Bleaching and dyeing; fluid treatment and chemical modification – Cleaning or laundering
Reexamination Certificate
1998-11-13
2001-03-06
Gupta, Yogendra (Department: 1751)
Bleaching and dyeing; fluid treatment and chemical modification
Cleaning or laundering
C510S220000, C510S221000, C510S226000, C510S235000, C510S238000, C510S276000, C510S300000, C510S320000, C510S321000, C510S337000, C510S344000, C510S392000, C510S393000, C510S405000, C510S530000, C510S531000, C435S201000, C435S202000, C435S203000, C435S204000, C134S025200, C134S025300, C134S042000
Reexamination Certificate
active
06197070
ABSTRACT:
TECHNICAL FIELD
The present invention relates to detergent compositions comprising a combination of different &agr;-amylases delivering improved malodor stripping from soiled items in hard surface cleaning, dishwashing and laundry applications.
BACKGROUND OF THE INVENTION
For a number of years amylase enzymes have been used for a variety of different purposes, the most important of which are starch liquefaction, textile desizing, starch modification in the paper and pulp industry, and for brewing and baking. A further use of amylases which is becoming increasingly important, is the removal of starch containing soils and stains during the washing of fabrics, hard surfaces and dishes.
Indeed, amylase enzymes have long been recognised in dishwashing, hard surface cleaning and laundry compositions to provide the removal of starchy food residues or starchy films from dishware, flatware, glasses and hard surfaces or to provide cleaning performance on starchy soils as well as other soils typically encountered in laundry applications.
WO94/02597, Novo Nordisk A/S published Feb. 3, 1994, describes cleaning compositions which incorporate mutant amylases. See also WO94/18314, Genencor, published Aug. 18, 1994 and WO95/10603, Novo Nordisk A/S, published Apr. 20, 1995.
Other amylases known for use in cleaning compositions include both &agr;- and &bgr;-amylases. &agr;-Amylases are known in the art and include those disclosed in EP 252,666; WO91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent specification no. 1,296,839 (Novo).
Examples of commercial &agr;-amylases products are Termamyl®, Ban® and Fungamyl®, all available from Novo Nordisk A/S Denmark.
Recently new amylases have been identified and are described in WO95/26397, Novo Nordisk A/S, published Oct. 5, 1995, disclosing an &agr;-amylase having a specific activity superior than Termamyl®.
Combinations of an &agr;-amylase with a starch debranching enzyme selected from pullulanase, isopullulanase and iso amylase are described in EP 368 341, J04065494 and J06172796 for enhanced detergency against dirt containing starch, fat, oils and proteins in laundry and automatic dishwashing.
It has now been discovered that odorous materials are entrapped into different types of amylase-susceptible and everyday stains found on fabrics, dishware, hard surfaces and the like and that an uncomplete and unefficient removal of such stains leads to malodor formation.
It has now surprisingly been found that the combined use of different &agr;-amylases improves the removal of malodor coming from different types of amylase-susceptible and everyday stains. Especially good malodor control on everyday stains such as body soils is obtained when the amylases are further combined with a cellulase.
It is therefore an object of the present invention to provide detergent compositions containing &agr;-amylases which exhibit a good malodor control on amylase-susceptible and everyday stains.
It is another object of the present invention to provide detergent compositions containing &agr;-amylase enzymes which exihibit a good malodor control on body soils.
SUMMARY OF THE INVENTION
The present invention relates to detergent compositions comprising a combination of different &agr;-amylases delivering improved malodor stripping from soiled items in hard surface cleaning, dishwashing and laundry applications.
DETAILED DESCRIPTION OF THE INVENTION
&agr;-Amylase Enzymes
Essential components of the detergent compositions of the present invention are &agr;-amylase enzymes.
Without wishing to be bound by any theory, it is believed that a combination of several &agr;-amylases provides a more effective activity in solution and/or a broader hydrolytic cleavage pattern than a single amylase type as different amylases show different hydrolytic activity on various substrates. Odorous materials are entrapped into these substrates and a rapid and effective hydrolysis achieved on several different cleavage points allows a more effective suspension and dissolution of the odorous materials therein entrapped.
