, 183, or 184 and furthermore one or more substitutions in one or more positions corresponding to positions in the original alpha-amylase selected from the group consisting of 193, 195, 197, 198, 200, 203, 206, 210, 212, 213, 243 (using the numbering according to Seq. No. 6). Therefore, a preferred aspect relates to a variant of an original alpha-amylase comprising at least one, at least two, or at least three deletions in the amino acid region of 181, 182, 183, or 184, an alteration in one or more positions selected from the group consisting of 195, 197, 198, 200, 203, 206, 210, 212, 213, 243, and further comprising an alteration in one or more positions selected from the group consisting of 116, 118, 129, 133, 134, 142, 146, 147, 149, 151, 152, 169, 174, 186, 235, 244, 303, 320, 339, 359, 418, 431, 434, 447, 458, where (a) the alteration / alterations is / are independently (i) an insertion of an amino acid immediately downstream and adjacent to the position, (ii) a deletion of the amino acid occupying the position, and / or (iii) a substitution of the amino acid occupying the position, (b) the variant has alpha-amylase activity; and (c) each position corresponds to a position in the amino acid sequence of the enzyme that has the amino acid sequence of the sec. Id. no.: 6. In a preferred embodiment, the variant alpha-amylase has one or more amino acid deletions, substitutions, and / or insertions. In a particularly preferred embodiment, the variant alpha-amylases include an alpha-amylase having the amino acid sequence shown in Section Id. No. 6 of this specification and further comprising the following modification: D183*+G184* (deletion at positions 183 and 184). This variant exhibits good performance in detergents and has improved stability in the presence of chelating agents. In a preferred embodiment, the variant alpha-amylase comprises SP722 (Seq. no. Id.: 6), including any of SP722+R181* G182*, SP722+G182* D183*, SP722+D183* G184*. SP722+R181* G182* means that the alpha-amylase SP722 of Bacillus spp. has been mutated by deletions at positions R181 and G182, where the numbers correspond to the seq. ID no. 6. Therefore, as described in this document, the alpha-amylase variant comprises SP722, SP722 + R181*G182*, SP722+G182*+ D183*, SP722 + D183*+ G184*; SP722 + R181*G182* N195F; SP722 + G182*D183*N195F; SP722 + D183* G184*N195F; SP722 + R181*G182* M202L; SP722 + G182* DI83* M202L; SP722 + D183* G184* M202L;SP722 + R181* G182* N195F M202L; SP722 + G182 D183* N195F M202L SP722 + D183* G184* N195F M202L; SP722 + D183* G184* N195F V206L Y243F; SP722 + D183* G184* N195F V206Y Y243F; SP722 + D183* G184* N195F V206F Y243F; SP722 + R181* G182* R181Q; SP722 + G182* D183* R181Q; SP722+D183* G184* R181Q; SP722+R181* G182* L118K N195F H458K; SP722+G182* D183* L118K N195F H458K; SP722+D183* G184* L118K N195F H458K; SP722 + D183* G184 G133E G149R N195Y Y203F V206L; "SP722 + R181* G182* N195F" means that the alpha-amylase SP722 of Bacillus spp. has been mutated as follows: deletions at positions R181 and G182 and a substitution of Asn (N) to Phe (F) at position 195, where the numbering corresponds to the Id. of sec. n.°: 6 (counting as if the deleted positions are still present, i.e. the numbering is not reduced by two when deleting two positions). In a particularly preferred embodiment of the invention, the alterations are selected from the following substitutions: X193A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, X, Y, preferably S193T; X195A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, X, Y, preferiblemente N195 [F o Y]; X197A, C, D, E, F, G, H, I, K, L, N, P, Q, R, S, T, V, W, X, Y, preferiblemente N197 [F o L] XI98A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, X, Y, preferiblemente Y198N; X200A, C, D, E, F, G, H, I, L, M, N, P, Q, R, S, T, V, W, X, Y, preferiblemente Y200F; X203A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, T, V, W, X, Y, preferiblemente Y203F. X206A, C, D, E, F, G, H, I, K, L, N, P, Q, R, S, T, V, W, X, Y, preferiblemente V206 [F, Y, L, H o N]; X210A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, X, Y, preferiblemente H210Y; X212A, C, D, E, F, G, H, I, L, M, N, P, Q, R, S, T, V, W, X, Y, preferiblemente E212 [V o G]; y X213A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, T, V, W, X, Y, preferiblemente V213A; X243A, C, D, E, F, G, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferably Y243F. In another preferred embodiment, the variants comprise alterations in three positions, more preferably four positions, more preferably five positions, and more preferably six positions; in a particularly preferred embodiment, the variant comprises at least one, at least two, or at least three deletions in the amino acid region of 181, 182, 183, or 184 and further an alteration in one or more positions corresponding to positions selected from the group consisting of 193, 195, 197, 198, 200, 203, 206, 210, 212, 213, 243, and an alteration in one or more positions corresponding to positions selected from the group consisting of 116, 129, 133, 142, 146, 147, 149, 151, 152, 169, 174, 186, 243, 244, 303, 320, 359, 418, 447 (using numbering according to Seq. ID No.: 6) Therefore, in an especially preferred embodiment of the invention, the alterations are selected from the following substitutions: X116A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferably N116T X118A, C, D, E, F, G, H, I, K, L, P, Q, R, S, T, V, W, Y, preferably X118K C, F, F, D, E G, H, I, K, L, M, N, P, Q, S, T, V, W, Y, preferably Q129L X133A, C, D, E, F, H, I, K, L, M, N, P, Q, R, R, S, T, V, W, Y, preferably G133E X133E X134A, C, D, E, F, Q, L, Q, Q R, S, T, V, W, Y, preferably D134Y X142A, C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferably K142R X142R X146A, C, E, F, G, H, I, K, L, M, N, R, Q, V, V, W, Y, preferably P146S X147A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, W, Y, preferably G147E X147A, C, D, E, F, G, I, K, L, N, P, Q, R, S, T, V, W, Y, M, P, Q, R, S, T, V, W, Y, preferably X149, C, G149 E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferably T151R X152A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferiblemente Y152H X169A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente Q169E X174C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente Q174R X186A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, W, Y, preferiblemente A186R X235A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferiblemente I235N X243A, C, D, E, F, G, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente Y243F X244A, C, D, E, F, G, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente S244Q X303A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferiblemente G303V X320A, C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente K320N X339A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferiblemente S339P X359C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferiblemente R359I X418A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y,preferably N418D X431A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferably S431T X431T X434A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, V, W, P44T preferably X44T C, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y, preferably A447V X458A, C, D, E, F, G, H, I, K, L, M, P, Q, R, S, T, V, W, Y, preferably R458K, In a particular preferred embodiment, the variant further comprises at least one, at least two, or at least three deletions in the region of amino acids 181, 182, 183, or 184. In a preferred embodiment, the number of amino acid substitutions in the variants of the present invention is preferably 17 substitutions, more preferably 16 substitutions, more preferably 15 substitutions, more preferably 14 substitutions, more preferably 13 substitutions, more preferably 12 substitutions, more preferably 11 substitutions, more preferably 10 substitutions, more preferably 9 substitutions, more preferably 8 substitutions, more preferably 7 substitutions, more preferably 6 substitutions, more preferably 5 substitutions, more preferably 4 substitutions, even more preferably 3 substitutions, and most preferably 2 substitutions.In another preferred embodiment, the number of amino acid substitutions in the variants of the present invention consists of preferably 17 substitutions, more preferably 16 substitutions, more preferably 15 substitutions, more preferably 14 substitutions, more preferably 13 substitutions, more preferably 12 substitutions, more preferably 11 substitutions, more preferably 10 substitutions, more preferably 9 substitutions, more preferably 8 substitutions, more preferably 7 substitutions, more preferably 6 substitutions, more preferably 5 substitutions, more preferably 4 substitutions, even more preferably 3 substitutions, and most preferably 2 substitutions. In a particular preferred embodiment, the variants comprise a combination of different alterations. Therefore, in a preferred embodiment, the variant comprises at least one, at least two, or at least three deletions in the amino acid region of positions 181, 182, 183, or 184, preferably the deletion at positions 183 and 184, and further comprises one of the following combinations of alterations and substitutions at positions 186 and 195; substitutions at positions 174 and 212; substitutions at positions 206 and 212; substitutions at positions 206, 212, and 304; substitutions at positions 206, 212, 304, and 447; substitutions at positions 116 and 133; substitutions at positions 235 and 339; substitutions at positions 193 and 206; substitutions in positions 116, 133 and 142; substitutions in positions 116, 133, 142 and 198; substitutions in positions 116, 133, 142, 198 and 206; substitutions in positions 133 and 195;substitutions in positions 133, 195 and 198; substitutions in positions 133, 195, 198 and 200; substitutions in positions 116 and 195; substitutions in positions 116, 195 and 198; substitutions in positions 142 and 146; substitutions in positions 142, 146 and 149; substitutions in positions 142, 146, 149 and 195; substitutions in positions 142, 146, 149, 195 and 198; substitutions in positions 142, 146, 149, 195, 198 and 206; substitutions in positions 151 and 210; substitutions in positions 151, 210 and 320; substitutions in positions 186, 195, 212 and 213; substitutions in positions 151, 210, 320 and 359; substitutions in positions 151, 210, 320, 359 and 418; substitutions in positions 147 and 149; substitutions in positions 147, 149 and 169; substitutions in positions 147, 149, 169 and 198; substitutions in positions 147, 149, 169, 198 and 203; substitutions in positions 147, 149, 169, 198, 203 and 206;substitutions in positions 133 and 149; substitutions in positions 133, 149 and 195; substitutions in positions 133, 149, 195 and 198; substitutions in positions 133, 149, 195, 198 and 203; substitutions in positions 147 and 152; substitutions in positions 147, 152 and 169; substitutions in positions 147, 152, 169 and 198; substitutions in positions 147, 152, 169, 198 and 206; substitutions in positions 195 and 206; substitutions in positions 195 and 243; substitutions in positions 195 and 210; substitutions in positions 206 and 210; substitutions in positions 186 and 195; substitutions in positions 195 and 206; substitutions in positions 195, 206 and 243; substitutions in positions 206 and 243; substitutions in positions 133 and 149; substitutions in positions 133, 149 and 198; substitutions in positions 133, 149, 198 and 206; substitutions in positions 116 and 133; substitutions in positions 116, 133 and 147;substitutions in positions 116, 133, 147 and 152; substitutions in positions 116, 133, 147, 152 and 198; substitutions in positions 116, 133, 147, 152, 198 and 203; substitutions in positions 116, 133, 147, 152, 198, 203 and 206; substitutions in positions 147 and 149; substitutions in positions 147, 149 and 195; substitutions in positions 147, 149, 195 and 198; substitutions in positions 147, 149, 195, 198 and 206; substitutions in positions 133 and 142; Substitutions in positions 133, 142 and 195; Substitutions in positions 133, 142, 195 and 198; Substitutions in positions 133 and 149; Substitutions in positions 133, 149 and 152; Substitutions in positions 133, 149, 152 and 195; Substitutions in positions 133, 149, 152, 195 and 198; Substitutions in positions 133, 149, 152, 195, 198 and 206; Substitutions in positions 116 and 129; Substitutions in positions 116, 129 and 142; Substitutions in positions 116, 129, 142 and 195;Substitutions in positions 116, 129, 142, 195 and 198; Substitutions in positions 116, 129, 142, 195, 198 and 203; Substitutions in positions 116, 129, 142, 195, 198, 203 and 206; Substitutions in positions 133 and 149; Substitutions in positions 133, 149 and 152; Substitutions in positions 133, 149, 152 and 195; Substitutions in positions 133, 149, 152, 195 and 198; Substitutions in positions 133, 149, 152, 195, 198 and 203; Substitutions in positions 133, 116, 149, 152, 195, 198, 203 and 206; Substitutions in positions 116 and 133; Substitutions in positions 116, 133 and 149; Substitutions in positions 116, 133, 149 and 198; Substitutions in positions 116, 133, 149, 198 and 203; Substitutions in positions 116, 133, 149, 198, 203 and 206; Substitutions in positions 195 and 198; Substitutions in positions 195, 198 and 203; Substitutions in positions 195, 198, 203 and 206; substitutions in positions 133, 149, 195, 203 and 206.; In another preferred embodiment, the variants comprise a combination of different alterations. Accordingly, in one particular preferred embodiment, the variant according to the present invention comprises at least one, at least two, or at least three deletions in the amino acid region of positions 181, 182, 183, or 184, preferably deletions at positions 183 and 184, and further comprising one of the following combinations of alterations and substitutions at positions 186 with [R, T, K, H, E, D, Q, or N] and 195 with [F, W, Y, L, I, or V]; substitutions at positions 174 with [R, K, H, E, D, Q, or N] and 212 with [F, W, Y, L, I, or V]; substitutions in positions 206 with [D, E, F, W, Y, L, I, V, N, Q or H] and 212 with [F, W, Y, L, I or V]; substitutions in positions 206 with [F, W, Y, L, I, V, N, Q or H], 212 with [F, W, Y, L, I or V] and 304 with [F, W, Y, L, I or V];substitutions in positions 206 with [F, W, Y, L, I, V, N, Q or H], 212 with [F, W, Y, L, I or V], 304 with [F, W, Y, L, I or V] and 447 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M] and 133 with [E or D]; substitutions in positions 235 with [N or L] and 339 with [P]; substitutions in positions 193 with [G, A, T or M] and 206 with [F, W, Y, L, I, V, N, Q, or H]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D] and 142 with [R, K, H, Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 142 with [R, K, H, Q or N] and 198 with [Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 142 with [R, K, H, Q or N], 198 with [Q or N] and 206 with [F, W, Y, L, I, V, N, Q or H]; substitutions in positions 133 with [E or D] and 195 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 195 with [F, W, Y, L, I or V] and 198 with [Q or N];substitutions in positions 186 with [R, T, K, H, E, D, Q, or N], 195 with [F, W, Y, L, I, or V], 212 with [F, W, Y, L, I, or V] and 213 with [A]; substitutions in positions 13 with [E or D], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 200 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M] and 195 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 142 with [R, K, H, Q or N] and 146 with [G, A, S, T or M]; substitutions in positions 142 with [R, K, H, Q or N], 146 with [G, A, S, T or M] and 149 with [R, K, H, Q or N]; substitutions in positions 142 with [R, K, H, Q or N], 146 with [G, A, S, T or M], 149 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 142 with [R, K, H, Q or N], 146 with [G, A, S, T or M], 149 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V] and 198 with [Q or N];substitutions in positions 142 with [R, K, H, Q or N], 146 with [G, A, S, T or M], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 206 with [F, W, Y, L, I, V, N, Q or H]; substitutions in positions 151 and 210 with [F, W, Y, L, I or V]; substitutions in positions 151, 210 with [F, W, Y, L, I or V] and 320 with [Q or N]; substitutions in positions 151, 210 with [F, W, Y, L, I or V], 320 with [Q or N] and 359 with [F, W, Y, L, I or V]; substitutions in positions 151, 210 with [F, W, Y, L, I or V], 320 with [Q or N], 359 with [F, W, Y, L, I or V] and 418 with [E or D]; substitutions in positions 147 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N] and 169 with [E or D]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N], 169 with [E or D] and 198 with [Q or N];substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N], 169 with [E or D], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N], 169 with [E or D], 198 with [Q or N], 203 with [F, W, Y, L, I or V] and 206 with [F, W, Y, L, I, V, N, Q or H]; substitutions in positions 133 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 147 with [E or D] and 152 with [R, K, H, Q or N]; substitutions in positions 147 with [E or D], 152 with [R, K, H, Q or N] and 169 with [E or D];substitutions in positions 147 with [E or D], 152 with [R, K, H, Q or N], 169 with [E or D] and 198 with [Q or N]; substitutions in positions 147 with [E or D], 152 with [R, K, H, Q or N], 169 with [E or D], 198 with [Q or N] and 206 with [F, W, Y, L, I, V, N, Q or H]; substitutions in positions 195 with [F, W, Y, L, I or V] and 206 with [F, W, Y, L, I, V, N, Q, or H]; substitutions in positions 195 with [F, W, Y, L, I or V] and 243 with [F, W, Y, L, I or V]; substitutions in positions 195 with [F, W, Y, L, I or V] and 210 with [F, W, Y, L, I or V]; substitutions in positions 206 with [F, W, Y, L, I, V, N, Q or H] and 210 with [F, W, Y, L, I or V]; substitutions in positions 186 with [R, K, H, E, D, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 195 with [F, W, Y, L, I or V] and 206 with [F, W, Y, L, I, V, N, Q, or H]; substitutions in positions 195 with [F, W, Y, L, I or V], 206 and 243 with [F, W, Y, L, I or V]; substitutions in positions 206 and 243 with [F, W, Y, L, I or V];substitutions in positions 133 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N] and 198 with [Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 198 with [Q or N] and positions 116 with [G, A, S, T or M], 133 with [E or D] and 147 with [E or D]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 147 with [E or D] and 152 with [R, K, H, Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 147 with [E or D], 152 with [R, K, H, Q or N] and 198 with [Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 147 with [E or D], 152 with [R, K, H, Q or N], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 147 with [E or D], 152 with [R, K, H, Q or N], 198 with [Q or N] and 203 with [F, W, Y, L, I or V] and 206;substitutions in positions 147 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 147 with [E or D], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 206; substitutions in positions 133 with [E or D] and 142 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 142 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 142 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 133 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N] and 152 with [R, K, H, Q or N];substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V] and 198 with [Q or N] and 206; substitutions in positions 116 with [G, A, S, T or M] and 129 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 129 with [F, W, Y, L, I or V] and 142 with [R, K, H, Q or N]; substitutions in positions 116 with [G, A, S, T or M], 129 with [F, W, Y, L, I or V], 142 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 129 with [F, W, Y, L, I or V], 142 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N];substitutions in positions 116 with [G, A, S, T or M], 129 with [F, W, Y, L, I or V], 142 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 129 with [F, W, Y, L, I or V], 142 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N], 203 with [F, W, Y, L, I or V] and 206; substitutions in positions 133 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N] and 152 with [R, K, H, Q or N]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N] and 195 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V] and 198 with [Q or N];substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 152 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 198 with [Q or N], 203 with [F, W, Y, L, I or V] and 206; substitutions in positions 116 with [G, A, S, T or M] and 133 with [E or D]; substitutions in positions 116 with [G, A, S, T or M] and 133 with [E or D] and 149 with [R, K, H, Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 149 with [R, K, H, Q or N] with [R, K, H, Q or N] and 198 with [Q or N]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 149 with [R, K, H, Q or N], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 116 with [G, A, S, T or M], 133 with [E or D], 149 with [R, K, H, Q or N], 198 with [Q or N], 203 with [F, W, Y, L, I or V] and 206;substitutions in positions 195 with [F, W, Y, L, I or V] and 198 with [Q or N]; substitutions in positions 195 with [F, W, Y, L, I or V], 198 with [Q or N] and 203 with [F, W, Y, L, I or V]; substitutions in positions 195 with [F, W, Y, L, I or V], 198 with [Q or N], 203 with [F, W, Y, L, I or V] and 206 with [F, W, Y, L, I, V, N, Q or H]; substitutions in positions 133 with [E or D], 149 with [R, K, H, Q or N], 195 with [F, W, Y, L, I or V], 203 with [F, W, Y, L, I or V], and 206 with [F, W, Y, L, I, V, N, Q or H].; Specific useful variants include (using the numbering of sec. ID no. 6): D183* G184* N195L; D183* G184* N197F; D183* G184* N197L; D183* G184* Y243F; D183* G184* N195F, D183* G184* N277F; D183* G184* S431T; D183* G184* P434T; D183* G184* I235N S339P; D183* G184* L351F; D183* G184* A186R, N195F; DI83* G184* H210Y; DI83* G184* V206Y; DI83* G184* V206L; DI83* G184* V206F; D183* G184* V213A Q174R; D183* G184* E212V; D183* G184* V206F E212G G304V A447V; N116T G133E K142R D183* G184* Y198N V206Y; G133E D183* G184* N195Y Y198N Y200F; D183* G184* A186D N195F E212V V213A; N116T D183* G184* N195Y Y198N; K142R P146S G149K D183* G184* N195Y Y198N V206I; D134Y D183* G184*; T151R D183 * G184* H210Y K320N R359I N418D Q490H; G147E G149R Q169E D183 * G184* Y198N Y203F V206Y; G133E G149R D183* G184* N195Y Y198N Y203F V206Y; G147E Y152H Q169E D183* G184* Y198N V206Y; D183* G184* N195F V206Y; D183* G184* N195F V206L; D183* G184* N195F V206F; D183* G184* V206L Y243F; D183* G184* V206F Y243F; D183* G184* N195F Y243F; D183* G184* N195F H210Y; D183* G184* V206Y H210Y;D183* G184* V213A; D183* G184* S193T; D183* G184* A186T N195F; D183* G184* N195F V206Y Y243F; D183* G184* N195F V206L Y243F; D183* G184* N195F V206Y Y243F; D183* G184* N195F V206F Y243F; D183* G184* V206Y Y243F; D183* G184* N195Y; G133D G149R D183* G184* Y198N V206Y; N116T G133E G147E Y152H D183* G184* Y198N Y203F V206Y; G147E G149R D183* G184* N195F Y198N V206Y; G133E K142R D183* G184* N195F Y198N; G133E G149R Y152H D183* G184* N195Y Y198N V206Y; N116T Q129L K142R D183* G184* N195Y Y198N Y203F V206Y; G133E G149R Y152H D183* G184* N195Y Y198N Y203F V206Y; N116T G133E G149R G182* D183* Y198N Y203F V206Y; D183* G184* S193T V206L, D183* G184* G133E G149R N195Y Y203F V206L.; In a preferred embodiment, the variants include, SP722SP722 + D183* G184* N195L; SP722SP722 + D183* G184* N197F; SP722SP722 + D183* G184* N197L; SP722SP722 + D183* G184* Y243F; SP722SP722 + D183* G184* N195F, SP722SP722 + D183* G184* N277F; SP722 + D183* G184* S431T; SP722 + D183* G184* P434T; SP722 + D183* G184* I235N S339P; SP722 + D183* G184* L351F; SP722 + D183* G184* A186D N195F E212V V213A; SP722 + D183* G184* A186R, N195F; SP722 + DI83* G184* H210Y; SP722 + D183* G184* V206Y; SP722 + D183* G184* V206L, SP722 + D183* G184* V206F; SP722 + D183* G184* V213A Q174R; SP722 + D183* G184* E212V; SP722 + D183* G184* V206Y E212G G304V A447V; SP722 + N116T G133E K142R D183* G184* Y198N V206Y; SP722 + G133E D183* G184* N195Y Y198N Y200F; SP722+N116T D183* G184* N195Y Y198N; SP722 + K142R P146S G149K D183* G184* N195Y Y198N V206I; SP722 + D134Y D183* G184*; SP722 + T151R D183* G184* H210Y K320N R359I N418D; SP722 + G147E G149R Q169E D183* G184* Y198N Y203F V206Y; SP722 + G133E G149R D183* G184* N195Y Y198N Y203F V206Y;SP722 + G147E Y152H Q169E D183* G184* Y198N V206Y; SP722 + D183* G184* N195F V206Y; SP722 + D183* G184* N195F V206F; SP722 + D183* G184* N195F V206L; SP722 + D183* G184* I206L Y243F; SP722 + D183* G184* I206F Y243F; SP722 + D183* G184* N195F Y243F; SP722 + D183* G184* N195F H210Y; SP722 + D183* G184* V206Y H210Y; SP722 + D183* G184* V213A; SP722 + D183* G184* S193T; SP722 + D183* G184* A186T N195F; SP722 + D183* G184* N195F V206Y Y243F; SP722 + D183* G184* V206Y Y243F; SP722 + D183* G184* N195Y; SP722 + G133D G149R D183* G184* Y198N V206Y; SP722 + N116T G133E G147E Y152H D183* G184* Y198N Y203F V206Y; SP722 + G147E G149R D183* G184* N195F Y198N V206Y; SP722 + G133E K142R D183* G184* N195F Y198N; SP722 + G133E G149R Y152H D183* G184* N195Y Y198N V206Y; SP722 + N116T Q129L K142R D183* G184* N195Y Y198N Y203F V206Y; SP722 + G133E G149R Y152H D183* G184* N195Y Y198N Y203F V206Y; SP722 + N116T G133E G149R G182* D183* Y198N Y203F V206Y; SP722 + D183* G184* G133E G149R N195Y Y203F V206L.; In a preferred embodiment, the variants are selected from the following: SP722 + D183* G184* N195F V206L Y243F; SP722 + D183* G184* N195F V206Y Y243F; SP722 + D183* G184* N195F V206N Y243F; SP722 + D183* G184* N195F V206F Y243F; SP722 + D183* G184* N195F V206H; SP722 + D183* G184* N195F V206Y; SP722 + D183* G184* V206F Y243F; SP722 + D183* G184* N195F V206L H210Y; SP722 + D183* G184* S193T V206L; SP722 + D183* G184* G133E G149R N195Y Y203F V206L. Cleaning compositions The present invention preferably relates to products and / or methods connected with and / or used according to the claimed compositions, which are for air care, car care, dishwashing, fabric conditioning (including softening), fabric detergents, laundry and rinsing additives and / or garment care, cleaning and / or treating hard surfaces, and other cleaning for consumer or institutional use. According to the invention, the above alpha-amylase variants can typically be a component in a cleaning composition such as a detergent composition, for example, a laundry detergent composition or a dishwashing detergent composition. A liquid laundry detergent composition is particularly preferred. These cleaning compositions comprise a cleaning aid / detergent, which is not a chelating agent as defined above, preferably comprising a mixture of components. Typically, the cleaning aid is present in the composition in an amount of 0.001 to 99.9% by weight, more typically from 0.01 to 80% by weight of cleaning aid. Suitable cleaning aids include: surfactants, detergency boosters, bleaches, bleach catalysts, dyes, bleach boosters, dye transfer agents, deposition aids, surfactants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, optical brighteners, photoactivators, fluorescents, fabric tinting agents, fabric conditioners, preformed peracids, polymeric surfactants,Clay stain removers / anti-redeposition agents, bulking salts, hydrotropes, brighteners, soap scum suppressants, structural elasticizing agents, fabric softeners, hydrolyzable surfactants, preservatives, antioxidants, anti-shrink agents, germicides, fungicides, anti-tarnish agents, anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, dyes, perfumes, and pH control agents. For example, these may include bleaching ingredients such as an imine bleach booster; hydrogen peroxide sources such as percarbonate and / or perborate, especially percarbonate coated with a material such as a carbonate and / or sulfate salt, silicate salt, borosilicate, and any mixture thereof; preformed peracid,including preformed peracid in encapsulated form; transition metal catalysts; soap