METHOD FOR CLEANING MEDICAL DEVICES

Description

Reference to a Sequence Listing

[0001] This application contains a Sequence Listing in computer readable form.Background of the Invention

[0002] The present invention relates to the use of compositions comprising a hexosaminidase enzyme for cleaning a medical device and to methods for cleaning a medical device using such compositions.Description of the Related Art

[0003] Surfaces of medical and surgical equipment may become soiled with many different types of organic soiling e.g. from body tissue or feces. Such soils may include proteins from blood and muscular tissue, fats e.g. from adipose tissue and carbohydrates e.g. from feces. Other types of organic soiling may be dead tissue cells, biofilm, or EPS (extracellular polysaccharide substance), produced by various microorganisms. Organic stains may be composed of different molecules such as polysaccharides, macromolecules, and proteins. Biofilm is produced by populations of bacteria or fungi growing attached to a surface. Bacteria growing in biofilms exhibit increased resistance to antimicrobial agents and are difficult to remove. Many biofilms are embellished in a slimy layer termed EPS. Biofilm EPS is a polymeric conglomeration generally composed of proteins, macromolecules and polysaccharides. The presence of biofilm on medical devices, in particular medical indwelling devices and intravascular catheters, is of particular concern in the clinic. Kaplan et.al. (WO 2004 / 061117 A2) has shown that compositions comprising beta-N-acetylglucosaminidase enzymes promote detachment of bacterial or fungal cells from biofilm. The medical industry utilizes devices that are required to be cleaned to remove soil, including organic soil such as blood, faces, dead cells and biofilm from the device. The presence of organic material or soil may contribute to the failure of disinfection by harboring embedded microbes and preventing the penetration of the germicide. Thus, there is a need for efficient cleaning compositions and methods for cleaning of medical devices. Although enzymes have been used to reduce or remove biofilms in industrial and clinical environments, enzymes suitable for cleaning of e.g. medical devices need to be compatible with compositions used for cleaning of such devices. Thus, enzymes suitable for cleaning of e.g. medical devices are preferably those which remove or reduce organic stains such as biofilm and components hereof and are stable in presence of detergent components such as surfactants.

[0004] EP 0 425 017 A2 discloses methods for removing microorganisms such as bacteria from surfaces by treatment with a Type II endoglycosidase.

[0005] WO 2008 / 157350 discloses methods and materials for reducing biofilms, including the use of Dispersin B to detach biofilms.

[0006] WO 2009 / 121183 discloses antibiofilm compositions comprising two or more compounds selected from Dispersin B, 5-fluorouracil, deoxyribonuclease I and Proteinase K.

[0007] Uniprot:A0A075LPR4 is the sequence of a glycoside hydrolase family 20 catalytic domain-containing protein from Terribacillus goriensis.

[0008] The present invention provides methods for cleaning a medical device using cleaning compositions comprising hexosaminidases having beta-N-acetylglucosaminidase activity.Summary of the Invention

[0009] The present invention relates to a method of cleaning a medical device, wherein the method comprises a) contacting the medical device with a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, for a period effective to clean the medical device; b) cleaning the medical device; and optionally c) disinfecting the medical device wherein the hexosaminidase is a polypeptide having at least 80% sequence identity to the amino acid sequence shown in SEQ ID NO: 4, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 5.

[0010] The invention further relates to the use of a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity and at least one adjunct ingredient for cleaning of a medical device, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is selected from the group of polypeptides having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 4, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 5.Detailed Description of the Invention

[0011] Various enzymes are applied in cleaning processes each targeting specific types of soiling such as protein, starch and grease soiling. Enzymes are standard ingredients in detergents for laundry and dish wash. The effectiveness of these commercial enzymes provides detergents which removes much of the soiling. However, organic matters such as EPS (extracellular polymeric substance) comprised in much biofilm constitute a challenging type of soiling due to the complex nature of such organic matters. EPS is mostly composed of polysaccharides (exopolysaccharides) and proteins, but includes other macro-molecules such as eDNA, lipids and other organic substances. A biofilm may include one or more microorganisms, including gram-positive and gram-negative bacteria, algae, protozoa, and / or yeast or filamentous fungi and viruses and / or bacteriophage. Examples of problematic biofilms are dental plaque, infections on medical implants, but also the initial fouling on ship hulls. Biofilms are attributed to the pathogenesis of many infections in humans and are a significant problem in industry in terms of biofouling of exposed surfaces where biofilm colonisation can form the base component of a localised ecosystem which can disrupt and interfere with industrial processes and components. The enzymes used in the invention are capable of reducing and / or removing components of the biofilm such as polysaccharides e.g. PNAG (Poly-N-acetyl glucosamine) in e.g. an EPS layer and thus reducing or removing e.g. biofilm e.g. by detachment of bacterial cells in biofilm on surfaces, such as medical devices. Hexosaminidases, such as dispersins, are known for degrading PNAG, a major component of most biofilm EPS. Compositions comprising hexosaminidases have been shown to effectively promote detachment of bacterial cells from a biofilm on various surfaces (WO04061117 A2). To be effective in a cleaning process the enzymes need to be compatible with the cleaning / detergent components present in the cleaning composition. Thus, a suitable enzyme for e.g. cleaning of medical devices has the capability of reducing or removing organic matter such as PNAG in e.g. biofilm and is stable in a composition suitable for cleaning. Enzymes such as hexosaminidases suitable for medical cleaning should be effective in reducing or removal of the relevant stain and be stable in compositions suitable for medical cleaning. Such compositions usually comprise surfactants, in particular anionic surfactants. Frequently used anionic surfactants include linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) and alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates). The hexosaminidase used according to the present invention has improved stability in the presence of e.g. LAS compared to the hexosaminidases previously used for cleaning medical devices. The hexosaminidases having beta-N-acetylglucosaminidase activity are particularly useful in cleaning of medical devices as they combine the ability to reduce or remove organic stains e.g. comprising PNAG with stability in compositions comprising anionic surfactants.

[0012] The polypeptides suitable for use in medical cleaning and in compositions for medical cleaning are described below. The polypeptides for use in methods according to the invention are hexosaminidases, preferably dispersins. The term "hexosaminidases" means a polypeptide having hexosaminidase activity (hexosaminidases), and includes EC 3.2.1. e.g. that catalyzes the hydrolysis of N-acetyl-D-hexosamine or N-acetyl-glucosamine polymers found e.g. in biofilm. The term includes dispersins and includes polypeptides having N-acetylglucosaminidase activity and β-N-acetylglucosamininidase activity. The term "polypeptide having hexosaminidase activity" may be used interchangeably with the term hexosaminidase and similarly the term "polypeptide having β-N-acetylglucosaminidase activity" may be used interchangeably with the term β-N-acetylglucosamininidase. For the purposes of the present invention, hexosaminidase activity is determined according to the procedure described in Assay I. Hexosaminidases having β-N-acetylglucosamininidase activity include dispersins. The term "dispersin" and the abbreviation "Dsp" means a polypeptide having hexosaminidase activity, EC 3.2.1.- that catalyzes the hydrolysis of β-1,6-glycosidic linkages of N-acetyl-glucosamine polymers (poly-N-acetylglucosamine) found e.g. in biofilm. In preferred embodiments of the invention the hexosaminidases are dispersins.

