WO1997002753A1 - Nettoyage en place a l'aide d'une solution contenant une protease et une lipase - Google Patents

Nettoyage en place a l'aide d'une solution contenant une protease et une lipase Download PDF

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Publication number
WO1997002753A1
WO1997002753A1 PCT/DK1996/000301 DK9600301W WO9702753A1 WO 1997002753 A1 WO1997002753 A1 WO 1997002753A1 DK 9600301 W DK9600301 W DK 9600301W WO 9702753 A1 WO9702753 A1 WO 9702753A1
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WO
WIPO (PCT)
Prior art keywords
protease
cleaning
solution
lipase
process equipment
Prior art date
Application number
PCT/DK1996/000301
Other languages
English (en)
Inventor
Hans Sejr Olsen
Original Assignee
Novo Nordisk A/S
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Novo Nordisk A/S filed Critical Novo Nordisk A/S
Priority to AU65129/96A priority Critical patent/AU695776B2/en
Priority to EP96924788A priority patent/EP0840553A2/fr
Publication of WO1997002753A1 publication Critical patent/WO1997002753A1/fr
Priority to US09/003,768 priority patent/US6071356A/en

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Classifications

    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B08—CLEANING
    • B08B—CLEANING IN GENERAL; PREVENTION OF FOULING IN GENERAL
    • B08B9/00—Cleaning hollow articles by methods or apparatus specially adapted thereto 
    • B08B9/02—Cleaning pipes or tubes or systems of pipes or tubes
    • B08B9/027—Cleaning the internal surfaces; Removal of blockages
    • B08B9/032—Cleaning the internal surfaces; Removal of blockages by the mechanical action of a moving fluid, e.g. by flushing
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C7/00—Other dairy technology
    • A23C7/02—Chemical cleaning of dairy apparatus; Use of sterilisation methods therefor
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01D—SEPARATION
    • B01D65/00—Accessories or auxiliary operations, in general, for separation processes or apparatus using semi-permeable membranes
    • B01D65/02—Membrane cleaning or sterilisation ; Membrane regeneration
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B08—CLEANING
    • B08B—CLEANING IN GENERAL; PREVENTION OF FOULING IN GENERAL
    • B08B9/00—Cleaning hollow articles by methods or apparatus specially adapted thereto 
    • B08B9/02—Cleaning pipes or tubes or systems of pipes or tubes
    • B08B9/027—Cleaning the internal surfaces; Removal of blockages
    • B08B9/032—Cleaning the internal surfaces; Removal of blockages by the mechanical action of a moving fluid, e.g. by flushing
    • B08B9/0321—Cleaning the internal surfaces; Removal of blockages by the mechanical action of a moving fluid, e.g. by flushing using pressurised, pulsating or purging fluid
    • B08B9/0323—Arrangements specially designed for simultaneous and parallel cleaning of a plurality of conduits
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B08—CLEANING
    • B08B—CLEANING IN GENERAL; PREVENTION OF FOULING IN GENERAL
    • B08B9/00—Cleaning hollow articles by methods or apparatus specially adapted thereto 
    • B08B9/08—Cleaning containers, e.g. tanks
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
    • C12Y301/01003—Triacylglycerol lipase (3.1.1.3)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
    • C12Y301/01004—Phospholipase A2 (3.1.1.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01001—Alpha-amylase (3.2.1.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21004—Trypsin (3.4.21.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21014—Microbial serine proteases (3.4.21.14)
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01D—SEPARATION
    • B01D2321/00—Details relating to membrane cleaning, regeneration, sterilization or to the prevention of fouling
    • B01D2321/16—Use of chemical agents
    • B01D2321/166—Use of enzymatic agents
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/14—Hard surfaces
    • C11D2111/20—Industrial or commercial equipment, e.g. reactors, tubes or engines