suppressants or suppression systems such as silicone-based soap suppressants and / or fatty acid-based soap suppressants; fabric softeners such as clay, silicone, and / or quaternary ammonium compounds; flocculants such as poly(ethylene oxide); dye transfer inhibitors such as polyvinylpyrrolidone, poly(4-vinylpyridine N-oxide), and / or vinylpyrrolidone-vinylimidazole copolymer; fabric integrity components such as oligomers produced by the condensation of imidazole and epichlorohydrin; soil dispersants and anti-redeposition aids such as alkoxylated polyamines and ethoxylated ethyleneimine polymers; anti-redeposition components,such as polyesters; carboxylate polymers such as maleic acid polymers or maleic acid-acrylic copolymers; perfumes such as perfume microcapsules; starch-encapsulated accords, spray-deposited perfumes; soap rings; aesthetic particles; dyes; fillers such as sodium sulfate, although it is preferred that the composition be practically free of fillers; silicate salts such as sodium silicate, including sodium silicate 1.6R and 2.0R, or sodium metasilicate; copolyesters of dicarboxylic acids and diols; cellulosic polymers such as methylcellulose, carboxymethylcellulose, hydroxyethoxycellulose, or other alkyl or alkylalkoxy celluloses; solvents such as 1,2-propanediol, monoethanolamine; diethylene glycol, ethanol, and any mixture thereof; hydrotropes such as sodium cumenesulfonate, sodium xylenesulfonate, sodium toluenesulfonate,and any mixtures thereof; organic acids such as citric acid; and any combination thereof. In another preferred aspect, the composition comprises one or more surfactants, which may be nonionic, including semipolar surfactants, and / or anionic and / or cationic and / or hybrid ion and / or ampholytic surfactants, and / or semipolar nonionic surfactants, and / or mixtures thereof. The surfactants are typically present at a level of 0.1% to 60% by weight, or 0.5% to 50% by weight, or 1% to 40% by weight of the composition. When included in the above, the cleaning composition will normally contain from approximately 1% to approximately 40% of an anionic surfactant such as a linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, fatty alpha-sulfo acid methyl ester, alkyl or alkenylsuccinic acid, or soap. When included in the above, the cleaning agent will normally contain from approximately 0.2% to approximately 40% of a nonionic surfactant such as an ethoxylated alcohol, ethoxylated nonylphenol, alkyl polyglycosidic acid, alkyl dimethylamine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxylated fatty acid amide, or N-acyl and N-alkyl derivatives of glucosamine ("glucamides"). The cleaning composition may comprise one or more additional enzymes such as a protease, a lipase, a peroxidase, another amylolytic enzyme, for example, another alpha-amylase, glucoamylase, maltophenic amylase, CGTase and / or a cellulase, mannanase (such as MANNAWAY™ from Novozymes, Denmark), pectinase, pectate lyase, cutinase, and / or laccase. In general, the properties of the selected enzyme or enzymes must be compatible with the selected detergent (i.e., optimum pH, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme or enzymes must be present in an effective quantity. Proteases: Suitable proteases include metalloproteases and / or serine proteases, including neutral or alkaline serine proteases, such as subtilisins (EC 3.4.21.62). Suitable proteases include those of animal, plant, or microbial origin. In one respect, such a suitable protease may be of microbial origin. Suitable proteases include chemically or genetically modified mutants of the aforementioned suitable proteases. In one respect, the suitable protease may be a serine protease, such as a microbial alkaline protease and / or a trypsin-like protease. Examples of suitable neutral or alkaline proteases include: (a) subtilisins (EC 3.4.21.62), including those derived from Bacillus, such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in US-6,312,936 B1, US-5,679,630, US-4,760,025, US-7,262,042 and WO09 / 021867. (b) trypsin-like or chymotrypsin-like proteases, such as trypsin (e.g., of porcine or bovine origin) including the Fusarium protease described in WO 89 / 06270 and the Cellumonas-derived chymotrypsin proteases described in WO 05 / 052161 and WO 05 / 052146. (c) metalloproteases, including those derived from Bacillus amyloliquefaciens described in WO 07 / 044993A2. Preferred proteases include those derived from Bacillus gibsonii or Bacillus lentus. Suitable commercial protease enzymes include those sold under the trade names Alcalase®, Savinase®, Primase®, Durazym®, Polarzyme®, Kannase®, Liquanase®, Liquanase Ultra®, Savinase Ultra®, Ovozyme®, Neutrase®, Everlase® and Esperase® by Novozymes A / S (Denmark), those sold under the trade names Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase® and Purafect OXP® by Genencor International, those sold under the trade names Opticlean® and Optimase® by Solvay Enzymes, and those marketed by Henkel / Kemira, especially BLAP (sequence shown in Figure 29 of US-5.352).604 with the following mutations S99D + S101 R + S103A + V104I + G159S, hereinafter referred to as BLAP), BLAP R (BLAP with S3T + V4I + V199M + V205I + L217D), BLAP X (BLAP with S3T + V4I + V205I) and BLAP F49 (BLAP with S3T + V4I + A194P + V199M + V205I + L217D) - all from Henkel / Kemira; and KAP (subtilisin from Bacillus alkalophilus with mutations A230V + S256G + S259N) from Kao. Lipases: Suitable lipases include those of bacterial or fungal origin. Chemically modified mutants or those obtained by protein engineering are included. Examples of useful lipases include Humicola (synonym Thermomyces) lipases, for example, from H. lanuginosa (T. lanuginosus) as described in EP 258068 and EP 305 216 or from H. insolens as described in WO 96 / 13580, a Pseudomonas lipase, for example, from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1.372.034), P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (WO 96 / 12012), a Bacillus lipase, for example, from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360), B. stearothermophilus (JP-64 / 744992) or B. pumilus (WO 91 / 16422). The lipase may be a "first-cycle lipase" as described in US-6,939,702 B1 and US-PA 2009 / 0217464. In one respect, the lipase is a first-wash lipase, preferably a variant of the natural lipase from Thermomyces lanuginosus comprising the T231R and N233R mutations. The natural sequence has the 269 amino acids (amino acids 2-291) of the Swissprot registration number Swiss-Prot O59952 (derived from Thermomyces lanuginosus (Humicola lanuginosa)). Preferred lipases would include those marketed under the trade names Lipex®, Lipolex®, and Lipoclean®. Suitable cellulases include those of bacterial or fungal origin. Chemically modified mutants or those obtained through protein engineering are also included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum described in US-4,435,307, US-5,648,263, US-5,691,178, US-5,776,757 and WO 89 / 09259. Cellulases: Suitable cellulases include those of bacterial or fungal origin. Chemically modified mutants or those obtained through protein engineering are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum described in US-4,435,307, US-5,648,263, US-5,691,178, US-5,776,757, and WO 89 / 09259. The most suitable cellulases are alkaline or neutral cellulases, which offer color-preserving advantages. Examples of these cellulases are those described in EP-0495257, EP-0531372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940. Other examples include cellulase variants such as those described in WO 94 / 07998, EP 0 531315, US-5.457.046, US-5.686.593, US-5.763.254, WO 95 / 24471, WO 98 / 12307, and PCT / DK98 / 00299. Commercially available cellulases include CELLUZYME®, and CAREZYME® (Novozymes A / S), CLAZINASE®, and PURADAX HA® (Genencor International Inc.) and KAC-500 (B) ® (Kao Corporation). Peroxidases / Oxidases: Peroxidases / oxidases include those of plant, bacterial, or fungal origin. Chemically modified mutants or those obtained through protein engineering are included. Examples of useful peroxidases include Coprinus peroxidases, for example, from C. cinereus, and variants thereof such as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercial peroxidases include GUARDZYME® (Novozymes A / S). Other enzymes: Other preferred enzymes include pectate lyases sold under the trade names Pectawash®, Pectaway® and mannases sold under the trade names Mannaway® (all from Novozymes A / S, Bagsvaerd, Denmark), and Purabrite® (Genencor International Inc., Palo Alto, California). Detergent enzymes can be included in a detergent composition by separately adding additives containing one or more enzymes, or by adding a combined additive comprising all such enzymes. A detergent additive of the invention, i.e., a separate or combined additive, can be formulated, for example, as granules, a liquid, or an aqueous suspension. Detergent additive formulations are granules, especially dust-free granules, liquids, particularly stabilized liquids, or aqueous suspensions. Dust-free granules can be produced, for example, as described in US-4,106,991 and US-4,661,452, and can optionally be coated using methods known in the art. Examples of cerulean coating materials include poly(ethylene oxide) (polyethylene glycol, PEG) products having average molecular weights of 1,000 to 20,000; ethoxylated nonylphenols having 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains 12 to 20 carbon atoms and which have 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, diglycerides, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed techniques are provided in GB-1483591.Liquid enzyme preparations can, for example, be stabilized by the addition of a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid, or boric acid according to established methods. Protected enzymes can be prepared according to the method described in EP-238.216. The composition may comprise a fabric tinting agent. Suitable fabric tinting agents include dyes, dye-clay conjugates, and pigments that preferably meet the requirements of Test Method 1 described later in this specification. Suitable dyes include micromolecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes found in the color index (CI) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet, and Basic Red, or mixtures thereof, for example: (1) Tris-azo direct blue dyes of formula where at least two of the naphthyl rings A, B and C are substituted by a sulfonate group, ring C may be substituted at position 5 by an NH2 or NHPh group, X is a benzyl or naphthyl ring substituted with up to 2 sulfonate groups and may be substituted at position 2 with an OH group and may also be substituted with an NH2 or NHPh group. (2) bis-azo type direct violet dyes of formula: where Z is H or phenyl, ring A is preferably substituted by a methyl and methoxy group in the positions indicated by arrows, ring A can also be a naphthyl-type ring, group Y is a benzyl ring or a naphthyl ring, which is substituted by a sulfate group and can be mono- or disubstituted by methyl groups. (3) Acidic blue or red dyes of formula where X and Y must each be, at least one of the two, an aromatic group. In one respect, both aromatic groups may be a substituted benzyl or naphthyl group, which may be substituted with water-insoluble groups such as alkyl, alkyloxy, or aryloxy groups; X and Y may be unsubstituted with water-soluble groups such as sulfonates or carboxylates. In another respect, X is a benzyl group substituted with a nitro group, and Y is a benzyl group. (4) Red acidic dyes of the structure where B is a naphthyl or benzyl group that may be substituted with water-insoluble groups such as alkyl or alkyloxy or aryloxy groups, B may not be substituted with water-soluble groups such as sulfonates or carboxylates. (5) Dis-azo type dyes of the structure where X and Y, independently of each other, are each hydrogen, C1-C4 alkyl or C1-C4 alkoxy, R is hydrogen or aryl, Z is C1-C4 alkyl; C1-C4 alkoxy; halogen; hydroxyl or carboxyl, n is 1 or 2 and m is 0, 1 or 2, as well as corresponding salts thereof and mixtures thereof (6) Triphenylmethane dyes of the following structures and mixtures thereof. In another respect, suitable small molecule dyes include small molecule dyes selected from the group consisting of numbered dyes, according to the Colour Index (Society of Dyers and Colourists, Bradford, UK): Direct Violet 9, Direct Violet 35, Direct Violet 48, Direct Violet 51, Direct Violet 66, Direct Violet 99, Direct Blue 1, Direct Blue 71, Direct Blue 80, Direct Blue 279, Acid Red 17, Acid Red 73, Acid Red 88, Acid Red 150, Acid Violet 15, Acid Violet 17, Acid Violet 24, Acid Violet 43, Acid Red 52, Acid Violet 49, Acid Blue 15, Acid Blue 17, Acid Blue 25, Acid Blue 29, Acid Blue 40, Acid Blue 45, Acid Blue 75, Acid Blue 80, Acid Blue 83, Acid Blue 90 and Acid Blue 113, Acid Black 1, Basic Violet 1, Basic Violet 3, Basic Violet 4, Basic Violet 10, Basic Violet 35, Basic Blue 3, Basic Blue 16, Basic Blue 22, Basic Blue 47, Basic Blue 66, Basic Blue 75, Basic Blue 159 mixtures thereof.In another respect, suitable small molecule dyes include those selected from the group consisting of the following numbers, according to the Colour Index (Society of Dyers and Colourists, Bradford, UK): Acid Violet 17, Acid Violet 43, Acid Red 52, Acid Red 73, Acid Red 88, Acid Red 150, Acid Blue 25, Acid Blue 29, Acid Blue 45, Acid Blue 113, Acid Black 1, Direct Blue 1, Direct Blue 71, Direct Violet 51, and mixtures thereof. Suitable polymeric dyes include polymeric dyes selected from the group consisting of polymers containing conjugated chromogens (polymeric dye conjugates) and polymers with chromogens copolymerized in the polymer backbone and mixtures thereof. In another respect, suitable polymeric dyes include polymeric dyes selected from the group consisting of high fabric affinity dyes marketed under the name Liquitint® (Milliken, Spartanburg, South Carolina, USA), polymeric dye conjugates