[0013] In one aspect, the polypeptide having hexosaminidase activity is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus saccharophilus. In a preferred aspect, the polypeptide is a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 1. It may be obtained from Terribacillus, preferably Terribacillus saccharophilus.

[0014] In another aspect, the polypeptide is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus goriensis. In a preferred aspect, the polypeptide is a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 2. It may be obtained from Terribacillus, preferably Terribacillus goriensis.

[0015] In another aspect, the polypeptide is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus saccharophilus. In a preferred aspect, the polypeptide is a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 3. It may be obtained from Terribacillus, preferably Terribacillus saccharophilus.

[0016] In another aspect, the polypeptide having hexosaminidase activity is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus saccharophilus. In a preferred aspect, the polypeptide is a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 4. It may be obtained from Terribacillus, preferably Terribacillus saccharophilus.

[0017] In another aspect, the polypeptide having hexosaminidase activity is a Terribacillus polypeptide, e.g., a polypeptide obtained from Terribacillus saccharophilus. In a preferred aspect, the polypeptide is a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 5. It may be obtained from Terribacillus, preferably Terribacillus saccharophilus.

[0018] The present invention relates to methods for cleaning medical devices or the use of compositions comprising hexosaminidases having beta-N-acetylglucosaminidase activity for cleaning medical devices.

[0019] One embodiment of the invention relates to a method of cleaning a medical device, wherein the method comprises a) contacting the medical device with a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, for a period effective to clean the medical device; b) cleaning the medical device; and optionally c) disinfecting the medical device, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is selected from the group consisting of; i) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 1 or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, ii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 2 or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, iii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 3 or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% % sequence identity hereto, iv) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 4 or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, or v) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 5 or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto.

[0020] Also disclosed herein is a method of cleaning a medical device, wherein the method comprises a) contacting the medical device with a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, for a period effective to clean the medical device; b) cleaning the medical device; and optionally c) disinfecting the medical device, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is selected from the group consisting of: vi) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 6 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, vii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 7 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, viii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 8 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, ix) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 9 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, x) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 10 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xi) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 11 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 12 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xiii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 13 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xiv) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 14 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xv) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 15 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xvi) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 16 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xvii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 17 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xviii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 18 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xix) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 19 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xx) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 20 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xxi) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 21 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xxii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 22 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, xxiii) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 23 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, and xxiv) a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 24 or a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto, preferably wherein the composition is administered as a coating on a medical device implanted in the organism.

[0021] In a method of cleaning a medical device, wherein the method comprises a) contacting the medical device with a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, for a period effective to clean the medical device; b) cleaning the medical device; and optionally c) disinfecting the medical device, the hexosaminidase having beta-N-acetylglucosaminidase activity may be obtained from Terribacillus and selected from the group consisting of a polypeptide comprising the amino acid sequence shown in SEQ ID NOs: 1, 2, 3, 4, 5 and a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or at least 100% sequence identity hereto.

[0022] One embodiment relates to the use of a hexosaminidase having beta-N-acetylglucosaminidase activity, preferably a dispersin, for cleaning of a medical device, wherein the medical device is selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, endoscopes, or wherein the device is a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument

[0023] One aspect of the invention relates to the use of a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, preferably a dispersin and at least one adjunct ingredient for cleaning of a medical device. The composition may comprise a hexosaminidase and at least one surfactant. The adjunct is preferably selected from the group consisting of surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers. The composition may be an anti-biofouling composition and the composition may be a pharmaceutical or cleaning composition.

[0024] One embodiment relates to the use of a composition for cleaning a medical device, wherein the composition comprises; a) at least 0.01 mg / mL hexosaminidases having beta-N-acetylglucosaminidase activity, preferably a dispersin; b) at least one cleaning component, preferably selected from surfactants, builders, bleach components, polymers and dispersing agents.

[0025] The composition preferably comprises at least one anionic surfactant selected from linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) or alcohol ethersulfates (AES or AEOS or FES, alcohol ethoxysulfates or fatty alcohol ether sulfates). The medical device is preferably selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, endoscopes, or wherein the device is a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument. The use for medical cleaning may be indwelling medical device characterized in that at least a portion of a patient-contactable surface of the device is coated with composition comprising the hexosaminidase of the invention. The device may be a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, or wherein the device is a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector or a surgical instrument.

[0026] The choice of additional components is within the skill of the artisan and includes conventional ingredients for the type of composition e.g. cleaning or pharmaceutical compositions, including the exemplary non-limiting components set forth below.

[0027] A composition of the invention comprises a polypeptide having β-N-acetylglucosamininidase activity and preferably an adjunct ingredient. The composition may be an anti-biofouling composition and the composition may be a cleaning or pharmaceutical composition. The adjunct ingredient may be any excipient suitable for e.g. cleaning or pharmaceutical compositions. The adjuncts / excipients are within the choice of the skilled artisan. The adjunct ingredient may be selected from the group consisting of surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers. The compositions may be used for detaching biofilm or preventing biofilm formation on surfaces such as medical devices. The medical device may be characterized in that at least a portion of a patient-contactable surface of the device is coated with composition comprising the hexosaminidase of the invention. The medical device may be selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, endoscope or wherein the device is a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument.

[0028] The invention relates to compositions e.g. cleaning compositions comprising a hexosaminidase having β-N-acetylglucosamininidase activity and an adjunct ingredient, which may e.g. be one or more cleaning adjuncts e.g. cleaning components or pharmaceutical adjuncts e.g. a pharmaceutical expient. The composition may be used for releasing or detachment of bacterial or fungal cells from a biofilm, reducing, removing a biofilm or preventing biofilm formation.

[0029] A composition of the invention may be an anti-biofouling composition comprising one or more antiparasitic, antiviral, antibacterial or antifungal compound.

[0030] The antiparasitic compound can be one or more of a benzazole, such as albendazole, mebendazole and tiabendazole; an azole, such as metronidazole and tinidazole; a macrocycle, such as amphotericin B, rifampin and ivermectin; pyrantel pamoate; diethylcarbamazine; niclosamide; praziquantel; melarsopro; and eflornithine.