Suitable &agr;-amylases include those disclosed in U.S. Pat. No. 5,003,257; EP 252,666; WO91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent specification no. 1,296,839 (Novo). Examples of commercial &agr;-amylases products are Termamyl®, Ban® and Fungamyl®, all available from Novo Nordisk A/S Denmark. Other suitable &agr;-amylases are derived from
B. Subtilis
or
B. stearothermophilus.
Other &agr;-amylases herein have the commonality of being derived using site-directed mutagenesis from one or more of the Bacillus &agr;-amylases, regardless of whether one, two or multiple amylases strains are the immediate precursors.
&agr;-Amylases of this invention include those amylases having improved stability in detergents, especially improved oxidative stability. In general, the stability-enhanced amylases can be obtained from Novo Nordisk A/S or from Genencor International:
(a) An amylase according the WO94/02597, Novo Nordisk A/S published Feb. 3, 1994:
(i) a variant &agr;-amylase wherein one or more of the Met amino residues is exchanged with any amino acid residue except for Cys and Met,
(ii) a Bacillus &agr;-amylase according to (i),
(iii) a variant &agr;-amylase according to (i-ii) wherein one or more Met amino acid residues is exchanged with a Leu, Thr, Ala, Gly, Ser, Ile, or Asp amino acid residue, preferably a Leu, Thr, Ala or Gly amino acid residue,
(iv) a variant &agr;-amylase according to (i) in which substitution is made, using preferably Ala or Thr (more preferably Thr), of the Met residue located in position 197 of the
B. lichenformis
&agr;-amylase, or the homologous position variation of as similar parent amylase, such as
B. amyloliquefaciens, B. Subtilis
, or
B. stearothermophilus;
(b) Stability-enhanced amylases, including Purafact Ox AM®, as described in WO94/18314, published Aug. 18, 1994. Therein it was noted that improved oxidative stability amylases have been made by Genencor from
B. licheniformis
NCIB8061. Met was identified as the most likely residue to be modified. Met was substitued, one at a time, in positions 8, 15, 197, 256, 304, 366 and 438 leading to specific mutants, particulary important being M197L and M197T with the M197T variant being the most stable expressed variant; corresponding &agr;-amylases will therefore include:
(i) a variant &agr;-amylase that is the expression product of a mutated DNA sequence encoding an &agr;-amylase, the mutated DNA sequence being derived from a precursor &agr;-amylase by the deletion or substitution of one or more oxidisable acids selected from the group consiting of Met, Trp, Cys and Tyr amino acid residues, in the precursor &agr;-amylase,
(ii) a variant &agr;-amylase according to (i) wherein the oxidisable amino acid residue to be deleted or substitued is a Met in the precursor &agr;-amylase equivalent to +8, +15, +197, +256, +304, +366 or +438 in
Bacillus licheniformis
&agr;-amylase,
(iii) a variant &agr;-amylase according to (ii) which is M197T;
(c) Preferred herein are amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S. These amylases are disclosed in WO95/10603, published April 1995:
(i) A variant of a parent &agr;-amylase enzyme having an improved washing and/or dishwashing performance as compared to the parent enzyme, wherein one or more amino acid of the parent enzyme has been replaced by a different amino acid and/or wherein one or more amino acid have been deleted and/or wherein one or more amino acid have been added to the parent &agr;-amylase enzyme, provided that the variant is different from one in which the Met in position 197 of parent
B. licheniformis
&agr;-amylase has been replaced by Ala or Thr amino acid residue, as the only modification being made,
(ii) A variant according to (i) comprising a C-terminal part of an &agr;-amylase derived from
B. licheniformis
and a N-terminal part of an &agr;-amylase derived from
B. amyloliquefaciens
or from
B. stea
Govers Kristien Greta
Horner Thomas Wilhelm
Cook C. Brant
Gupta Yogendra
Mruk Brian P.
The Procter & Gamble & Company
Waugh Kevin L.
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