formed from at least one reactive dye and a polymer selected from the group consisting of a hydroxyl moiety, a primary amine moiety, a secondary amine moiety, a thiol moiety, and mixtures thereof. In a further respect, suitable polymeric dyes include polymeric dyes selected from the group consisting of Liquitint® (Milliken, Spartanburg, South Carolina, USA) Violet CT, carboxymethylcellulose (CMC) conjugated with a Reactive Blue, Reactive Violet, or Reactive Red dye, such as, for example, CMC conjugated with the dyes named according to the CI code.Reactive Blue 19, marketed by Megazyme, Wicklow, Ireland, under the product name AZO-CM-CELLULOSE, product code S-ACMC, alkoxylated triphenylmethane polymeric dyes, alkoxylated thiophene polymeric dyes, and mixtures thereof. Suitable dye-clay conjugates include dye-clay conjugates selected from the group comprising at least one cationic / basic dye and a smectite-type clay, and mixtures thereof. In another respect, suitable dye-clay conjugates include dye-clay conjugates selected from the group consisting of a cationic / basic dye selected from the group consisting of CI Basic Yellow, 1 to 108, CI Basic Orange, 1 to 69, CI Basic Red, 1 to 118, CI Basic Violet, 1 to 51, CI Basic Blue, 1 to 164, CI Basic Green, 1 to 14, CI Basic Brown, 1 to 23; CI Basic Black, 1 to 11; and a clay selected from the group consisting of montmorillonite-type clay, hectorite-type clay, saponite-type clay, and mixtures thereof.In another additional aspect, suitable clay-dye conjugates include clay-dye conjugates selected from the group consisting of: montmorillonite conjugate Basic Blue B7 CI 42595, montmorillonite conjugate Basic Blue B9 CI 52015, montmorillonite conjugate Basic Violet V3 CI 42555, montmorillonite conjugate Basic Green G1 CI42040, montmorillonite conjugate Basic Red R1 CI45160, montmorillonite conjugate CI Basic Black 2, hectorite conjugate Basic Blue B7 CI42595, hectorite conjugate Basic Blue B9 CI52015, hectorite conjugate Basic Violet V3 CI 42555, hectorite conjugate Basic Green G1 CI 42040, hectorite conjugate Basic Red R1 CI45160, and so on. hectorite CI Basic Black 2, saponite conjugate Basic Blue B7 CI42595, saponite conjugate Basic Blue B9 CI 52015, saponite conjugate Basic Violet V3 CI 42555, saponite conjugate Basic Green G1 CI 42040, saponite conjugate Basic Red R1 CI45160, CI Basic Black 2 saponite conjugate and mixtures thereof. Suitable pigments include pigments selected from the group consisting of flavanthrone, indanthrone, chlorinated indanthrone containing 1 to 4 chlorine atoms, pyranthrone, dichloropyranthrone, monobromodichloropyranthrone, dibromodichloropyranthrone, tetrabromopyranthrone, diimide of perylene-3,4,9,10-tetracarboxylic acid, wherein the imide groups may be unsubstituted or substituted by a C1-C3 alkyl or a phenyl or heterocyclic radical, and wherein the phenyl and heterocyclic radicals may additionally bear substituents that do not confer water solubility, amides of anthrapyrimidicarboxylic acid, violantrone, isoviolantrone, dioxazine-type pigments, copper phthalocyanine, which may contain up to 2 chlorine atoms per molecule, phthalocyanine of polychloro-copper or polybromochloro-copper phthalocyanine containing up to 14 bromine atoms per molecule and mixtures thereof. In another respect, suitable pigments include selected pigments from the group consisting of Ultramarine Blue (name CI Pigment Blue 29), Ultramarine Violet (CI Pigment Violet 15) and mixtures thereof. The fabric colorants mentioned above may be used in combination (any mixture of fabric colorants may be used). Suitable fabric colorants may be purchased from Aldrich, Milwaukee, Wisconsin, USA; Ciba Specialty Chemicals, Basel, Switzerland; BASF, Ludwigshafen, Germany; Dayglo Color Corporation, Mumbai, India; Organic Dyestuffs Corp., East Providence, Rhode Island, USA; Dystar, Frankfurt, Germany; Lanxess, Leverkusen, Germany; Megazyme, Wicklow, Ireland; Clariant, Muttenz, Switzerland; Avecia, Manchester, UK; and / or as per the examples contained herein. Suitable colorants are described in US-7,208,459 B2. Test Method 1 The following is a protocol for determining whether a dye or pigment material is a fabric coloring agent for the purpose of the present invention: 1.) Fill two Tergotometer containers with 800 ml of mains water from Newcastle upon Tyne, UK (~12 grains per US gallon total hardness, supplied by Northumbrian Water, Pity Me, Durham, Co. Durham, UK). 2) Insert the containers into the Tergotometer apparatus, with the water temperature controlled at 30 °C and the stirring set at 40 rpm for the duration of the experiment. 3) Add 4.8 g of IEC-B detergent (type B detergent for a base reference washing machine IEC 60456), supplied by wfk, Brüggen-Bracht, Germany, to each container. 4) After two minutes, add 2.0 mg of active dye to the first container. 5) After one minute, add 50g of plain cotton t-shirt (supplied by Warwick Equest, Consett, County Durham, UK), cut into 5cm x 5cm samples, to each container. 6) After 10 minutes, empty the containers and refill them with cold water (16 °C) with a hardness of 14.4 English Clark hardness grades with a molar ratio of calcium to magnesium of 3:1. 7) After 2 minutes of rinsing, remove the tissues. 8) Repeat steps 3-7 for three more cycles using the same treatments. 9) Collect and hang the fabrics in an enclosed area for 12 hours. 10) Analyze the samples using a Hunter Miniscan spectrometer equipped with D65 illuminant and UVA filter to obtain Hunter a (red-green axis) and Hunter b (yellow-blue axis) values. 11) Average the Hunter a and Hunter b values ​​for each set of fabrics. If the dye-treated fabrics subjected to evaluation show an average shade difference greater than 0.2 units on the a-axis or on the b-axis, it is considered to be a fabric tinting agent for the purpose of the invention. The cleaning composition may also include detergent boosters, such as carbonate, bicarbonate, or silicate additives, which may be zeolites such as Zeolite A or MAP Zeolite (maximum P-type aluminum). Zeolites suitable for laundry use preferably have the formula Na₁₂(AlO₂)₁₂(SiO₂)₁₂·27H₂O, and the particle size is usually between 1–10 µm for Zeolite A and 0.7–2 µm for MAP Zeolite. Other additives include strongly alkaline sodium metasilicate (Na₂SiO₃·nH₂O or Na₂Si₂O₅·nH₂O), which is preferably used in dishwashing. In preferred embodiments, the amount of detergent-boosting additive may be greater than 5%, greater than 10%, greater than 20%, greater than 30%, greater than 40% or greater than 50%, and may be less than 80%, 65%.In a dishwashing detergent, the level of detergent-boosting additive is typically 40-65%, especially 50-65% or even 75-90%. The composition may comprise an encapsulation. In one aspect, an encapsulation comprises a core, a shell having an inner and an outer surface, said shell encapsulating said core. In one aspect of said encapsulation, said core may comprise a material selected from the group consisting of perfumes; brighteners; dyes; insect repellents; silicones; waxes; flavorings; vitamins; fabric softeners; skin care agents; in one aspect, paraffins; enzymes; antibacterial agents; bleaches; sensory stimulants; and mixtures thereof; and said shell may comprise a material selected from the group consisting of polyethylenes; polyamides; polystyrenes; polyisoprenes; polycarbonates; polyesters; polyacrylates;aminoplasts, in one aspect, said aminoplast may comprise polyureas, polyurethane, and / or polyureaurethane, in one aspect, said polyurea may comprise polyoxymethylene and / or melamine formaldehyde; polyolefins; polysaccharides, in one aspect, said polysaccharide may comprise alginate and / or chitosan; gelatin; shellac; epoxy resins; vinyl polymers; water-insoluble inorganic compounds; silicone; and mixtures thereof. In one aspect of said encapsulation, said core may comprise perfume. In one aspect of said encapsulation, said envelope may comprise melamine formaldehyde and / or crosslinked melamine formaldehyde. In one aspect, suitable encapsulations may comprise a core material and a shell, the shell at least partially surrounding the core material described. At least 75%, 85%, or even 90% of such encapsulations may have a fracture toughness of approximately 0.2 MPa to approximately 10 MPa, approximately 0.4 MPa to approximately 5 MPa, approximately 0.6 MPa to approximately 3.5 MPa, or even approximately 0.7 MPa to approximately 3 MPa; and a beneficial agent leakage of 0% to approximately 30%, 0% to approximately 20%, or even 0% to approximately 5%. In one respect, at least 75%, 85%, or even 90% of such encapsulated particles may have a particle size of approximately 1 micrometer to approximately 80 micrometers, approximately 5 micrometers to 60 micrometers, approximately 10 micrometers to approximately 50 micrometers, or even approximately 15 micrometers to approximately 40 micrometers. In one respect, at least 75%, 85%, or even 90% of such encapsulates may have a particle wall thickness of approximately 30 nm to approximately 250 nm, approximately 80 nm to approximately 180 nm, or even approximately 100 nm to approximately 160 nm. In one aspect, said core material of the encapsulants may comprise a material selected from the group consisting of a perfume raw material and / or optionally a material selected from the group consisting of vegetable oil, including pure and / or mixed vegetable oils including castor oil, coconut oil, cottonseed oil, grape pomace oil, rapeseed oil, soybean oil, corn oil, palm oil, linseed oil, safflower oil, olive oil, peanut oil, coconut oil, palm kernel oil, castor oil, lemon oil and mixtures thereof; vegetable oil esters, including dibutyl adipate, dibutyl phthalate, butyl benzyladipate, benzyl octyladipate, tricresyl phosphate, trioctyl phosphate and mixtures thereof; linear or branched chain hydrocarbons, including those linear or branched chain hydrocarbons having a boiling point above approximately 80 °C;Partially hydrogenated terphenyls, dialkyl phthalates, alkylbiphenyl, including monoisopropylbiphenyl, alkylated naphthalene, including dipropylnaphthalene, volatile petroleum substances including kerosene, mineral oil and mixtures thereof; aromatic solvents, including benzene, toluene and mixtures thereof; silicone oils; and mixtures thereof. In one aspect, the wall material of the encapsulated components may comprise a resin that includes the reaction product of an aldehyde and an amine; suitable aldehydes include formaldehyde. Suitable amines include melamine, urea, benzoguanamine, glycoluril, and mixtures thereof. Suitable melamines include methyl melamine, methylated methyl melamine, iminomelamine, and mixtures thereof. Suitable ureas include dimethyl urea, methylated dimethyl urea, urea-resorcinol, and mixtures thereof. In one respect, suitable formaldehyde removers can be used with the encapsulated products, for example, in an aqueous suspension of capsules and / or added to the consumer product before, during or after adding the encapsulated products to said consumer product. Suitable capsules may be prepared following the instructions of USPA 2008 / 0305982 A1; and / or USPA 2009 / 0247449 A1. Alternatively, suitable capsules may be purchased from Appleton Papers Inc. of Appleton, Wisconsin, USA. In addition, the materials for manufacturing the aforementioned encapsulants can be obtained from Solutia Inc. (St. Louis, Missouri, USA), Cytec Industries (West Paterson, New Jersey, USA), Sigma-Aldrich (St. Louis, Missouri, USA), CP Kelco Corp. of San Diego, California, USA; BASF AG of Ludwigshafen, Germany; Rhodia Corp. of Cranbury, New Jersey, USA; Hercules Corp. of Wilmington, Delaware, USA; Agrium Inc. of Calgary, Alberta, Canada, ISP of New Jersey, USA, Akzo Nobel of Chicago, IL, USA; Stroever Shellac Bremen of Bremen, Germany; Dow Chemical Company of Midland, MI, USA; Bayer AG of Leverkusen, Germany; Sigma-Aldrich Corp., St. Louis, Missouri, USA. In one aspect, the composition may comprise an enzyme stabilizer selected from the group consisting of (a) inorganic salts selected from the group consisting of calcium salts, magnesium salts and mixtures thereof; (b) carbohydrates selected from the group consisting of oligosaccharides, polysaccharides and mixtures thereof; (c) bulk-effective reversible protease inhibitors selected from the group consisting of phenylboronic acid and derivatives thereof; and (d) mixtures thereof. In another embodiment, the composition comprises: (1) reversible protease inhibitors such as a boron-containing compound; (2) 1-2 propanediol; (3) calcium formate and / or sodium formate; and (4) any combination thereof. In one aspect, the composition may comprise a structuring agent selected from the group consisting of diglycerides and triglycerides, microcrystalline cellulose with ethylene glycol distearate, cellulosic-type materials, cellulose microfiber, biopolymers, xanthan gum, gellan gum, and mixtures thereof. The detergent may comprise one or more polymers. Examples include carboxymethylcellulose, poly(vinylpyrrolidone), poly(ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic acid / acrylic copolymers, and lauryl methacrylate / acrylic acid copolymers. The detergent may include a bleaching system, which may comprise a source of H₂O₂ such as perborate or percarbonate that may be combined with a peracid-forming bleach activator such as a tetraacetylethylenediamine or nonanoyloxybenzenesulfonate. Alternatively, the bleaching system may comprise peroxyacids of the amide, imide, or sulfone type. In general, when a bleaching agent is used, the compositions of the present invention may comprise from approximately 0.1% to approximately 50% or even from approximately 0.1% to approximately 25%, of bleaching agent by weight of the cleaning composition of the invention. The enzyme variants of the invention can be stabilized using conventional stabilizing agents, and / or protease inhibitors, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, salts such as sodium chloride and