[0031] The antiviral compound can be one or more of a nucleoside analog reverse transcriptase inhibitor, such as acyclovir, didanosine, stavudine, zidovudine, lamivudine, abacavir, emtricitabine and entecavir; an uncoating inhibitor such as amantadine, rimantadine and pleconaril; a protease inhibitor such as saquinavir, ritonavir, indinavir, nelfinavir and amprenavir; zanamivir; oseltamivir; and rifampin.

[0032] The antibacterial compound can be one or more of an aminoglycoside such as gentamicin, kanamycin and streptomycin; a beta-lactam such as penicillin, ampicillin and imipenem; a cephalosporin such as ceftazidime, a quinolone such as ciprofloxacin; a macrolide such as azithromycin, clarithromycin, dirithromycin, erythromycin, roxithromycin and telithromycin; an oxazolidinone such as linezolid ; an ansamycin such as rifamycin; a sulphonamide; a tetracycline such as doxycycline; a glycopeptide such as vancomycin; sulfisoxazole, trimethoprim, novobiocin, daptomycin and linezolid.

[0033] The antifungal compound can be one or more of an azole, such as miconazole, ketoconazole, clotrimazole, econazole, omoconazole, bifonazole, butoconazole, fenticonazole, isoconazole, sertaconazole, sulconazole, tioconazole, fluconazole, itraconazole, isavuconazole, ravuconazole, posaconazole, voriconazole, terconazole and abafungin; a macrocycle, such as natamycin, rimocidin, filipin, nystatin, amphotericin B, candicin, hamycin; an allyl amine such as terbinafine, naftifine and butenafine; an echinocandin such as andidulafungin, caspofungin and micafungin; or others such as polygodial, ciclopirox, tolnaftate, benzoic acid, undecylenic acid, flucytosine and griseofulvin.

[0034] The anti-biofouling composition preferably comprises a fungicide or biocide preferably a biocidal quaternary ammonium biocide.

[0035] Also disclosed herein is an indwelling medical device wherein at least a portion of a patient-contactable surface of the device is coated with a composition hexosaminidase having β-N-acetylglucosamininidase activity.

[0036] An indwelling medical device may be one wherein at least a portion of a patient-contactable surface of the device is coated with a composition hexosaminidase having β-N-acetylglucosamininidase activity.

[0037] In one embodiment, the composition is a cleaning composition and the adjunct ingredient is selected from at least one or more cleaning component optionally selected from surfactants, builders, bleach components, polymers, dispersing agents.

[0038] A composition for cleaning a medical advice preferably comprises at least one surfactant. One aspect of the invention relates to a composition comprising; a) at least 0.01 mg / mL hexosaminidases having beta-N-acetylglucosaminidase activity; b) at least one cleaning component, preferably selected from surfactants, builders, bleach components, polymers and dispersing agents.

[0039] Surfactants are typical ingredients of cleaning compositions. Surfactants are added to assist removal of soil and are used extensively in the cleaning industry. The anionic surfactants are the most widely used type of surfactants for laundering, dishwashing compositions. Anionic surfactants are particularly good at keeping the dirt, once dislodged, away from fabrics. Thus, a cleaning composition of the invention preferably comprises at least one anionic surfactant, such as alkylbenzene sulfonates, alkyl sulfates or alkyl ether sulfates.

[0040] One embodiment of the invention relates to the composition comprising at least one anionic surfactant selected from linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) or alcohol ethersulfates (AES or AEOS or FES, alcohol ethoxysulfates or fatty alcohol ether sulfates).

[0041] Not all enzymes are stable in the presence of anionic surfactants. The hexosaminidases obtained from Terribacillus e.g. hexosaminidases comprising the amino acid sequence shown in SEQ ID NOs: 1, 2, 3, 4, 5 or closely related homologues having beta-N-acetylglucosaminidase activity are stable in the presence of anionic surfactants and are particularly useful in cleaning compositions such as cleaning compositions for cleaning of medical devices. The hexosaminidases of the invention are also stable in the presence of nonionic surfactants. Nonionic surfactants are less sensitive to water hardness than anionic surfactants, and they foam less strongly and are thus preferred for low foaming compositions. In a preferred aspect of the invention the cleaning composition comprises at least one anionic surfactant in particular linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) or alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates).

[0042] One aspect of the invention relates to a composition comprising; a) at least 0.01 mg / mL hexosaminidases having beta-N-acetylglucosaminidase activity; b) at least one anionic surfactant preferably selected from linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) and alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates).

[0043] A polypeptide having hexosaminidase activity may be obtained from microorganisms of any genus. The hexosaminidases having beta-N-acetylglucosaminidase activity are preferably selected from any of those listed below.

[0044] The polypeptides useful in the present invention belonging to the Glycoside Hydrolase family 20 (GH20, www.cazy.org). This family includes dispersins such as Dispersin B (DspB) which is β-N-acetylglucosamininidases belonging to the Glycoside Hydrolase 20 family.

[0045] One aspect of the invention relates to a composition for cleaning a medical device comprising; a) at least 0.01 mg / mL hexosaminidase having beta-N-acetylglucosaminidase activity, wherein the hexosaminidase is selected from the group consisting of: a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 1, a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acids sequence shown in SEQ ID NO: 2, a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acids sequence shown in SEQ ID NO: 3, a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acids sequence shown in SEQ ID NO: 4, and a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acids sequence shown in SEQ ID NO: 5; b) at least one cleaning component, preferably selected from the group consisting of: surfactants, builders, bleach components, polymers and dispersing agents, preferably wherein the composition comprises at least one anionic surfactant preferably selected from the group consisting of: linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) and alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates).

[0046] The hexosaminidase may be included in the cleaning e.g. detergent composition of the present invention at a level of at least 0.0001 to at least 100, at least 0.001 to at least 100, at least 0.01 to at least 100, at least 0.02 to at least 100, at least 0.01 to at least 100, at least 0.1 to at least 100, at least 0.2 to at least 100, at least 0.5 to at least 100 mg / mL, preferably, the concentration of hexosaminidase enzyme in the cleaning composition e.g. detergent is in the range 0.01 to 100, 0.1 to 50 or 1 to 10 mg / mL. The detergent composition may comprise at least 0.00008%, preferably at least 0.002%, 0.003%, 0.004%, 0.005%, 0.006%, 0.008%, 0.01%, 0.02%, 0.03%, 0.05%, 0.1%, 0.2%, 0.3%, 0.4%, 0.6%, 0.7%, 0.8%, 0.9% or 1.0% of hexosaminidase enzyme.

[0047] The choice of adjunct ingredients e.g. cleaning components may include consideration of the type of textile to be cleaned, the type and / or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.Surfactants

[0048] The composition preferably comprises one or more surfactants, which may be anionic and / or cationic and / or non-ionic and / or semi-polar and / or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant(s) is typically present at a level of from about 0.1% to 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 3% to about 10%. The surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.

