Chemistry: molecular biology and microbiology – Carrier-bound or immobilized enzyme or microbial cell;... – Enzyme or microbial cell is immobilized on or in an organic...
Reexamination Certificate
1993-08-20
2001-07-24
Naff, David M. (Department: 1651)
Chemistry: molecular biology and microbiology
Carrier-bound or immobilized enzyme or microbial cell;...
Enzyme or microbial cell is immobilized on or in an organic...
C435S134000, C435S178000, C435S198000, C435S263000, C435S264000, C435S877000
Reexamination Certificate
active
06265191
ABSTRACT:
FIELD OF THE INVENTION
The present invention relates to the field of use of lipases in laundry applications. More broadly, it relates to modification of surfaces such as for oil stain removal, improved wettability and anti-redeposition. More particularly, it relates to formation of hydrolase-fabric complexes which are stable and hydrolytically active during laundering, drying and use, and provide increased oil stain removal, wettability and anti-redeposition properties.
BACKGROUND OF THE INVENTION
Lipases are enzymes naturally produced by a wide variety of living organisms from microbes to higher eukaryotes. Fatty acids undergoing oxidation in tissues of higher animals must be in free form (that is, non-esterified) before they can undergo activation and oxidation. Thus, intracellular lipases function to hydrolyze the triacylglycerols to yield free fatty acids and glycerol. Enzymes useful in the present invention will be referred to as “lipases”, but include enzymes described as being a “hydrolase” or “cutinase”, as well as a “lipase”, because the useful enzymes form hydrolysis by-products from oil substrates. All three terms and enzymes are contemplated and included by the use of the term “lipase” herein.
Bacterial lipases are classically defined as glycerolesterhydrolases (EC 3.1.1.3) since they are polypeptides capable of cleaving ester bonds. They have a high affinity for interfaces, a characteristic which separates them from other enzymes such as proteases and esterases.
Cutinases are esterases that catalyze the hydrolysis of cutin. For example, cutinase allows fungi to penetrate through the cutin barrier into the host plant during the initial stages of a fungal infection. The primary structures of several cutinases have been compared and shown to be strongly conserved. Ettinger,
Biochemistry.
26, pp. 7883-7892 (1987). Sebastian et al.,
Arch. Biochem. Biophys.,
263 (1), pp. 77-85 (1988) have recently found production of cutinase to be induced by cutin in a fluorescent
P. putida
strain. This cutinase catalyzed hydrolysis of p-nitrophenyl esters of C
4
-C
16
fatty acids.
Because of this ability, lipases have long been considered as potential components in detergent compositions, and lipases obtained from certain Pseudomonas or Chromobacter microorganisms have been disclosed as useful in detergent compositions: Thom et al., U.S. Pat. No. 4,707, 291, issued Nov. 17, 1987 and Wiersema et al., European Patent Application 253,487, published Jan. 20, 1988. However, although lipases hydrolyze oil in solutions simulating laundry wash compositions, they have not proven to be very effective in removing oil stains from fabrics.
PCT application WO 88/09367 suggests the use of one of the lipases employed in the present invention in laundry applications. However, the method of use suggested merely comprises conventional use in laundry solutions or cleaning compositions. This lipase, so used by conventional methods, is no more effective than other lipases in removing oil stains from fabrics. Therefore, a need remains for effective utilization for the potential of lipases for removing oil stains in laundry applications.
Fabric treatments with non-enzyme compounds are known to alter the properties of fabric surfaces. For example, paralleling the development of durable-press and wash/wear fabrics, has been work on imparting oil and water repellency to fabrics. A widely used treatment utilizes a fluorochemical (sold by Minnesota Mining and Manufacturing Company under the mark Scotchgard) and another composition used for such fabric treatment is sold by E.I. du Pont de Nemours & Co. under the trademark Zepel. But oil and water repellant treated fabric have posed difficulties in removing stains by laundering, due to the fact that these repellant treatments make the fabric hydrophobic, and the oils forced onto such fabrics (particularly clothing at collar and cuffs) therefore are difficult to remove. One approach to this problem has been to treat the fabrics with soil release polymers. However, a need remains for imparting improved oil stain removal properties to surfaces, and particularly to fabrics exposed to significant oil staining, such as table cloths, aprons and clothing at body contact points such as collars and cuffs.
The use of lipases and/or cutinases in imparting oil hydrolysis activity during storage or wear has not been previously recognized.
When soil is released from fabric during laundering there is a further problem of redeposition of the oily soil on the previously cleaned fabric. This problem is well recognized. U.S. Pat. No. 4,909,962, issued Mar. 20, 1990, inventor Clark, attributes the redeposition of oily soil, in part, to phase separation (at least in the case of a pre-spotting composition when diluted with water in the wash bath). U.S. Pat. No. 4,919,854, issued Apr. 24, 1990, inventors Vogt et al., discloses detergent and cleaning preparations which include redeposition inhibitors described as water-soluble, generally organic, colloids (e.g. polymeric carboxylic acids and gelatin).
SUMMARY OF THE INVENTION
The present invention provides a novel use of the oil hydrolyzing potential of lipases for removing oil stains from fabrics more effectively than prior art attempts to utilize lipases for laundry cleaning applications.
In one aspect of the present invention, a method for modifying surfaces is provided to facilitate oil removal therefrom and comprises selecting a surface to be modified and then immobilizing (by chemical or physical means) an lipase onto the surface by forming a surface-lipase complex. The immobilized lipase is isolatable from Pseudomonas organisms. Suitable enzymes are lipases that are isolated from an organism expressing a coding region found in or cloned from
P. putida
ATCC 53552 or P. sp., more preferably from the
putida
species. A particularly preferred lipase is isolated with a molecular weight of about 30,000 daltons and is resolvable as a single band by SDS gel electrophoresis. The surfaces on which the enzyme is immobilized can be solid (e.g. glass) or can be fabrics (natural, synthetic, or metallic, woven or non-woven).
In another aspect of the present invention, a fabric is provided that is treated to have improved oil stain removal properties. The treated fabric has a lipase immobilized on the surface, forming a fabric-lipase complex. The fabric-lipase complex has substantial hydrolysis activity for oil stains during both subsequent use and laundering, and is resistant to removal during such use in laundering. Thus, although initial use of even the preferred lipases will not be effective for oil stain removal, the fabric-lipase-complex is effective for oil stain removal. The preferable lipase used to form the fabric-hydrolase complex is isolated from
Pseudomonas putida
ATCC 53552, including modifications such as mutants or clones.
In yet another aspect of the present invention, a fabric treating composition, useful to improve oil stain removal of fabrics, comprises a solid or gelled carrier and the lipase described above. The lipase is dispersed in the carrier and can be applied to fabric, and once applied, the lipase sorbs and forms the fabric-lipase complexes.
Fabric having improved oil stain removal properties in accordance with the present invention can be repeatedly laundered without effective loss of such preparation because the lipase used is immobilized to the fabric, resists removal during laundering, and has substantial hydrolysis activity for oil stains on the fabric in both air and laundering solutions. The inventive treatments can be used to treat fabrics either before or after exposure to oily stains. The fabrics so treated need not be immediately laundered because the fabric-lipase complexes are hydrolytically active even on dry fabric in ambient air.
Other applications of the ability for the immobilized lipase to modify surfaces include uses to alter the wettability of the surface on which the lipase is sorbed. Thus, for example, solid plastic or glass surfaces having surface modifications in accordance with the
Anderson Susan A.
El-Sayed Maha Y.
Leiske Daniel R.
Mizusawa Eugene A.
Wiersema Richard J.
Coudert Brothers
Naff David M.
The Clorox Company
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