Definitions

  • This invention relates to an enzymatic method of cleaning-in-place soiled process equipment, in particular dairy and slaughter house process equipment.
  • Cleaning-in-place which has replaced hand cleaning in, e.g., dairies, breweries and all potable liquid installations, involves circulating non-foaming or low foaming 15 detergents through process equipment in the assembled state.
  • a typical basic CIP sequence may consist of the following five stages (for reference see “Hygiene for Manage ⁇ ment” by Richard A. Sprenger, 5th Ed., p. 135, published by Highfield Publications) : 20 (1) pre-rinse with cold water to remove gross soil;
  • the time allowed for each operation must be 30 determined for each particular plant or circuit being cleaned.
  • the detergent in step (2) in the above mentioned sequence is often 0.5-1% NaOH/KOH (+/- surfactants) at 75-85°C followed by a rinsing with water followed by a treatment with
  • the surfactants used are typically selected from nonionic and/or anionic surfactants often in combination with sequestering agents.
  • a new cleaning media should offer one or more of the following advantages : Reduction of the water consumption, less damage to the equipment, lower temperatures, less risk for residues of surfactants and/or caustic and/or acids and/or sequestering agents in the food or beverage, less risk for accidents to the people handling the cleaning media. For membrane cleaning media also an improved cleaning efficacy is wanted.
  • a solution comprising a protease and a lipase is very efficient in cleaning, e.g., process equipment containing residues of milk or burnt milk.
  • the present invention relates to a method of cleaning-in-place soiled process equipment compris ⁇ ing circulating a solution comprising a protease and a lipase for a sufficient period of time to permit action of the enzymes.
  • the method of the present invention may be applied to cleaning-in-place of any process equipment known in industry.
  • the method is particularly well suited for cleaning process equipment that prior to cleaning has contained materials containing proteins, fats or carbohydrates, in particular materials that prior to cleaning has contained fats and proteins such as milk, whey, cheese, cream, butter, milk based desserts, fermented milk products such as yoghurt, ymer, Gaio, meat, meat emulsions, sausages, whole meat cuts, feed products, liquid feed products, soy milk, tofu, fermented oriental fat-containing foods, extruded foods such as spaghetti and egg products, mayonnaise, sauces such as bearnaise sauce, fish, fish emulsions, fish sausages and whole fish cuts.
  • the mechanism of the enzymatic cleaning of the hard surfaces of the process equipment is believed to be the following: During enzymatic degradation of the soils (protein, fat, carbohydrates) a solubilization occur. Using a protease, the sections formed by the degradation of the protein become soluble. Using a lipase, the degraded fat becomes soluble at alkaline conditions. Using a carbohydrase, degraded polysac- charides becomes soluble or the viscosity may be reduced significantly which help on the mechanical action needed for effective cleaning and rinsing.
  • Proteins are degraded to emulsifying or foaming products. When degraded by use of efficient serine proteases the amphophilic properties of the peptides formed secure a high foam or emulsification effect. The peptides so formed also have a significant buffer capacity, and generally stabilize enzymes in solution.
  • Fats degraded by use of a lipase under alkaline conditions form soaps or other amphipatic compounds.
  • the time for cleaning may be reduced. • The energy consumption may be reduced. (The enzymatic cleaning is performed at a lower temperature) .
  • the waste water treatment may be cheaper. • The waste water may be used for feed or (food) .
  • the waste water may also be used for other purposes like emulsifiers, buffers or cleaning agents for reuse or use in other places, such as lubrication purposes or polymer production.
  • the method of the invention could therefore be very important in e.g. cleaning milking machines because it is a problem today to keep the inner surfaces of the milking machines free of microorganisms.
  • the method of the invention works very well without any detergents being added. It may, however, in some cases be an advantage also to add a small amount of a surfactant, preferably a non-ionic surfactant, in an amount of up to 1% w/w, preferably in an amount of up to 0.1% w/w, more preferably in an amount of up to 0.025% w/w.
  • a surfactant preferably a non-ionic surfactant
  • a surfactant it will normally be selected from the nonionic group or from the amphoterics.
  • One or more of the following nonionic surfactants may be applied: - glycerol derivatives,
  • amphoterics one or more of following may be applied:
  • any process equipment known in the art may be cleaned as described herein.
  • all process equipment used in the food/feed industry may advantageously be cleaned as described in the present invention.
  • process equipment used for waste treatment e.g., oil/water separators, tanks, pipes, and membrane separation equipment on, e.g., shipboard installations, in particular process equipment for the treatment of the so called “Gray water”, may be cleaned as described in the present invention.
  • Dairy, slaughter house, brewery, feed, feed pelleting, fish and fish meal process equipment is particularly well suited.
  • the milk forms gels on the inner surfaces (the surfaces that are in contact with the milk) of, e.g., heat exchangers, tanks, pipes, centrifuges, evaporators and filters.