[0049] When included therein the detergent will usually contain from about 1% to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.

[0050] When included therein the detergent will usually contain from about 1% to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.

[0051] When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and / or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.

[0052] When included therein the detergent will usually contain from about 0.01 to about 10 % by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N-(tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof.

[0053] When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.Builders and Co-Builders

[0054] The composition may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof. In a dish wash detergent, the level of builder is typically 40-65%, particularly 50-65%. The builder and / or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and / or co-builder known in the art for use in cleaning detergents may be utilized. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

[0055] The detergent composition may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder. The detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA). Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2,2',2"-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTMPA or DTPMPA), 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), α-alanine-N,N-diacetic acid (α-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) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)ethylenediamine-N,N',N"-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and / or co-builders are described in, e.g., WO 09 / 102854, US 5977053Bleaching Systems

[0056] The composition may contain 0-30% by weight, such as about 1% to about 20%, of a bleaching system. Any bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.Sources of hydrogen peroxide:

[0057] Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide-urea (1 / 1).Sources of peracids:

[0058] Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester. a) Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-α-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, ε-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of the compounds. It is understood that the peracids mentioned may in some cases be best added as suitable salts, such as alkali metal salts (e.g., Oxone ®< ) or alkaline earth-metal salts. b) Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), sodium 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO98 / 17767. A particular family of bleach activators of interest was disclosed in EP624154 and particularly preferred in that family is acetyl triethyl citrate (ATC). ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators. Finally, ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder. Bleach catalysts and boosters

[0059] The bleaching system may also include a bleach catalyst or booster.

[0060] Some non-limiting examples of bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1,2-diylazanylylidene-κN-methanylylidene)triphenolato-κ3O]manganese(III). The bleach catalysts may also be other metal compounds; such as iron or cobalt complexes.

[0061] In some embodiments, where a source of a peracid is included, an organic bleach catalyst or bleach booster may be used having one of the following formulae: (i) (ii) (iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.

[0062] Other exemplary bleaching systems are described, e.g. in WO2007 / 087258, WO2007 / 087244, WO2007 / 087259, EP1867708 (Vitamin K) and WO2007 / 087242. Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.Metal care agents

[0063] Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following: (a) benzatriazoles, including benzotriazole or bis-benzotriazole and substituted derivatives thereof. Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or completely substituted. Suitable substituents include linear or branch-chain Ci-C20- alkyl groups (e.g., C1-C20- alkyl groups) and hydroxyl, thio, phenyl or halogen such as fluorine, chlorine, bromine and iodine. (b) metal salts and complexes chosen from the group consisting of zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cerium salts and / or complexes, the metals being in one of the oxidation states II, III, IV, V or VI. In one aspect, suitable metal salts and / or metal complexes may be chosen from the group consisting of Mn(ll) sulphate, Mn(ll) citrate, Mn(ll) stearate, Mn(ll) acetylacetonate, K^TiF6 (e.g., K2TiF6), K^ZrF6 (e.g., K2ZrF6), CoSO4, Co(NOs)2 and Ce(NOs)3, zinc salts, for example zinc sulphate, hydrozincite or zinc acetate.; (c) silicates, including sodium or potassium silicate, sodium disilicate, sodium metasilicate, crystalline phyllosilicate and mixtures thereof.

[0064] Further suitable organic and inorganic redox-active substances that act as silver / copper corrosion inhibitors are disclosed in WO 94 / 26860 and WO 94 / 26859. Preferably the composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.Hydrotropes

[0065] The composition may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.Polymers

[0066] The composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1% of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and / or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and / or more than one of the below-mentioned motifs. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA / PMA, poly-aspartic acid, and lauryl methacrylate / acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aqualon, and Sokalan ®< HP 165, Sokalan ®< HP 50 (Dispersing agent), Sokalan ®< HP 53 (Dispersing agent), Sokalan ®< HP 59 (Dispersing agent), Sokalan ®< HP 56 (dye transfer inhibitor), Sokalan ®< HP 66 K (dye transfer inhibitor) from BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., WO 2006 / 130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan ®< HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.Fabric hueing agents

[0067] The composition of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when the fabric is contacted with a wash liquor comprising the detergent compositions and thus altering the tint of the fabric through absorption / reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.I.) 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 as described in WO2005 / 03274, WO2005 / 03275, WO2005 / 03276 and EP1876226. The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007 / 087257 and WO2007 / 087243.Enzymes

[0068] The composition may comprise one or more additional enzymes such as one or more lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and / or peroxidase.

[0069] In general, the properties of the selected 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

[0070] Suitable proteases for the compositions of the invention include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families.

[0071] Examples of subtilases are those derived from Bacillus such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09 / 021867. Subtilisin lentus, Subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 described in (WO93 / 18140). Other useful proteases may be those described in WO01 / 016285 and WO02 / 016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO94 / 25583 and WO05 / 040372, and the chymotrypsin proteases derived from Cellumonas described in WO05 / 052161 and WO05 / 052146.

[0072] A further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO95 / 23221, and variants thereof which are described in WO92 / 21760, WO95 / 23221, EP1921147 and EP1921148.

[0073] Examples of metalloproteases are the neutral metalloprotease as described in WO07 / 044993 (Proctor & Gamble / Genencor Int.) such as those derived from Bacillus amyloliquefaciens.

[0074] Examples of useful proteases are the variants described in: WO89 / 06279, WO92 / 19729, WO96 / 034946, WO98 / 20115, WO98 / 20116, WO99 / 011768, WO01 / 44452, WO03 / 006602, WO04 / 03186, WO04 / 041979, WO07 / 006305, WO11 / 036263, WO11 / 036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101, 102, 104, 116, 118, 121, 126, 127, 128, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211, 212, 216, 218, 226, 229, 230, 239, 246, 255, 256, 268 and 269 wherein the positions correspond to the positions of the Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016 / 001449. More preferred the protease variants may comprise one or more of the mutations selected from the group consisting of: S3T, V4l, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199l, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, N255W, N255D, N255E, L256E, L256D T268A and R269H. The protease variants are preferably variants of the Bacillus lentus protease (Savinase ®< ) shown in SEQ ID NO: 1 of WO 2016 / 001449, the Bacillus amylolichenifaciens protease (BPN') shown in SEQ ID NO: 2 of WO2016 / 001449. The protease variants preferably have at least 80 % sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2 of WO 2016 / 001449.

[0075] A protease variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO: 1 of WO2004 / 067737, wherein the protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO2004 / 067737.