potassium chloride, lactic acid, formic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenylboronic acid derivative such as 4-formylphenylboronic acid, or a peptide aldehyde such as di-, tri- or tetrapeptide aldehydes or aldehyde analogues (either in the form of B1-B0-R where, R is H, CH3, CX3, CHX2, or CH2X (X=halogen), B0 is a simple amino acid residue (preferably with an optionally substituted aliphatic or aromatic side chain); and B1 consists of one or more amino acid residues (preferably one, two, or three) optionally comprising an N-terminus protecting group, or as described in WO09118375, WO98 / 13459) or a protein-like protease inhibitor such as RASI, BASI, WASI (bifunctional alpha-amylase / subtilisin inhibitors from rice, barley, and wheat) or CI2 or SSI. The composition may be formulated as described in, for example, WO 92 / 19709 and WO 92 / 19708 or US-6472364.In some embodiments, the enzymes employed in the present invention are stabilized by the presence of water-soluble sources of zinc (II), calcium (II) and / or magnesium (II) ions in the finished compositions that provide said ions to the enzymes, as well as other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II), and oxovanadium (IV)). The composition may also include other conventional detergent ingredients such as, for example, fabric conditioners (including clays), foam boosters, soap scum suppressants, anti-corrosion agents, soil suspending agents, soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, organic solvents such as ethanol, or perfumes. In addition, the detergent may include a pretreat or booster, which is added to the wash to increase the overall level of cleaning; some of these additives can also be used as a pretreatment agent applied to the textile material before the washing stage. It is currently contemplated that any enzyme, particularly the enzyme of the invention, can be added to detergent compositions in an amount corresponding to 0.001-100 mg of enzyme protein per liter of washing solution, preferably 0.005-5 mg of enzyme protein per liter of washing solution, more preferably 0.01-1 mg of enzyme protein per liter of washing solution, and particularly 0.1-1 mg of enzyme protein per liter of washing solution. However, the compositions of the present invention comprise at least 0.0001 to approximately 0.1% by weight of pure enzyme protein, such as approximately 0.0001% to approximately 0.01%, approximately 0.001% to approximately 0.01%, or approximately 0.001% to approximately 0.01%.However, when a formulated enzyme is used, the detergent composition comprises from approximately 0.02% to approximately 20% by weight, such as from approximately 0.05% to approximately 15% by weight, or from approximately 0.05% to approximately 20%, or from approximately 0.05% to approximately 5%, or from approximately 0.05% to approximately 3%. The alpha-amylase variants useful in the present invention can be further incorporated into the detergent formulations described in WO 97 / 07202, which is incorporated herein by reference. The detergent composition of the invention may be in any convenient form, for example, a bar, tablet, powder, granule, paste, gel, or liquid. The composition may be a heavy-duty universal cleaning agent, a universal paste form, a heavy-duty liquid type, a liquid for delicate fabrics, a hand dishwashing agent, a gentle dishwashing agent, a high-foaming type, an automatic dishwasher agent, various tablets, dishwashing granules, dishwashing liquid, and a rinse aid. The composition may also include unit-dose packaging, including those known in the art and those that are water-soluble, water-insoluble, and / or water-permeable.A liquid detergent can be aqueous, typically containing a maximum of 70% water and 0-30% organic solvent, or non-aqueous, or a solution containing more than 0.5 g / l of the detergent composition. The composition of the invention can be formulated, for example, as a detergent composition for hand or machine washing, including a laundry additive composition suitable for pretreating stained fabrics and a fabric softener composition added during rinsing; or formulated as a detergent composition for use in general household cleaning operations on hard surfaces; or formulated for hand or machine dishwashing. The detergent can be in powder or granular form, or in the form of a liquid, gel, or paste; or in the form of a unit-dose product such as a tablet or pouch, including multi-compartment pouches; or the detergent can be in the form of a sheet. Example of detergent composition for washing clothes The following are liquid detergent compositions for washing clothes especially suitable for top-loading washing machines (1 and 2) and front-loading washing machines (3), respectively. Examples of dishwasher detergents The following examples 4-8 of dishwasher detergents are in the form of gels. 2.0R Silicate is supplied by PQ Corporation, Malvern, PA, USA. Sodium carbonate is supplied by Solvay, Houston, Texas, USA. Sodium percarbonate (2Na2CO3.3H2O2) supplied by Solvay, Houston, Texas, USA. Hydroxyethanediphosphonate (HEDP) is marketed by Dow Chemical, Midland, Michigan, USA. Dishwashing detergent compositions The enzyme of the invention can also be used in detergent compositions for dishwashing, including the following: 1) Powder composition for automatic dishwashing 2) Powder composition for automatic dishwashing 3) Powder composition for automatic dishwashing Enzymes 0.000 - 0.1% 4) Powder composition for automatic dishwashing 5) Powder composition for automatic dishwashing 6) Composition of powder and liquid dishwashing liquid with surfactant cleaning system 7) Non-aqueous liquid composition for automatic dishwashing 8) Non-aqueous liquid dishwashing composition 9) Thixotropic liquid composition for automatic dishwashing 10) Liquid composition for automatic dishwashing 11) Liquid composition for automatic dishwashing containing protected bleach particles 12) Compositions for automatic dishwashing as described in 1), 2), 3), 4), 6) and 10), wherein perborate is replaced by percarbonate. 13) Automatic dishwashing compositions as described in 1.- 6) which additionally contain a manganese catalyst. The manganese catalyst may, for example, be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Nature, 369, 1994, pp. 637-639. The present invention is also directed to methods of using compositions comprising alpha-amylase variants for cleaning. The alpha-amylase variant is preferably incorporated into and / or used in conjunction with detergent compositions, for example, laundry detergent compositions, such as household laundry detergent compositions, especially liquid laundry detergent compositions. Specifically, the detergent composition comprises at least one chelating agent and typically includes conventional detergent adjuvants / ingredients such as surfactants (anionic, cationic, nonionic, hybrid ion, amphoteric), detergency boosters, bleaches, polymers, other enzymes, and other ingredients, for example, as described in WO2007 / 130562 and WO2007 / 149806, which are incorporated herein by reference in their entirety. Therefore, in a useful aspect of the present invention, a cleaning method is provided comprising adding a composition according to the invention to a cleaning process.In preferred embodiments, this cleaning process is selected from the group consisting of at least one cleaning step in a laundry, dishwashing, industrial, or institutional cleaning process. Due to their activity at alkaline pH values, the α-amylases of the invention are well-suited for use in various industrial processes. In particular, the enzyme has potential applications as a component in detergent compositions for laundry, dishwashing, and hard surface cleaning, but it can also be useful in the production of sweeteners and ethanol from starch. The conditions for conventional starch conversion and liquefaction and / or saccharification processes are described, for example, in US patent publication 3,912,590 and EP patent publications 252,730 and 63,909. Materials and methods Enzymes: SP722: Seq. ID No.: 6, marketed by Novozymes, and described in document WO 95 / 26397. SP707 or #707: Sec ID No.: 8 (comparative) AA560: Sec ID No.: 10 (comparative) General methods of molecular biology: Unless otherwise stated, DNA manipulations and transformations are carried out using standard molecular biology methods (Sambrook et al. (1989); Ausubel et al. (1995); Harwood and Cutting (1990). Alpha-amylase fermentation and variants Fermentation can be carried out using methods well known in the technique or in the following way. A strain of B. subtilis containing the relevant expression plasmid is plated onto a CL medium plate with a relevant antibiotic and cultured overnight at 37°C. Colonies are transferred to 100 ml of BPX medium supplemented with a relevant antibiotic (e.g., chloramphenicol at 10 mg / L) in a 500 ml shaking flask. Composition of the BPX medium: Potato starch 100 g / l Barley flour 50 g / l BAN 5000 SKB 0.1 g / l Sodium caseinate 10 g / l Soybean seed flour 20 g / l Na2HPO4, 12 H2O 9 g / l Antifoaming agent 0.1 g / l The culture is agitated at 37°C at 270 rpm for 4 to 5 days. Cells and cell debris are removed from the fermentation broth by centrifugation at 4,500 rpm for 20–25 minutes. The supernatant is then filtered to obtain a completely clear solution. The filtrate is concentrated and washed on a UF filter (a 10,000 cutoff membrane), and the buffer is changed to 20 mM acetate at pH 5.5, for example, by dialysis or gel filtration. The UF filtrate is applied to S-Sepharose FF (General Electric, Cation Exchange, Matrix: crosslinked agarose, functional group: -OCH₂CHOHCH₂OCH₂CH₂CH₂SO₃), and elution is carried out by stepwise elution with 0.2 M NaCl in the same buffer. The eluate is dialyzed against 10 mM Tris (2-amino-2-hydroxymethyl-propane-1, 3-diol), pH 9.0 and applied in a Q-sepharose FF (General Electric, anion exchange, matrix: crosslinked agarose, functional group: -OCH2CHOHCH2OCH2CHOHCH2N+(CH3)3) and eluted with a linear gradient of 0-0.3M NaCl with 6 column volumes.The fractions containing the activity (measured by the EnzCheck assay) are collected, the pH is adjusted to 7.5, and any remaining color is removed by treatment with 0.5% w / v activated carbon for 5 minutes. It may also be advantageous to add another buffer change step, e.g., by dialysis or gel filtration, to a buffer system that does not affect the washing result itself, e.g., EPPS buffer, glycine buffer, acetate buffer, or similar, preferably with a small concentration of calcium (e.g., 0.1 mM) to stabilize the amylase during storage and approximately 0.01% Triton X-100 to reduce the risk of enzyme protein adsorption to containers and pipettes. Detergent model Composition of detergent model A: Composition of detergent model B: Free calcium ion measurement assay The following test can be used for the measurement of free calcium ions in solution and thus for the determination of the ability of chelating agents (chelants) to reduce the concentration of free calcium ions (Ca2+) from, e.g., 2.0 mM to 0.10 mM at pH 8. Test principle: Various amounts of chelating agents are added to a 2.0 mM Ca²⁺ solution, and the free Ca²⁺ concentration is determined using a calcium ion-selective electrode at a fixed pH and temperature. The concentration of chelating agent required to reduce the free calcium concentration from 2.0 mM to 0.10 mM can be determined from a plot of the measured free calcium concentration against the concentration of chelating agent. In this assay, the concentration of chelating agent required to reduce the free calcium concentration from 2.0 mM to 0.10 mM is measured at pH 8, at 21 °C, in potassium chloride and 49 mM EPPS. Solutions: Electrolyte solution: 4 M potassium chloride in ultrapure water (Milli-Q water). pH 8 buffer: 50 mM EPPS (4-(2-hydroxyethyl)piperazine-1-propanesulfonic acid) adjusted to pH 8.0 using minimal amounts of 1 N sodium hydroxide. Calcium stock solution: Ca2+ 25 mM in pH 8 buffer, prepared from CaCl22H2O. Chelant stock solution: 15 mM chelant (relative to 100% dry chelant) in pH 8 buffer, readjusted to pH 8.0 using trace amounts of 1 M NaOH or 11 M HC. Ultra-pure water (Milli Q water) is used for the preparation of all buffers and solutions. Equipment: Thermo Scientific calcium ion selective electrode (cat. no. 9720BNWP) calibrated against a standard calcium chloride solution. The electrode is calibrated according to the guidelines for the electrode. Procedure: A series of vials are prepared, each containing 4 ml of calcium stock solution (final concentration 2.0 mM), 1 ml of electrolyte solution (final concentration 80 mM potassium chloride), chelating agent stock solution in varying amounts (0-45 ml), and using pH 8 buffer to adjust the total volume to 50 ml. The final concentration of EPPS in the assay is 49 mM. After mixing, the free Ca2+ concentration is measured using the calcium electrode. The free calcium concentration should be determined at a sufficient number of different chelating agent concentrations for each agent tested, ensuring that the data set covers the entire range from 2.0 mM free calcium ions to less than 0.10 mM, or that the final chelating agent concentration in the assay is greater than 10.0 mM. An adequate number of data points is eight or more. The chelating agent concentration required to reduce the initial 2.0 mM free calcium ions to 0.10 mM is obtained by interpolating a plot of the measured free calcium ion concentration against the chelating agent concentration. The solutions are equilibrated to the desired temperature, which in this test is 21 °C. Determination of log K Chelating agents can also be characterized by the binding constant of the chelating agent (chelant) and calcium ions. This constant can be determined by ITC (isothermal titration calorimetry) as described in AD Nielsen, CC Fuglsang and P Westh, Analytical Biochemistr vol.314 (2003) pp.227-234 and T Wiseman, S Williston, JF Brandts and LN