Reduction of malodor from laundry

Details Reduction of malodor from laundry Reduction of malodor from laundry

2002-02-14

2004-09-21

Einsmann, Margaret (Department: 1751)

Cleaning compositions for solid surfaces, auxiliary compositions

Cleaning compositions or processes of preparing

Enzyme component of specific activity or source

C510S393000, C008S115510, C435S263000, C435S264000

Reexamination Certificate

active

06794350

ABSTRACT:

FIELD OF THE INVENTION
The invention relates to enzymatic reduction of malodor from laundry.
BACKGROUND
Clothes that have been used for e.g. sports activities or in other ways have been exposed to sweat from the wearer during use are often difficult to clean in terms of the smell of sweat and other body odors (malodor), when subjected to wash in a laundry machine.
SUMMARY OF THE INVENTION
We have found that an enzyme having lysostaphin activity is capable of reducing malodor from laundry. Accordingly, the invention provides a method comprising contacting laundry with an enzyme having lysostaphin activity.
In a second aspect, there is provided a composition comprising a surfactant and an enzyme having lysostaphin activity.
In another aspect, an enzyme is used for reducing malodor in laundry.
DETAILED DESCRIPTION
Lysostaphin
The enzyme Lysostaphin is a glycyl-glycine endopeptidase from the enzyme class E.C. 3.4.24.75. It hydrolyses the —Gly—Gly—bond in the polyglycine inter-peptide link joining staphylococcal cell wall peptidoglycans. Lysostaphin is commercially available from several suppliers, such as from Sigma-Aldrich, Inc.
An enzyme having lysostaphin activity may be a natural or synthetic variant of lysostaphin, wherein amino acid substitutions or deletions have been introduced. It may also be an amino acid fragment with lysostaphin activity, which is optionally fused to one or more other proteins.
Lysostaphin Activity
One unit of lysostaphin activity will reduce the turbidity (absorbance at 620 nm) of a suspension of
Staphylococcus aureus
(ATCC 6538) cells by 50%, when the initial absorbance is approximately 0.250, after 10 minutes at pH 7.5 and 37 degrees Celsius.
Malodor
During wear, fabrics are contaminated with microorganisms from the human skin together with sebaceous lipids, sweat and dead skin cells serving as microbial substrates. Particularly at mild wash conditions these microorganisms survive laundering. A consequence of microorganisms surviving household laundering is malodor generation in the fabrics. We have now found that these microorganisms are mainly Staphylococcus species.
The malodor of the method of the invention thus comprises all body odors present in laundry originating from contact with the human skin. In an embodiment the malodor may be axillary odors, such as the smell of sweat.
In another embodiment, the malodor may originate from activity of Staphylococcus species (such as
S. aureus, S. epidermis, S. intermedius, S. saprophyticus
and
S. hyicus
).
In yet another embodiment the malodor originates from fabrics, which have been in contact with the axilla.
Evaluation of Malodor
Wet laundry swatches are placed in tinted 200 ml glasses with snap lids. A trained sensory panel (10 persons) evaluates the odor by sniffing the headspace over the wet items and indicating the total odor intensity. The odor intensity is indicated on a scale from 0 to 15 where 0 equals ‘no malodor’ and 15 equals ‘very strong malodor’. All evaluations are performed twice (double determinations). The swatches are evaluated after approximately 24 hours and after 48 hours (swatches are kept in the glasses at all times). An average of all 20 evaluations (10 persons each evaluate twice) is calculated after both 24 hours and 48 hours. These average values are referred to as “Malodor index (24 hours)” and “Malodor index (48 hours)”.
Laundry
The laundry of the method of the invention comprises all kinds of textile items or fabrics suitable for being used as clothes or for personal use in other ways comprising contact with the human skin.
Methods and Uses
By contacting laundry with an enzyme having lysostaphin activity, as defined in the method of the invention, the “Malodor index (48 hours)”, as defined above, may be reduced by at least 10% (preferably 20%, more preferably 30%, most preferably 40%, and in particular 50%) compared to laundry which has not been contacted with an enzyme having lysostaphin activity.
The method of the invention may also result in killing or inhibiting growth of microbial cells in laundry. In an embodiment the microbial cells are bacteria, such as Staphylococcus species. In another embodiment, the method of the invention may result in a reduction in the number of living microbial cells of at least 25%, preferably at least 50%, more preferably at least 90%, and most preferably at least 99%.
In the context of the present invention the term “inhibiting growth of microbial cells” is intended to mean that the cells are in the non-growing state, i.e., that they are not propagating. The term “microbial cells” denotes bacterial cells (such as Staphylococcus species), fungal cells or algae, and the term “microorganism” denotes a fungus (including yeasts) or a bacterium.
The present invention covers use of an enzyme for reducing malodor from laundry items. In an embodiment, the enzyme may have lysostaphin activity. The invention may also be used for reducing the number of living bacteria in laundry; for reducing allergens in laundry; or for sterilizing laundry.
Detergent composition
Lysostaphin may be added to and thus become a component of a detergent composition.
The detergent composition of the invention may for example be formulated as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.
In a specific aspect, the invention provides a detergent additive comprising lysostaphin. The detergent additive as well as the detergent composition may comprise one or more other enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, e.g., a laccase, and/or a peroxidase.
In general the properties of the chosen enzyme(s) should be compatible with the selected detergent, (i.e. pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
Proteases: Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. The protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279). Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583.
Examples of useful proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274.
Preferred commercially available protease enzymes include Alcalase™, Savinase™, Primase™, Everlase™, Esperase™, and Kannase™ (Novozymes A/S), Maxatase™, Maxacal™, Maxapem™, Properase™, Purafect™, Purafect OXP™, FN2™, and FN3™ (Genencor International Inc.).
Lipases: Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from
H. lanuginosa
(
T. lanuginosus
) as described in EP 258 068 and EP 305 216 or from
H. insolens
as described in WO 96/13580, a Pseudomonas lipase, e.g. 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, e.g. from
B. subtilis
(Dartois e

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