[0076] Suitable commercially available protease enzymes include those sold under the trade names Alcalase ®< , Duralase Tm< , Durazym Tm< , Relase ®< , Relase ®< Ultra, Savinase ®< , Savinase ®< Ultra, Primase ®< , Polarzyme ®< , Kannase ®< , Liquanase ®< , Liquanase ®< Ultra, Ovozyme ®< , Coronase ®< , Coronase ®< Ultra, Blaze ®< , Blaze Evity ®< 100T, Blaze Evity ®< 125T, Blaze Evity ®< 150T, Neutrase ®< , Everlase ®< and Esperase ®< (Novozymes A / S), those sold under the tradename Maxatase ®< , Maxacal ®< , Maxapem ®< , Purafect Ox ®< , Purafect OxP ®< , Puramax ®< , FN2 ®< , FN3 ®< , FN4 ®< , Excellase ®< , Excellenz P1000 ™< , Excellenz P1250 ™< , Eraser ®< , Preferenz P100 ™< , Purafect Prime ®< , Preferenz P110 ™< , Effectenz P1000 ™< , Purafect ®™< , Effectenz P1050 ™< , Purafect Ox ®™< , Effectenz P2000 ™< , Purafast ®< , Properase ®< , Opticlean ®< and Optimase ®< (Danisco / DuPont), Axapem ™< (Gist-Brocases N.V.), BLAP (sequence shown in Figure 29 of US5352604) and variants hereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.Cellulases

[0077] Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757 and WO 89 / 09259.

[0078] Especially suitable cellulases are the alkaline or neutral cellulases having colour care benefits. Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307 and WO99 / 001544.

[0079] Other cellulases are endo-beta-1,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002 / 099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001 / 062903.

[0080] Commercially available cellulases include Celluzyme ™< , and Carezyme ™< (Novozymes A / S) Carezyme Premium ™< (Novozymes A / S), Celluclean ™< (Novozymes A / S), Celluclean Classic ™< (Novozymes A / S), Cellusoft ™< (Novozymes A / S), Whitezyme ™< (Novozymes A / S), Clazinase ™< , and Puradax HA ™< (Genencor International Inc.), and KAC-500(B) ™< (Kao Corporation).Mannanases

[0081] Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999 / 064619. A commercially available mannanase is Mannaway (Novozymes A / S).Peroxidases / Oxidases

[0082] Suitable peroxidases / oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercially available peroxidases include Guardzyme ™< (Novozymes A / S).Lipases and Cutinases

[0083] Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96 / 13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp. strain SD705 (WO95 / 06720 & WO96 / 27002), P. wisconsinensis (WO96 / 12012), GDSL-type Streptomyces lipases (WO10 / 065455), cutinase from Magnaporthe grisea (WO10 / 107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (WO11 / 084412), Geobacillus stearothermophilus lipase (WO11 / 084417), lipase from Bacillus subtilis (WO11 / 084599), and lipase from Streptomyces griseus (WO11 / 150157) and S. pristinaespiralis (WO12 / 137147).

[0084] Other examples are lipase variants such as those described in EP407225, WO92 / 05249, WO94 / 01541, WO94 / 25578, WO95 / 14783, WO95 / 30744, WO95 / 35381, WO95 / 22615, WO96 / 00292, WO97 / 04079, WO97 / 07202, WO00 / 34450, WO00 / 60063, WO01 / 92502, WO07 / 87508 and WO09 / 109500.

[0085] Preferred commercial lipase products include Lipolase ™< , Lipex ™< ; Lipolex ™< and Lipoclean ™< (Novozymes A / S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).

[0086] Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10 / 111143), acyltransferase from Mycobacterium smegmatis (WO05 / 56782), perhydrolases from the CE 7 family (WO09 / 67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10 / 100028).Amylases

[0087] Suitable amylases include alpha-amylases and / or a glucoamylases and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1,296,839.

[0088] Suitable amylases include amylases having SEQ ID NO: 2 in WO 95 / 10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and SEQ ID NO: 4 of WO 99 / 019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

[0089] Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02 / 010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.

[0090] Other amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006 / 066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209 and Q264. Most preferred variants of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 are those having the substitutions: M 197T; H156Y+A181T+N190F+A209V+Q264S; or G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

[0091] Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99 / 019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.

[0092] Additional amylases which can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96 / 023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96 / 023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181, 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.

[0093] Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08 / 153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01 / 66712. Preferred variants of SEQ ID NO: 10 in WO 01 / 66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264.

[0094] Further suitable amylases are amylases having SEQ ID NO: 2 of WO 09 / 061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof. Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and / or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131l, T165l, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and / or deletion in position R180 and / or S181 or of T182 and / or G183. Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions: N128C+K178L+T182G+Y305R+G475K; N128C+K178L+T182G+F202Y+Y305R+D319T+G475K; S125A+N128C+K178L+T182G+Y305R+G475K; or S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K wherein the variants are C-terminally truncated and optionally further comprises a substitution at position 243 and / or a deletion at position 180 and / or position 181.

[0095] Further suitable amylases are amylases having SEQ ID NO: 1 of WO13184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, l203, S241, R458, T459, D460, G476 and G477. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, l203YF, S241QADN, R458N, T459S, D460T, G476K and G477K and / or deletion in position R178 and / or S179 or of T180 and / or G181. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions: E187P+I203Y+G476K E187P+I203Y+R458N+T459S+D460T+G476K wherein the variants optionally further comprise a substitution at position 241 and / or a deletion at position 178 and / or position 179.

[0096] Further suitable amylases are amylases having SEQ ID NO: 1 of WO10104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477 and G478. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21D, D97N, V128l K177L, M200L, L204YF, E242QA, G477K and G478K and / or deletion in position R179 and / or S180 or of I181 and / or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions: N21D+D97N+V128I wherein the variants optionally further comprise a substitution at position 200 and / or a deletion at position 180 and / or position 181.

[0097] Other suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01 / 66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R118K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.

[0098] Other examples are amylase variants such as those described in WO2011 / 098531, WO2013 / 001078 and WO2013 / 001087.