Lin, Analytical Biochemistr vol.179 (1989) pp.131-137. All glassware and plastic bottles used are washed with a 1% (w / w) EDTA solution and then thoroughly rinsed in Chelex 100 treated ultrapure water (Milli-Q water). The solutions are stored in plastic bottles and kept at 5°C until use. Tampons: HEPES 20 mM (2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid), pH 8 prepared with ultrapure water (Milli-Q water) Glycine 20 mM, pH 10 prepared with ultrapure water (Milli-Q water) Solutions: - 125 M chelating agent in 20 mM HEPES, pH 8 or 125 M chelating agent in 20 mM glycine, pH 10 - 24 mM CaCl in 20 mM HEPES, pH 8 or 24 mM CaCl in 20 mM glycine, pH 10 - Ultrapure water (Milli-Q water) All buffers are passed through Quelex 100 columns (Sigma Aldrich C-7901, 1% matrix, cross-linked polystyrene matrix, active group iminodiacetic acid (sodium form) matrix bonded via methyl group to aromatic rings) to remove calcium ions. All solutions are degassed by vacuum shaking before experiments. Instrument: MCS ITC (MicroCal Inc., Northampton, MA, USA) Procedure The reference cell is filled with ultrapure water (Milli-Q water). The sample cell is filled with the chelating solution at the selected pH, and the syringe is filled with the calcium solution at the selected pH. The solutions are equilibrated to the desired temperature, for example, 19 °C. Next, the chelating solution from the sample cell is titrated volumetrically with 30-40 aliquots of 8 l of the calcium solution. The signals obtained from the ITC are then integrated using the Origin software provided by MicroCal Inc. To obtain the binding isotherms, regression routines are developed using the same software package. These data are then fitted to a model using the routines built into the Origin software. Currently, the "OneSites" model is preferred, as it provides the best fit for most commonly used chelating agents; that is, the residuals are uniformly distributed around zero. From the K value, log K is calculated as the base-10 logarithm of the K value. Tests to determine cleaning capacity To evaluate the cleaning capacity of alpha-amylase variants in a detergent composition, washing experiments can be performed. The enzymes are tested using the Automatic Mechanical Stress Assay (AMSA) or the washing capacity test, using beakers. With the AMSA test, the cleaning capacity of a wide range of detergent solutions containing small volumes of enzyme can be examined. The AMSA plate has a series of grooves for test solutions and a lid that firmly presses the fabric sample to be washed against all the groove openings. During the washing time, the plate, test solutions, textile material, and lid are vigorously shaken to bring the test solution into contact with the textile material and apply mechanical stress in a periodically oscillating manner.For a further description, see WO02 / 42740, especially the paragraph "Special method embodiments" on page 23-24. Overview of cleaning capacity: A test solution was prepared comprising water (15°dH), 0.8 g / L detergent, e.g., detergent A or B as described above, or 50 mM HCO3-, and the enzyme of the invention, e.g., at a concentration of 0, 0.2, 0.4, 0.8, and / or 1.2 mg of enzyme protein / L. Starch-stained fabrics (e.g., CS-28 from Center For Testmaterials BV, PO Box 120, 3133 KT, Vlaardingen, The Netherlands) were added and washed for 30 minutes at 20°C. After thorough rinsing under running water and drying in the dark, the light intensity or reflectance values ​​of the stained fabrics were subsequently measured as a measure of cleaning ability. The test with 0 mg of enzyme protein / L was used as a blank to obtain a delta remission value. Preferably, mechanical action is applied during the washing stage, for example, in the form of agitation, turning or revolution of the washing solution with the fabric. AMSA cleaning capacity experiments can be carried out under the experimental conditions specified below: Detergent Detergent model A or B Detergent dosage 0.8 g / l Volume of test solution 160 micro l pH As is Wash time 30 minutes Temperature 20 °C Water hardness 15°dH Enzyme concentration in the solution of trial 0; 0.2; 0.4; 0.8; 1.2 mg / l CS-28 (Rice starch on Test material (cotton) The water hardness was adjusted to 15°dH by adding CaCl2, MgCl2, and NaHCO3 (Ca2+:Mg2+:HCO3- = molar ratio 4:1:7.5) to the test system. After washing, the fabrics were rinsed with running water and dried in the dark. The effectiveness of an enzyme variant is measured as the brightness of the color of fabric washed with that specific amylase. Brightness can also be expressed as the intensity of light reflected from the sample when illuminated with white light. When the sample is stained, the intensity of the reflected light is lower than that of the clean sample. Therefore, the intensity of reflected light can be used to measure the cleaning power of an amylase. Color measurements are performed using a professional horizontal scanner (Kodak iQsmart, Kodak), which is used to capture an image of the washed fabric. To extract a light intensity value from the scanned images, the 24-bit pixel values ​​of the image are converted to red (r), green (g), and blue (b) values, also known as RGB values. The intensity value (Int) is calculated by summing the RGB values ​​together as vectors and then taking the length of the resulting vector. Textiles: CS-28 fabric samples (rice starch on cotton) can be obtained from Center For Test materials BV, PO Box 120, 3133 KT Vlaardingen, The Netherlands. The beaker cleaning capacity test is a trial in a small-scale model of a top-loading washing machine, and is used to evaluate the washing effectiveness of amylases.The beaker cleaning capacity test, in which 250 ml beakers and a paddle stirrer providing a rotating oscillating motion, 180° in each direction, at a frequency of 80 per minute, are used, comprises the following steps: providing 100 ml of wash solution (6 °C, 15° dH, pH 8.0) containing 350 mM NaHCO3 and enzyme at 0.4 mg / l; adding two CS-28 samples (5x5 cm) and two EMPA 162 samples (5x5 cm) to the wash solution to begin washing; setting the stirring speed to 80 rpm; stopping the stirring after 60 minutes, rinsing the samples with cold running water; drying the rinsed samples in the dark overnight; and assessing the cleaning capacity by measuring the emission of incident light at 460 nm using Color Eye as described below. Equipment and materials Water bath (5 °C) with circulation; Glass beakers (250 ml); one rotating arm per beaker with a capacity of 100 ml of washing solution; test samples: CS-28 (rice starch on cotton) from the Center for Testmaterials BV, Vlaardingen, Netherlands and EMPA 162 (rice starch on cotton / polyester) from EMPA Testmaterials AG, St. Gallen, Switzerland, the samples are cut into 5x5 cm. Washing solution: NaHCO350 mM buffer solution, pH 8.0, water hardness: 15° dH, Calcium:Magnesium ratio of 4:1. Amylase stock solution: 1 mg of enzyme protein per ml. - A 0.1% (w / v) solution of Triton-x-100 and 1 mM CaCl2O in ultrapure water (MilliQ water) is used for amylase dilution (amylase dilution regulator). Measurement with Color Eye The cleaning capacity is expressed as a delta remission (Rem) value. Light reflectance assessments of the samples were performed using a Macbeth Color Eye 7000 reflectance spectrophotometer with a very small oval aperture, i.e., 0.7 cm² (~0.7 x 1.0 cm). Measurements were taken without UV in the incident light, and remission was extracted at 460 nm. The sample to be measured was placed on top of another sample of the same type before measurement to reduce reflection from the piston pushing the sample up against the measuring aperture. Delta remission values ​​were calculated for individual samples by subtracting the remission value of the sample washed without added amylase (control) from the remission value of the sample washed with amylase. Assays for measuring amylolytic activity (alpha-amylase activity) EnzChek test Amylase activity or residual amylase activity can be determined using the following EnzCheck assay. The substrate is a corn starch derivative, DQ™ starch (BODIPY FL corn starch conjugate), which is corn starch labeled with BODIPY® FL dye (4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-5-indacen-3-propionic acid) to such an extent that fluorescence is inactivated. A vial containing approximately 1 mg of lyophilized substrate is dissolved in 100 µL of 50 mM sodium acetate, pH 4.0. The vial is vortexed for 20 seconds and allowed to stand at room temperature in the dark, with occasional stirring, until the substrate is dissolved. Next, 950 l of 10 mM sodium acetate, Triton X100 ( (polyethylene glycol p- (1, 1, 3, 3-tetramethylbutyl) -phenyl ether 0, 01 % (w / v) (C14H22O (C2H4O) n (n = 9-10) ) ), pH 5, 0, are added, shaken well in a vortex and stored at room temperature, in the dark until ready for use.Starting from 1 ml of this solution, the substrate working solution was prepared by mixing with 5 mL of HEPES 50 mM, Triton X1000, 01% (w / v), CaCl21 mM, pH 7, 0. The enzyme-containing detergent is diluted to a concentration of 15 ng of enzyme protein / ml (6826, 7 times dilution) in HEPES 50 mM, Triton X1000, 01%, CaCl21 mM, pH 7, 0. For the assay, 25 µL of the substrate working solution are mixed for 10 seconds with 25 µL of the diluted enzyme in a black 384-well microtiter plate. Fluorescence intensity (excitation: 485 nm, emission: 555 nm) is measured once every two minutes for 30 minutes in each well at 25 °C, and Vmax is calculated as the slope of the graph of fluorescence intensity versus time. The graph should be linear, and the residual activity test should be adjusted so that the diluted reference enzyme solution is within the linear range of the activity assay. In some cases, there is significant interference from the amylase-free detergent in the assay. In these cases, alternative amylase assays may be used. The interference of a detergent in an amylase assay can be analyzed by adding a known quantity of amylase to the detergent at two concentrations and then measuring the activity of both samples. If the difference in the measured activities corresponds to the differences in the levels of the added amylases, the assay can be used to determine the residual amylase activity after storage. PNP-G7 Trial Alpha-amylase activity can be determined using a method that employs the substrate PNP-G7. PNP-G7, an abbreviation for 4,6-ethylidene(G7)-p-nitrophenyl(G1)-, D-maltoheptaoside, is a blocked oligosaccharide that can be cleaved by an endoamylase, such as alpha-amylase. Following cleavage, the alpha-glucosidase included in the kit further digests the hydrolyzed substrate, releasing a free PNP molecule that is yellow and can therefore be measured by spectrometry in the visible range at 405 nm (400–420 nm). Kits containing PNP-G7 substrate and alpha-glucosidase are manufactured by Roche / Hitachi (cat. no. 11876473). Reagents: The G7-PNP substrate in this kit contains 4, 6-ethylidene- G7-PNP 22 mM and HEPES (2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid), pH 7, 0) 52.4 mM. The alpha-glucosidase reagent contains HEPES 52, 4 mM, NaCl 87 mM, MgCl212, 6 mM, CaCl20, 075 mM (4 kU / l of alpha-glucosidase). The working substrate solution is prepared by mixing 1 ml of alpha-glucosidase reagent with 0.2 ml of G7-PNP substrate. This working substrate solution is prepared immediately before use. Dilution buffer: EPPS 50 mM, Triton X100 (polyethylene glycol p-(1,1,3,3-tetramethylbutyl)-phenyl ether (C14H22O (C2H4O) n (n = 9-10) ) ) , 0.01% (w / v) , CaCl21 mM, pH 7.0. Procedure: The amylase sample to be analyzed was diluted in dilution buffer to ensure that the pH of the diluted sample was 7. The assay was carried out by transferring 20 µl of the diluted enzyme sample to a 96-well microtiter plate and adding 80 µl of substrate working solution. The solution was mixed and pre-incubated for 1 minute at room temperature, and the absorbance was measured every 20 s for 5 minutes at an OD of 405 nm. The slope (absorbance per minute) on the time-dependent absorption curve is directly proportional to the specific activity (activity per mg of enzyme) of the alpha-amylase in question under the given set of conditions. The amylase sample should be diluted to a level where the slope is below 0.4 absorbance units per minute. Determination of the percentage point (pp) The improvement in percentage points (pp) in the residual activity (stability) of the variant with respect to the precursor is calculated as the difference between the residual activity of the variant and the residual activity of the precursor, i.e., the residual activity of the variant minus the residual activity of the parent. Examples Example 1: Preparing variants The amylase variants of sec. Id. no. 6 SP722 were prepared using conventional procedures, in summary: introducing random and / or site-directed mutations into the gene, transforming Bacillus subtilis host cells with the mutated genes, culturing the transformed host cells (e.g., as described in example 1 of WO 2004 / 111220), and purifying the amylase from the fermentation broth. The reference amylase (sc. Id. no. 6) was produced recombinantly in Bacillus subtilis in a similar manner. Example 2 Characterization of chelating agents Example 2a: Measurement of free calcium ions Chelating agents (chelants) can be classified by their ability to reduce the concentration of free calcium ions (Ca2+) from 2.0 mM to 0.10 mM at pH 8, a measurement developed from a method described by MK Nagarajan et al., JAOCS, vol.61, no. 9 (September 1984), pp.1475-1478. The assay described above in "Materials and Methods" was used to measure free calcium ions. Therefore, the concentration of chelating agent required to reduce water hardness from 2.0 mM to 0.10 mM was determined, as previously described. The experiment was conducted using pH 8 buffer at 21 °C. The final concentrations of chelating agent used and the measured free Ca2+ concentration are shown below in Table I. Table I Free Ca2+ concentration determined in a mixture of 2.0 mM Ca2+ and various amounts of chelating agent at pH 8. Based on these data, the concentration of chelating agent needed to reduce the concentration of free Ca2+ from 2.0 mM to less than 0.10 mM was determined by interpolation and the results are presented in Table II. A series of chelating agents were characterized using this assay, and Table II shows the concentrations of chelating agent needed to reduce the concentration of free calcium ions from 2.0 mM to 0.10 mM at pH 8.0 in 49 mM EPPS buffer and 80 mM potassium chloride. Table II Example 2b Determination of log K Alternatively, chelating agents can be characterized by the binding constant of the chelating agent (chelant) and calcium ions. This constant can be determined by ITC (isothermal titration calorimetry) as described in A.D. Nielsen, C.C. Fuglsang, and P. Westh, Analytical Biochemistr. vol. 314 (2003) pp. 227–234 and T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin, Analytical Biochemistr. vol. 179 (1989) pp. 131–137. The procedure for determining log K is described. Using this procedure, the following log K values ​​were determined at pH 10 (see Table III): Table III Example 3: Residual activity after incubation with chelating agent EnzChek test Amylase activity or residual amylase activity is determined in the present invention by the EnzCheck assay as described above. In general, the residual amylase activity in detergent model B was determined after incubation at 31 °C for 18 hours; the activity was then compared with the activity of a reference incubated at 4 °C for 18 hours as described above. Stability test of amylase variants in detergent with chelating agent For the determination of amylase stability in detergent, the enzymes under test were adjusted to a concentration of 0.6 mg / ml of enzyme protein by dilution in 20 mM HEPES, Triton X100 at 0.1% (w / v), pH 8.0. If the initial amylase concentration is too low, it can be concentrated by ultrafiltration (UF) using a UF membrane with a cutoff of 10 kDa. 25 µL of amylase solution and 125 µL of detergent (model B detergent) were transferred to a 96-well microtiter plate in 4 replicates. A small magnet (5 x 2 mm) was placed in each well, and the mixture was stirred for 5 minutes at room temperature on a magnetic stirrer. Two identical plates were prepared. One plate was incubated at 4 °C for 18 hours (reference sample), and the other plate was incubated at 31 °C for 18 hours (31 °C sample). Immediately after incubation, the plate samples were analyzed for amylase activity as described in the EnzCheck assay for determining residual amylase activity in detergents. It should be noted that to minimize interference from detergent ingredients other than the enzyme in the assay, both the reference and 31 °C samples were diluted to the same protein concentration. The activity of both the reference and 31 °C samples was determined in the same 384-well plate. It was ensured that the reference amylase was included in all microtiter plates for the assay. Residual activity was calculated as 100 * Vmax (31 °C sample) / Vmax (reference sample). The results are shown in Table IV using SP722 or SP722 + D183* G184* as the reference (parental) amylase. The improvement in percentage points (pp) in residual activity of the variant compared to the parental variant is calculated as the difference between the percentage of residual activity of the variant and that of the parental variant. Table IV The results clearly show that the variants of the invention are considerably more resistant to the presence of strong chelating agents than the reference alpha-amylase. In some cases, the residual activity is greater than 100, reflecting the analytical variance of the assay. The results show that the variants of the invention, also at pH 8.0, have improved stability compared to the reference alpha-amylase, which can be SP722 of Id. sec. no. 6 or Id. sec. no. 6 + DI83* G184*, which is Id. sec. no. 6 where amino acids 183 and 184 have been removed. Example 4: Residual activity after incubation with chelating agent at pH 8 and pH 10 In this example, the PNP-G7 assay described above is used to determine residual amylase activity after incubation in the presence of the chelating agent DTPA, but the principle is the same as that used to determine activity using the EnzCheck assay. In general, residual amylase activity was determined after incubation in a buffer containing a chelating agent at pH 8 and 49 °C or at pH 10 and 42 °C for 1 hour, and the activity was then compared to the activity of a reference incubated at 4 °C for 1 hour as described above in "Materials and Methods". Stability test of amylase variants after incubation with chelating agent at pH 8 and pH 10 in buffer Principle: Enzyme samples were incubated in pH 8.0 buffer with a final concentration of 1.5% DTPA at 49 °C for 1 h, and reference samples were incubated at 4 °C for 1 h. Additionally, enzyme samples were incubated in pH 10.0 buffer with a final concentration of 1.5% DTPA at 42 °C for 1 h, and their reference samples were incubated at 4 °C for 1 h. After incubation, residual activity was determined using the PNP-G7 amylase activity assay. Reagents: pH 8 buffer with DTPA: 50 mM EPPS, 01% Triton pH 10 buffer with DTPA: 50 mM EPPS, 01% Triton Amylase solutions: 0.25 and 0.5 mg of active amylase protein / ml in EPPS 5 mM, Triton X-100 (w / v) 0.01%, pH 8.0 Procedure: 160 µL of buffer (either pH 8 buffer with DTPA or pH 10 buffer with DTPA) and 40 µL of the amylase solutions were transferred in duplicate to a 96-well PCR microtiter plate, and the contents were mixed for 1 minute (PCR: polymerase chain reaction). The final DTPA concentration was 1.5% in each well. 20 µL from each well were transferred to a new PCR microtiter plate (PCR MTP), which was placed at 4 °C (reference sample). The PCR MTP was incubated in the PCR equipment for 1 h at 49 °C, when the buffer had a pH of 8.0 (samples at pH 8, 49 °C) and for 1 h at 42 °C, when the buffer had a pH of 10.0 (samples at pH 10, 42 °C). Immediately after incubation, the samples on PCR plates were diluted tenfold in dilution buffer, and the amylase activity level was analyzed as described in the PNP-G7 assay. It should be noted that to reduce interference from the chelating agent, here DTPA, in the assay, both the reference sample and the pH 8, 49 °C / pH 10, 42 °C sample were diluted to the same concentration before analyzing residual activity. The activity of both the reference samples and the pH 8, 49 °C or pH 10, 42 °C samples was determined in the same 96-well plate. Parental amylase was included in all assay microtiter plates. Residual activity was calculated as 100*Vmax (pH 8, 42 °C or pH 10, 49 °C sample) / Vmax (reference sample) and the results are shown in Table V. Percentage point (pp) improvements are calculated as the residual activity of the variant minus the residual activity of the original. Tabla V pH 8, 49 °C pH 10, 42 °C Actividad Mejora en pp con Actividad Mejora en pp con residual respecto a la parental residual (%) respecto a la parental (%) Enzima SP722 SP722+ SP722 SP722+ D183* 184* D183* 184* SP722 (parental) 1 0 8 0 SP722 + D183* G184* (parental) 2.- 0 2.- 0 SP722 + D183* G184* N195F V206L 97 96 77 93 85 73 Y243F SP722 + D183* G184* N195F V206Y 97 96 77 100 92 80 Y243F SP722 + D183* G184* N195F V206N 96 95 75 92 84 64 Y243F SP722 + D183* G184* N195F V206F 101 100 80 97 89 69 Y243F SP722 + D183* G184* N195F V206H 92 92 72 88 80 60 SP722 + D183* G184* N195F V206Y 95 94 74 96 88 68 SP722 + D183* G184* V206F Y243F 87 86 66 89 81 61 SP722 + D183* G184* N195F V206L 98 97 77 96 88 68 H210Y SP722 + D183* G184* S193T V206L 79 78 58 73 65 45 SP722+D183* G184* G133E G149R 90 89 69 83 75 55 N195Y Y203F V206L The results clearly show that the variants of the invention are highly stable and have high residual activity after incubation at pH 8 and 49 °C and pH 1042 °C for 1 hour, both when comparing the residual activities of the variants with that of the parent and when observing the improvement of the variants in percentage points. In comparison, amylase SP722 + D183* G184* has a residual activity of 20%, and SP722 has an even lower residual activity. Example 5: Residual activity after incubation in buffer with 1.5% (w / v) DTPA at pH 8 and pH 10 In this example, the PNP-G7 assay described above is used to determine the residual amylase activity of SP722 variants after incubation in the presence of the DTPA chelating agent. In general, the residual amylase activity was determined after incubation in a buffer containing a chelating agent at pH 8 or pH 10 and at the indicated temperatures, and the incubation times and activity were then compared with the activity of a reference incubated at 4 °C as described above in "Materials and Methods". Stability test of amylase variants after incubation with chelating agent at pH 8 and pH 10 in buffer Principle: Enzyme samples were incubated in buffer at pH 8.0 with a final concentration of 1.5% (w / v) DTPA at the indicated temperature and time, and their reference samples were incubated at 4°C for the same duration. After incubation, residual activity was determined using the PNP-G7 amylase activity assay. Reagents: pH 8 buffer with DTPA: 50 mM EPPS, 01% (w / v) Triton pH 10 buffer with DTPA: Glycine 50 mM, Triton Amylase solutions: 0.25 and 0.5 mg of active amylase protein / ml in EPPS 5 mM, Triton X-100 (w / v) 0.01%, pH 8.0 Procedure: 160 µL of buffer (either pH 8 buffer with DTPA or pH 10 buffer with DTPA) and 40 µL of the amylase solutions were transferred in duplicate to a 96-well PCR microtiter plate, and the contents were mixed for 1 minute (PCR: polymerase chain reaction). The final DTPA concentration was 1.5% (w / v) in each well. 20 µL from each well were transferred to a microtiter plate (MTP), which was incubated at 4 °C (reference sample). The PCR MTP (stressed sample) was incubated in the PCR equipment as described in the table below. Immediately after incubation, the samples on PCR plates were diluted tenfold in dilution buffer, and the amylase activity level was analyzed as described in the PNP-G7 assay. It should be noted that to reduce interference from the chelating agent, here DTPA, in the assay, both the reference and stressed samples were diluted to the same concentration before analyzing the residual activity. The activity of both the reference and stressed samples was determined on the same 96-well plate. Parental amylase was included in all assay microtiter plates. Residual activity was calculated as 100 * Vmax (stressed sample) / Vmax (reference sample). The percentage point (pp) improvement in residual activity of the variants compared to the parental sample was calculated as the residual activity of the variant minus the residual activity of the parental sample.The results are shown in Table 5.1. Table VI: SP722 variants with DTPA chelator Based on residual activities, it is clear that SP722 variants are more stable in the presence of DTP A, which is also reflected in the percentage point improvements in variant stability compared to the parental variant. Example 6: Residual activity after incubation with HEDP at pH 10 In this example, the PNP-G7 assay described above is used to determine residual amylase activity after incubation in the presence of the chelating agent HEDP. In general, residual amylase activity was determined after incubation in a buffer containing a chelating agent at pH 10 and the indicated temperatures, and the incubation times and activity were then compared with the activity of a reference incubated at 4 °C as described above in "Materials and Methods". Stability test of amylase variants after incubation with chelating agent at pH 10 in buffer Principle: The enzyme samples were incubated in buffer at pH 10.0 with a final concentration of 1.5% (w / v) HEDP at the indicated temperature and time, at 4 °C for the same incubation time. After incubation, the residual activity was determined using the PNP-G7 amylase activity assay. Reagents: pH 10 buffer with HEDP: Glycine 50 mM, Triton X1000, 0.01% (w / v), HEDP (1-hydroxyethylidenediphosphonic acid, CAS No. 2809-21-4) 1.875% (w / v), pH 10.0 Amylase solutions: 0.25 and 0.5 mg of active amylase protein / ml in EPPS 5 mM, Triton X-100 (w / v) 0.01%, pH 8.0 Procedure: 160 µL of buffer (pH 10 buffer with HEDP) and 40 µL of the amylase solutions were transferred in duplicate to a 96-well PCR microtiter plate and the contents were mixed for 1 minute (PCR: polymerase chain reaction). The final HEDP concentration was 1.5% (w / v) in each well. 20 µL from each well were transferred to a microtiter plate (MTP) that was incubated at 4 °C (reference sample). The PCR MTP (stressed sample) was incubated in the PCR equipment as described in Table 6.1 below. Residual activity was calculated as 100*Vmax (stressed sample) / Vmax (reference sample). The improvement in percentage points (pp) of the residual activity of the variants with respect to the parental is calculated as the residual activity of the variant minus the residual activity of the parental. Table VII: SP722 and its variant with HEDP The results clearly show that the variant is more stable when incubated in the presence of HEDP compared to the parental variant. Example 7: Stability of SP722+D183* G184* and variants thereof with 1.5% (w / v) HEDP In this example, the PNP-G7 assay described above is used to determine residual amylase activity after incubation in the presence of the chelating agent HEDP. In general, residual amylase activity was determined after incubation in a buffer containing a chelating agent at pH 8 or pH 10 at the indicated temperatures, and the incubation times and activity were then compared with the activity of a reference incubated at 4 °C as described above in "Materials and Methods". Stability test of amylase variants after incubation with chelating agent at pH 8 and pH 10 in buffer Principle: The enzyme samples were incubated in buffer at pH 8.0 with a