[0099] Commercially available amylases are Duramyl ™< , Termamyl ™< , Fungamyl ™< , Stainzyme ™< , Stainzyme Plus ™< , Natalase ™< , Liquozyme X and BAN ™< (from Novozymes A / S), and Rapidase ™< , Purastar ™< / Effectenz ™< , Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc. / DuPont).Peroxidases / Oxidases

[0100] Suitable peroxidases include those comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity. Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. A suitable peroxidase includes a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis. Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens. A suitable oxidase includes in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5). Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92 / 01046), or Coriolus, e.g., C. hirsutus (JP 2238885). Suitable examples from bacteria include a laccase derivable from a strain of Bacillus. A laccase derived from Coprinopsis or Myceliophthora is preferred; in particular, a laccase derived from Coprinopsis cinerea, as disclosed in WO 97 / 08325; or from Myceliophthora thermophila, as disclosed in WO 95 / 33836.Dispersants

[0101] The composition of the present invention can also contain dispersants. In particular, powdered detergents may comprise dispersants. Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71, Marcel Dekker, Inc.Dye Transfer Inhibiting Agents

[0102] The composition of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.Fluorescent whitening agent

[0103] The composition of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1,2,3-triazol-2-yl)stilbene-2,2'-disulfonate and sodium 5-(2H-naphtho[1,2-d][1,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%.Soil release polymers

[0104] The composition of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71, Marcel Dekker, Inc. Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009 / 087523. Furthermore, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856 and WO 2006 / 113314. Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1-C6 mono-carboxylic acid, Cl-C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1: 1 to 1:5, or from 1: 1.2 to 1:2. The average number of graft sites per ethylene oxide units can be less than 1, or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, or from 0.2 to 0.4. A suitable polyethylene glycol polymer is Sokalan HP22. Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose derivatives such as those described in EP 1867808 or WO 2003 / 040279. Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.Anti-redeposition agents

[0105] The composition of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and / or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.Rheology Modifiers

[0106] The composition of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents. The rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.

[0107] Other suitable cleaning composition components include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and / or structure elasticizing agents.Formulation of cleaning products

[0108] The composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid. A liquid or gel detergent, which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may be non-aqueous.Definitions

[0109] Adjunct ingredients: The term "Adjunct ingredient" means in the present context an additional substance added to a composition and which is normally not an essential part of the composition. In the context of the presence invention an adjunct may also be termed excipient and means the same. In the present context, the terms cleaning ingredient or adjunct and pharmaceutical ingredient or adjunct are used. The person skilled in the art would realize that cleaning adjuncts are adjuncts particularly suitable for cleaning compositions e.g. surfactants, builders etc. and similar for a pharmaceutical ingredient. The term adjunct ingredient includes ingredients suitable for cleaning compositions (also termed cleaning components) and adjunct ingredients suitable for pharmaceutical compositions (also termed excipient). Some ingredients for cleaning and pharmaceutical compositions may be the same.

[0110] Anti-biofouling: Biofouling is the accumulation of organic matter such as microorganisms on surfaces. Anti-biofouling is the ability to reduce, remove or prevent biofouling. Thus, an anti-biofouling composition have the ability to reduce, remove or prevent biofouling.

[0111] Biofilm: The term "Biofilm" means organic matter produced when any group of microorganisms cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS). Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides e.g. PNAG. Biofilms may form on living or non-living surfaces. The microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium. Bacteria living in a biofilm usually have significantly different properties from planktonic bacteria of the same species, as the dense and protected environment of the film allows them to cooperate and interact in various ways. One benefit of this environment for the microorganisms is increased resistance to detergents and antibiotics, as the dense extracellular matrix and the outer layer of cells protect the interior of the community. On surfaces biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus sp., Pseudomonas sp., Staphylococcus sp., Enterococcus sp. Streptococcus sp. and Stenotrophomonas sp. On hard surfaces biofilm producing bacteria may be found among the following species: Staphylococcus e.g. Staphylococcus aureus or Staphylococcus epidermidis, Pseudomonas e.g. Pseudomonas aeruginosa, Enterococcus e.g. Enterococcus faecalis, Streptococcus e.g. Streptococcus pneumoniae, Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus and Stenotrophomonas sp.

[0112] Cleaning adjunct ingredient: The detergent adjunct ingredient (or cleaning component) is different to the hexosaminidase. The precise nature of these additional adjunct components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used. Suitable adjunct materials include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal / anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric huing agents, anti-foaming agents, dispersants, processing aids, and / or pigments.

[0113] Cleaning Composition: The term "cleaning composition" refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles. The cleaning composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning. The terms encompass any materials / compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and / or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters / pretreatment). In addition to containing the enzyme of the invention, the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases and mannanases, or any mixture thereof), and / or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

[0114] The term "hard surface cleaning" is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash). Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.

[0115] The term "wash performance" is used as an enzyme's ability to remove stains present on the object to be cleaned during e.g. wash or hard surface cleaning.

[0116] By the term "medical device" is meant any medical device suitable for cleaning, reprocessing and reuse, such as, but not limited to an endoscope, encephaloscope, laryngoscope, esophagoscope, thoracoscope, nasopharyngoscope, angioscope, nephroscope, colonoscope, proctoscope, arthroscope, rhinoscope, esophagoscope, bronchoscope, pancreatoscope, mediastinoscope, gastroscope, laparoscope, amnioscope, cystoscope, a hysteroscope, choledochoscope or accessories for any of the scopes listed. The medical device may be selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, or wherein the device is a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument.

[0117] By the term "pharmaceutical adjunct ingredient" means any pharmaceutical excipient suitable for formulating the pharmaceutical compound. Such excipients, carriers, vehicles etc. are well known to those of skill in the art and are described in text books such as Remington's Pharmaceutical Sciences, Mack Publishing Co., Easton, Pa., 1985. Pharmaceutically acceptable excipients which are suitable for use in tablet formulations include, for example, inert diluents, such as calcium carbonate, sodium carbonate, lactose, calcium phosphate or sodium phosphate; granulating and disintegrating agents, for example, corn starch, or alginic acid; binding agents, for example starch, gelatin or acacia, and lubricating agents, for example magnesium stearate, stearic acid or talc. Tablets may be uncoated or they may be coated by known techniques to delay disintegration and absorption in the gastrointestinal tract and thereby provide a sustained action over a longer period. For example, a time delay material such as glyceryl monostearate or glyceryl distearate may be employed. For hard gelatin capsule formulations, the active ingredient can be mixed with an inert solid diluent, for example, calcium carbonate, calcium phosphate or kaolin. For soft gelatin capsule formulations the active ingredient can be mixed with water or an oil medium, for example peanut oil, liquid paraffin or olive oil. Excipients suitable for the manufacture of aqueous suspensions include suspending agents, for example sodium carboxymethylcellulose, methylcellulose, hydropropyl methylcellulose, sodium alginate, polyvinylpyrrolidone, gum tragacanth and gum acacia; dispersing or wetting agents may be a naturally- occurring phosphatide, for example, lecithin, or condensation products of an alkylene oxide with fatty acids, for example polyoxyethylene stearate, or condensation products of ethylene oxide with long chain aliphatic alcohols, for example heptadecaethyleneoxycetanol, or condensation products of ethylene oxide with partial esters obtained from fatty acids and a hexitol such as polyoxyethylene sorbitol monooleate, or condensation products of ethylene oxide with partial esters obtained from fatty acids and hexitol anhydrides, for example polyethylene sorbitan monooleate. Aqueous suspensions may also contain one or more preservatives, for example benzoates, such as ethyl, or n-propyl p-hydroxybenzoate, one or more colouring agents, one or more flavouring agents, and one or more sweetening agents, such as sucrose or saccharin. Oily suspensions may be formulated by suspending the active ingredients in a vegetable oil, for example arachis oil, olive oil, sesame oil or coconut oil, or in a mineral oil such as liquid paraffin. The oily suspensions may contain a thickening agent, for example beeswax, hard paraffin or cetyl alcohol. Sweetening agents and flavouring agents may be added. These compositions may be preserved by the addition of an antioxidant such as ascorbic acid.