final concentration of 1.5% (w / v) HEDP at the indicated temperature and time, and their reference samples were incubated at 4°C for the same duration. After incubation, residual activity was determined using the PNP-G7 amylase activity assay. Reagents: pH 8 buffer with HEDP: EPPS 50 mM, Triton pH 10 buffer with HEDP: Glycine 50 mM, Triton X1000, 0.01% (w / v), HEDP (1-hydroxyethylidenediphosphonic acid, CAS No. 2809-21-4) 1.875% (w / v), pH 10.0 Amylase solutions: 0.25 and 0.5 mg of active amylase protein / ml in EPPS 5 mM, Triton X-100 (w / v) 0.01%, pH 8.0 Procedure: 160 µL of buffer (either pH 8 buffer with HEDP or pH 10 buffer with HEDP) and 40 µL of the amylase solutions were transferred in duplicate to a 96-well PCR microtiter plate, and the contents were mixed for 1 minute (PCR: polymerase chain reaction). The final HEDP concentration was 1.5% (w / v) in each well. 20 µL from each well were transferred to a microtiter plate (MTP) that was incubated at 4 °C (reference sample). The PCR MTP (stressed sample) was incubated in the PCR equipment as described in Table 7.1 below. Residual activity was calculated as 100*Vmax (stressed sample) / Vmax (reference sample). The improvement in percentage points (pp) of the residual activity of the variants with respect to the parental is calculated as the residual activity of the variant minus the residual activity of the parental. Table VIII: Variants SP722 + D183* G184* with HEDP The results clearly show that the SP722+D183* G184* variants are much more stable when incubated in the presence of HEDP as a chelating agent. Example 8: Stability of AA560 variants in the presence of DTPA 1.5% (w / v) or HEDP 1.5% (w / v) In this example, the PNP-G7 assay described above is used to determine residual amylase activity after incubation in the presence of the chelating agent DTPA or HEDP. In general, residual amylase activity was determined after incubation in a buffer containing a chelating agent at pH 8 or pH 10 and at the indicated temperatures, and the incubation times and activity were then compared with the activity of a reference incubated at 4 °C as described above in "Materials and Methods". Stability test of amylase variants after incubation with chelating agent at pH 8 and pH 10 in buffer Principle: Enzyme samples were incubated in buffer at pH 8.0 with a final concentration of 1.5% (w / v) DTPA or HEDP at the indicated temperature and time, and their reference samples were incubated at 4°C for the same duration. After incubation, residual activity was determined using the PNP-G7 amylase activity assay. Reagents: pH 8 buffer with DTPA: 50 mM EPPS, 01% (w / v) Triton pH 10 buffer with DTPA: Glycine 50 mM, Triton pH 8 buffer with HEDP: EPPS 50 mM, Triton pH 10 buffer with HEDP: Glycine 50 mM, Triton X1000, 0.01% (w / v), HEDP (1-hydroxyethylidenediphosphonic acid, CAS No. 2809-21-4) 1.875% (w / v), pH 10.0 Amylase solutions: 0.25 and 0.5 mg of active amylase protein / ml in EPPS 5 mM, Triton X-100 (w / v) 0.01%, pH 8.0 Procedure: 160 µL of buffer (pH 8 buffer with DTPA or HEDP or pH 10 buffer with DTPA or HEDP) and 40 µL of the amylase solutions were transferred in duplicate to a 96-well PCR microtiter plate, and the contents were mixed for 1 minute (PCR: polymerase chain reaction). The final concentration of DTPA or HEDP was 1.5% (w / v) in each well. 20 µL from each well were transferred to a microtiter plate (MTP), which was set to 4 °C (reference sample). The PCR MTP (stressed sample) was incubated in the PCR equipment as described in Tables 8.1 and 8.2 below. Residual activity was calculated as 100*Vmax (stressed sample) / Vmax (reference sample). The improvement in percentage points (pp) of residual activity of the variants with respect to the parental sample is calculated as the residual activity of the variant minus the residual activity of the parental sample. Table IX: AA560 variants with DTPA Table 8.2: AA560 variants with HEDP Example 9: Residual activity after incubation in detergent with chelating agent In this example, the PNP-G7 assay is used to determine residual amylase activity after incubation in the detergent in the presence of chelating agents, as described in Example 5. In general, residual amylase activity was determined after incubation in detergent C containing the chelating agents DTPMP and HEDP at pH 8.2 after 3 weeks and 6 weeks at 30 °C. The residual amylase activity is then compared with the amylase activity in the freshly prepared detergent on day zero (before incubation) as described below. Table X Stability test of amylase variants after incubation in detergent C with chelating agents at pH 8.2. Method: Samples of detergent C, pH 8.2, were prepared, each containing an amylase variant of the invention or the id. of sec. no. 6 (SP722) with the following two deletions D183* + G184*, also denoted as SP722 + D183* + G184*. The initial residual enzymatic activity was determined for each detergent sample before incubation (reference samples). The residual enzyme activity of each sample was determined after incubation at 30 °C for 3 and 6 weeks and compared to its reference sample. Residual activity was determined using the PNP-G7 amylase activity assay. Amylase solutions: 13.77 mg of active amylase protein in 100 g of detergent C, pH 8.2 Procedure: Detergent C, 5 g pH 8.2, containing amylase, was placed in duplicate into a 7 ml glass bottle with an airtight cap. Residual enzyme activity was determined for the initial samples, in duplicate, before incubation. The samples were incubated for 3 weeks and 6 weeks at 30 °C. Immediately after incubation, the residual samples were analyzed for amylase activity as described in the PNP-G7 assay. In this assay, 100% residual activity is defined as no loss of amylase activity compared to the initial residual enzyme activity before incubation (reference sample). The percentage point (pp) improvement in residual activity (stability) of the variant compared to the parent is calculated as the difference between the residual activity of the variant and the residual activity of the parent. Table XI The results clearly show that the variants of the invention are highly stable and have high residual activity after incubation in detergent C at pH 8 for 2, 3, and 6 weeks at 30°C. In comparison, amylase SP722 + D183* G184* has a residual activity of 19% after 3 weeks and 3% after 6 weeks. This specification cites several references, the descriptions of which are incorporated herein in full by reference. The invention described and claimed herein shall not be limited in scope by the specific embodiments described herein, as these embodiments are intended as illustrations of various aspects of the invention. It is intended that any equivalent embodiment be within the scope of this invention. In fact, various modifications of the invention, in addition to those shown and described herein, will be obvious to those skilled in the art from the foregoing description. It is intended that such variations be included within the scope of the appended claims. In case of conflict, this specification, including the definitions, shall prevail. The dimensions and values ​​described in this document should not be understood as being strictly limited to the exact numerical values ​​stated. Instead, unless otherwise indicated, each of these dimensions is intended to mean both the stated value and a functionally equivalent interval around that value. For example, a dimension described as "40 mm" is intended to mean "approximately 40 mm."

Claims

1. A cleansing composition comprising: (a) a variant of a parental alpha-amylase, wherein the parental alpha-amylase is an alpha-amylase having the amino acid sequence shown in Seq. Id. No. 6, wherein the variant has amylolytic activity, and wherein the alpha-amylase variant has the amino acid sequence shown in Seq. Id. No. 6 with one of the following sets of mutations using the numbering according to Seq. Id. No. 6: D183* G184* N195F; D183* G184* N195L; D183* G184* N197F; D183* G184* N197L; D183* G184* A186R, N195F; D183* G184* H210Y; D183* G184* V206L; D183* G184* V213A; Q174R D183* G184* E212V; D183* G184* V206L E212G G304V A447V; N116T G133E K142R D183* G184* Y198N V206L; G133E D183* G184* N195Y Y198N Y200F; N116T D183* G184* N195Y Y198N; K142R P146S G149K D183* G184* N195Y Y198N V206I; D134Y D183* G184*; T151R D183* G184* H210Y K320N R359I N418D; G147E G149R Q169E D183* G184* Y198N Y203F V206L; G133E G149R D183* G184* N195YY198N Y203F V206L; G147E Y152H Q169E D183* G184* Y198N V206L; D183* G184* N195F V206L; D183* G184* N195F Y243F; D183* G184* N195F H210Y; D183* G184* V206L H210Y; D183* G184* V213A; D183* G184* S193T; D183* G184* A186T N195F; D183* G184* N195F V206L Y243F; D183* G184* V206L Y243F; D183* G184* N195Y; G133D G149R D183* G184* Y198N V206L; N116T G133E G147E Y152H D183* G184* Y198N Y203F V206L; G147E G149R D183* G184* N195F Y198N V206L; G133E K142R D183* G184* N195F Y198N; G133E G149R Y152H D183* G184* N195Y Y198N V206L; N116T Q129L K142R D183* G184* N195Y Y198N Y203F V206L; G133E G149R Y152H D183* G184* N195Y Y198N Y203F V206L; N116T G133E G149R D183* G184* Y198N Y203F V206L; D183* G184* N195F V206Y Y243F; D183* G184* N195F V206C Y243F; D183* G184* N195F V206T Y243F; D183* G184* N195F V206N Y243F; D183* G184* N195F V206C; D183* G184* N195F V206H; D183* G184* N195F V206Y; D183* G184* N195F V206L; D183* G184* N195F V206G Y243F; D183* G184* V206F Y243F; D183* G184* N195F V206I Y243F; D183*G184* N195F V206F Y243F; D183* G184* N195F V206S Y243F; D183* G184* A186T N195F; D183* G184* N195F V206L H210Y; D183* G184* S193T V206L; D183* G184* S193T V213A; D183* G184* S193T Y243F; D183* G184* N195F V206N; N195F; V206L; V206Y; Y243F; N195F V206L; N195F V206L Y243F; and D183* G184* G133E G149R N195Y Y203F V206L; and (b) a cleaning aid, preferably in an amount from 0.01 to 99.9% by weight; and (c) at least one chelating agent wherein said chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured at 21 °C and pH 8.

0.

2. A composition according to claim 1, wherein: (a) the chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured in 80 mM potassium chloride and 49 mM 4-(2-hydroxyethyl)piperazine-1-propanesulfonic acid (EPPS) at 21 °C and pH 8.0; and / or (b) the chelating agentat a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM when measured in the assay described in Example 2a; and / or (c) the chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a concentration of the chelating agent below 8 mM, preferably below 7 mM, preferably below 6 mM, preferably below 5 mM, preferably below 4 mM; and / or (d) the chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a concentration of the chelating agent below 0.9 times the concentration of citrate capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM, measured at 21 °C and pH 8; and / or (e) the chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a concentration of the chelating agent below 0.7 times, such as below 0.5times, such as below 0.3 times the citrate concentration capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM.

3. A cleaning composition according to claim 1 or claim 2 comprising at least one chelating agent, wherein said chelating agent is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at a chelating agent concentration less than 0.9 times the citrate concentration capable of reducing free calcium ions from 2.0 mM to 0.10 mM, when measured at 21 °C and pH 8.

0.

4. A composition according to claim 1 or claim 2, wherein: (a) the variant has at least 60% residual activity after 18 hours at pH 8 and 31 °C in the presence of a chelating agent, wherein said chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at 21 °C and pH 8.0; and / or (b) the variant has at least 70% ofresidual activity after 18 hours at pH 8 and 31 °C in the presence of a chelating agent wherein said chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at 21 °C and pH 8.0 and wherein the residual activity is measured as described in "Materials and Methods"; and / or (c) the variant has an improved washing performance compared to the original alpha-amylase when measured in AMSA as described in "Materials and Methods".

5. The composition according to any preceding claim, wherein the chelating agent is selected from the group consisting of: ethylenediamine tetraacetate (EDTA), methylglycinediacetic acid (MGDA), ethylene glycol tetraacetic acid (EGTA), diethylenetriaminepentaacetic acid (DTPA), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP), and mixtures thereof.

6. A composition according to any preceding claim, whereinThe variant has improved stability with respect to the parental alpha-amylase Id. of sec. no. 6 in a composition comprising a chelating agent, wherein said chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at 21 °C and pH 8.0, preferably wherein the variant has at least 60% residual activity after 18 hours at pH 8 in the presence of a chelating agent wherein said chelating agent at a concentration below 10 mM is capable of reducing the concentration of free calcium ions from 2.0 mM to 0.10 mM at 21 °C and pH 8.0, wherein the residual activity is measured as described in "Materials and Methods".

7. A composition according to any of the preceding claims, wherein the chelating agent is selected from the group consisting of: diethylenetriaminepentaacetic acid (DTPA), 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP), methylglycinediacetic acid (MGDA), acid8. A composition according to any of the preceding claims, wherein the cleaning aid comprises one or more of: a perfume microcapsule, a fabric-tinting agent, a protease, a polyethyleneimine polymer, a lipase, and any mixture thereof.

9. A composition according to any of the preceding claims, wherein the composition is a liquid laundry detergent composition.

10. A method of washing clothes, comprising washing a garment with a composition according to any of the preceding claims, preferably at a temperature of 30°C or less, or more preferably at a temperature of 20°C or less.