[0118] Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity". For purposes of the present invention, the 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 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: Identical Residues × 100 / Length of Alignment − Total Number of Gaps in Alignment .Examples Assays Assay I: testing of hexosaminidase activity

[0119] The hexosaminidase activity of the polypeptides listed in the table below was determined using 4-nitrophenyl N-acetyl-β-D-glucosaminide (Sigma-Aldrich) as substrate. The enzymatic reaction was performed in triplicates in a 96 well flat bottom polystyrene microtiter plate (Thermo Scientific) with the following conditions: 50 mM 2-(N-morpholino)ethanesulfonic acid pH 6 buffer, 1.5 mg / ml 4-nitrophenyl N-acetyl-β-D-glucosaminide and 20 µg / ml purified enzyme sample in a total reaction volume of 100 µl. Blank samples without polypeptide were run in parallel. The reactions were carried out at 37°C in a Thermomixer comfort (Eppendorf). After 10 minutes of incubation, 5 µl 1 M NaOH was added to each reaction mixture to stop the enzymatic reaction. The absorbance was read at 405 nm using a POLARstar Omega plate reader (BMG LABTECH) to estimate the formation of 4-nitrophenolate ion released because of enzymatic hydrolysis of the 4-nitrophenyl N-acetyl-β-D-glucosaminide substrate.Composition of model detergent A (liquid)

[0120] Ingredients: 12% LAS, 11% AEO Biosoft N25-7 (NI), 5% AEOS (SLES), 6% MPG (monopropylene glycol), 3% ethanol, 3% TEA, 2.75% coco soap, 2.75% soya soap, 2% glycerol, 2% sodium hydroxide, 2% sodium citrate, 1% sodium formate, 0.2% DTMPA and 0.2% PCA (all percentages are w / w).Composition of model detergent B (liquid)

[0121] Ingredients: 7,2% LAS, 6,6% AEO Biosoft N25-7 (NI), 4,2% AEOS (SLES), 6% MPG (monopropylene glycol), 3% ethanol, 3% TEA, 2.75% coco soap, 2.75% soya soap, 2% glycerol, 1,2% sodium hydroxide, 2% sodium citrate, 1% sodium formate, 0.2% DTMPA and 0.2% PCA (all percentages are w / w).Composition of Model Detergent MC

[0122] A medical cleaning model detergent (model detergent MC) was prepared containing 5% MPG (propylene glycol), 5% Pluronic PE 4300 (PO / EO block polymer; 70% / 30%, approx. 1750 g / mol), 2% Plurafac LF 305 (fatty alcohol alkoxylate; C6-10 + EO / PO), 1% MGDA (methyl glycine diacetic acid, 1% TEA (triethanolamine) (all percentages are w / w). The pH was adjusted to 8.7 with phosphoric acid.Example 1 Biofilm reduction in liquid model detergent

[0123] Staphylococcus aureus 15981 (kind gift from lñigo Lasa (Valle et al., Mol Microbiol.2003 May; 48 (4):1075-87) was used as a model microorganism in the present example. S.aureus was restreaked on Tryptone Soya Agar (TSA) (pH 7.3) (CM0131; Oxoid Ltd, Basingstoke, UK) and incubated at 37°C overnight. A single colony was inoculated into 15 mL of TSB and the culture was incubated 5 hours at 37°C under shaking conditions. The culture was subsequently diluted (1:100) in fresh TSB + 1% glucose (24563; Roquette Freres) and the bacterial suspension was added to 96-well microtiter plates (100 µL aliquots, Thermo Scientific, Nunclon Delta Surface, cat # 167008). The plates were incubated for 24 hours at 37°C under static conditions. After incubation, the biofilm plates were rinsed (100 µL of 0.9% sodium chloride), and the biofilms were treated with model cleaning solution (100 µL, 3.3 g / L Model detergent A or model detergent B in 15°dH water hardness) containing 0 µg / mL (control) or 20 µg / mL enzyme. The hexosaminidase with SEQ ID NO: 17 was used as benchmark. The plates were then incubated at 37°C for 1 hour, rinsed with water hardness and stained with 0.095% crystal violet (SIGMA V5265) for 15 min. Following the staining, the wells were rinsed and the dye was dissolved with 95% ethanol and the absorbance measured at 595nm. The results are displayed in table 1, 2 and 3 and 4, as percentages of remaining biofilm after enzymatic treatment compared the benchmark treatment (Absorbance(enzyme) / Absorbance(benchmark)* 100%). As clearly seen, the polypeptides display superior biofilm removal as compared to the benchmark, under the tested conditions. Table 1 Biofilm removal in model A detergent compared with the benchmark treatmentEnzyme% remaining biofilm (relative to benchmark treatment)SEQ ID NO: 18*23.4SEQ ID NO: 11*39.4SEQ ID NO: 12*13.8SEQ ID NO: 13*11.5SEQ ID NO: 14*10.0SEQ ID NO: 15*13.5SEQ ID NO: 16*84.3SEQ ID NO: 19.6SEQ ID NO: 6*23.5SEQ ID NO: 29.3* Not encompassed by the wording of the claims Table 2 Biofilm removal in model A detergent compared with the benchmark treatment Enzyme% remaining biofilm (relative to benchmark treatment)SEQ ID NO: 7*17.1SEQ ID NO: 416.1SEQ ID NO: 9*14.8SEQ ID NO: 8*12.6SEQ ID NO: 524.6SEQ ID NO: 10*26.8 * Not encompassed by the wording of the claims Table 3 Biofilm removal in model detergent B compared with the benchmark treatment Enzyme% remaining biofilm (relative to benchmark treatment)SEQ ID NO: 36.8 Example 2 Endoscope cleaning in liquid model detergent

[0124] Endoscope biofilms were established using S.aureus (Valle et al., Mol Microbiol.2003 May; 48 (4):1075-87) as follows: The strain was inoculated into 10 mL of TSB and incubated for 6 hours at 37°C with shaking (200 rpm). After propagation, the culture was diluted (1:100) in fresh TSB + 1% glucose (24563; Roquette Freres) and 2 mL aliquots were added to the wells of 24-well polystyrene flat-bottom microplates (144530; Thermo Fisher Scientific) containing sterile pieces (1cm) of endoscope tubing (4.7mm diameter, Fluoroelastomer / Viton ®< , USP Class VI, Endoscopy Development Company, LLC). Sterile medium was added to control wells. After 24h at 37°C (static incubation), the endoscope pieces were rinsed with water (6 0< dH), and treated with 2ml of a model cleaning solution (3.3 g / L Model detergent A in 6°dH water) containing no enzyme or 10 µg / mL enzyme for 1 hour at 37°C under static conditions. The endoscope pieces were then rinsed with 6 0< dH water and stained with 0.095% crystal violet (SIGMA V5265) for 15 min. Following staining, the endoscope pieces were rinsed twice, blotted on absorbent paper and the remaining dye was dissolved using 95% ethanol. 200 µl aliquots of the suspensions were moved to a 96-well microtiter plate and the absorbance was measured at 595nm. The results are displayed in table 4 as percentage of remaining biofilm after enzymatic treatment as compared to the control (endoscope biofilm treated without enzyme). The experiment was repeated three times. Table 4. Endoscope cleaning properties in model detergent AEnzymeEnzyme dosage (µg / ml)Remaining biofilm (% of untreated control)No enzyme0100.0SEQ ID NO: 31021.2SEQ ID NO: 4105.7

[0125] The results show that the polypeptides of the invention have endoscope cleaning properties i.e. disrupt and / or remove the biofilm or components of the biofilm tested when compared to samples comprising no enzyme.Example 3 Cleaning in medical cleaning model detergent

[0126] S.aureus 15981 was used as a model microorganism in the present example. The strain was inoculated into 10 mL of TSB+1% glucose (24563; Roquette Freres) and incubated for 16 hours at 37°C, 200rpm. After propagation, the culture was diluted (1:100) in fresh TSB + 1% glucose and 500 µL aliquots were added to the wells of 48-well polystyrene flat-bottom microplates (150787; Thermo Fisher Scientific). Sterile medium was added to control wells. After 16h at 37°C (static incubation), the microplates were rinsed with water hardness (5 0< dH), and treated with a model medical cleaning solution (0.5 g / L Model detergent MC in 5°dH water hardness) containing no enzyme or 2 µg / mL enzyme for 1 hour at 37°C under static conditions. The microplates were then rinsed with 5 0< dH water and stained with 0.095% crystal violet (SIGMA V5265) for 15 min. Following staining, the plates pieces were rinsed twice, and the remaining dye was dissolved (using 1vol:1vol 95% ethanol:30% Acetic acid). 200 µl aliquots of the suspensions were moved to 96-well microtiter plates and the absorbance was measured at 595nm. The results are displayed in table 5 as percentages of remaining biofilm after enzymatic treatment as compared to the control (biofilm treated without enzyme). The experiment was repeated three times. Table 5. Cleaning properties in medical cleaning model detergentEnzyme Enzyme dosage (µg / ml) Remaining biofilm (% of untreated control) SEQ ID NO: 322.0SEQ ID NO: 423.1SEQ ID NO: 19*22.5SEQ ID NO: 21*23.8SEQ ID NO: 23*22.2SEQ ID NO: 24*22.0SEQ ID NO: 22*21.9* Not encompassed by the wording of the claims

[0127] The results show that the polypeptides of the invention have cleaning properties in a medical cleaning relevant detergent i.e. disrupt and / or remove the biofilm or components of the biofilm tested when compared to samples treated with the cleaning solution comprising no enzyme.

Claims

1. A method of cleaning a medical device, wherein the method comprises a) contacting the medical device with a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity, for a period effective to clean the medical device; b) cleaning the medical device; and optionally c) disinfecting the medical device wherein the hexosaminidase is a polypeptide having at least 80% sequence identity to the amino acid sequence shown in SEQ ID NO: 4, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 5.

2. The method according to claim 1, wherein the polypeptide has at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 4, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 5.

3. The method according to claim 2, wherein the composition comprises at least one adjunct ingredient selected from the group consisting of surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

4. The method according to any of the preceding claims, wherein the composition is an anti-biofouling composition.

5. The method according to claim 4, wherein the composition comprises a fungicide or biocide, preferably a biocidal quaternary ammonium biocide.

6. The method according to any of the preceding claims, wherein the composition is a cleaning or pharmaceutical composition.

7. The method according to any of the preceding claims, wherein the composition is a cleaning composition and wherein the adjunct ingredient is at least one cleaning component optionally selected from surfactants, builders, bleach components, polymers and dispersing agents.

8. The method according to claim 7, wherein the composition comprises; a) at least 0.01 mg / mL hexosaminidase having beta-N-acetylglucosaminidase activity; and b) at least one cleaning component, preferably selected from surfactants, builders, bleach components, polymers and dispersing agents.

9. The method according to claim 8 wherein the composition comprises at least one anionic surfactant selected from linear alkylbenzenesulfonates (LAS), alpha-olefinsulfonates (AOS) or alcohol ethersulfates (AES or AEOS or FES, alcohol ethoxysulfates and fatty alcohol ether sulfates).

10. The method according to any of the preceding claims wherein the medical device is selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, or wherein the device is an endoscope, a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument.

11. The method according to any of the preceding claims wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 4, or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity hereto.

12. The method according to any of claims 1-10, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 1, or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity hereto.

13. The method according to any of claims 1-10, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 2, or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity hereto.

14. The method according to any of claims 1-10, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 3, or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity hereto.

15. The method according to any of claims 1-10, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is a polypeptide comprising the amino acid sequence shown in SEQ ID NO: 5, or a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity hereto.

16. The use of a composition comprising a hexosaminidase having beta-N-acetylglucosaminidase activity and at least one adjunct ingredient for cleaning of a medical device, wherein the hexosaminidase having beta-N-acetylglucosaminidase activity is selected from the group of polypeptides having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 4, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 5.

17. The use according to claim 16, wherein the adjunct ingredient is selected from the group consisting of surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

18. The use according to claim 16 or 17, wherein the medical device is selected from the group consisting of a catheter such as a central venous catheter, intravascular catheter, urinary catheter, Hickman catheter, peritoneal dialysis catheter, endrotracheal catheter, or wherein the device is an endoscope, a mechanical heart valve, a cardiac pacemaker, an arteriovenous shunt, a scleral buckle, a prosthetic joint, a tympanostomy tube, a tracheostomy tube, a voice prosthetic, a penile prosthetic, an artificial urinary sphincter, a synthetic pubovaginal sling, a surgical suture, a bone anchor, a bone screw, an intraocular lens, a contact lens, an intrauterine device, an aortofemoral graft, a vascular graft, a needle, a Luer-Lok connector, a needleless connector and a surgical instrument.