  • coagulated milk, melted and congealed cheese and milkstone, in particular all cheese manufacturing process equipment may be problematic to clean. All these items may be effectively cleaned by the method of the present invention.
  • meat choppers and other equipment used in meat processing are difficult to clean.
  • heat exchangers, cooking jars, coolers, storage tanks, pipes, centrifuges, evaporators, filters, sieves and hydrocyclones may be effec- tively cleaned by the method of the present invention.
  • the amount of chemicals may be reduced, the amount of rinsing water may be reduced, and the chance for residual amounts of surfactants in the milk is reduced.
  • Membrane processes are widely used in many industries today. Reverse osmosis covering ultrafiltration, nanofiltration, hyperfiltration and microfiltration are techniques used in the dairy industry and in the fermentation industry (for production of products such as enzymes and pharmaceutical products) .
  • the spiral wounded membrane types are in general not as alkali resistant as the plate and frame systems (dependent on the polymer type in question) .
  • Enzymes According to the invention a cleaning solution containing a protease and a lipase is preferred, but depending on the soil in question the solution may also contain other enzymes such as carbohydrases.
  • the amount of enzymes used in the solution varies according to the type of enzyme and the soil in question.
  • the amount of each enzyme will typically be 0.00001-0.1% calculated as pure enzyme protein, preferably 0.001-0.01% calculated as pure enzyme protein.
  • proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically or genetically modified mutants are included.
  • the protease may be a serine protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) .
  • trypsin-like proteases examples include trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270.
  • protease enzymes examples include AlcalaseTM, SavinaseTM' EsperaseTM and DurazymTM products of Novo Nordisk A/S; MaxacalTM, MaxapemTM, PurafectTM, and Purafect OXPTM products of Genencor International, and OpticleanTM and OptimaseTM by Solvay Enzymes.
  • Suitable lipases include those of bacterial and fungal origin. Chemically or genetically modified mutants are included.
  • useful lipases include a Humicola lanuginosa lipase, e.g., as described in EP 258 068 and EP 305 216, a Rhizomucor miehei lipase, e.g., as described in EP 238 023, a Candida lipase, such as a C. antarctica lipase, e.g., the C. antarctica lipase A or B described in EP 214 761, a Pseudomonas lipase such as a P. alcaligenes and P. pseudoalcaligenes lipase, e.g., as described in EP 218 272, a P.
  • a Humicola lanuginosa lipase e.g., as described in EP 258 068 and EP 305 216
  • a Rhizomucor miehei lipase e.g., as described in EP 238 023
  • cepacia lipase e.g., as described in EP 331 376, a Bacillus lipase, e.g., a B . subtilis lipase (Dartois et al. , (1993), Biochemica et Biophysica acta 1131, 253-260), a B . stearothermophilus lipase (JP 64/744992) and a B . pumilus lipase (WO 91/16422) .
  • a number of cloned lipases may be useful, including the Penicillium camembertii lipase described by Yamaguchi et al. , (1991), Gene 103, 61-67), the Geotricum candidum lipase (Schimada, Y. et al. , (1989), J. Biochem., 106, 383-388), and various Rhizopus lipases such as a R . delemar lipase (Hass, M.J et al. , (1991), Gene 109, 117-113), a JR. niveus lipase (Kugimiya et al. , (1992), Biosci. Biotech. Biochem. 56, 716-719) and a R . oryzae lipase.
  • Rhizopus lipases such as a R . delemar lipase (Hass, M.J et al. , (1991), Gene
  • lipases examples include LipolaseTM, Lipolase UltraTM, LipomaxTM and LumafastTM.
  • cutinases may also be useful, e.g., a cutinase derived from Pseudomonas mendocina as described in WO 88/09367, or a cutinase derived from Fusarium solani pisi (e.g. described in WO 90/09446) .
  • a phospholipase may also be used; phospholipases may be obtained from porcine or bovine pancreas or from snake or bee venom, or they may be obtained from a microorganism. Examples of commercial phospholipases are LecitaseTM available from Novo Nordisk A/S and Streptomyces chromofuscus phospholipase available from Toya Jozo Co., Ltd.
  • Carbohydrases Depending on the polysaccharides in question to be removed one or more carbohydrases such as amylases or cellulases may be used.
  • Amylase Any amylase suitable for use in alkaline solutions can be used. Suitable amylases include those of bacterial and fungal origin. Chemically or genetically modified mutants are included. Amylases include, for example, ⁇ -amylases obtained from a special strain of B . licheniformis , described in more detail in British Patent Specification No. 1,296,839. Particularly preferred are TermamylTM and DuramylTM, available from Novo Nordisk A/S. Cellulase: Any cellulase suitable for use in alkaline solutions can be used. Suitable cellulases include those of bacterial and fungal origin. Chemically or genetically modified mutants are included. Suitable cellulases are disclosed in US 4,435,307. Particularly preferred is CelluzymeTM produced by a strain of Humicola insolens, available from Novo Nordisk A/S.
  • the method of the invention is particularly well suited for cleaning process equipment that prior to cleaning is soiled with a material containing proteins, fats or carbohydrates, in particular process equipment that prior to cleaning is soiled with a material containing fats and pro- teins.
  • the solution containing the enzymes is circulated through the process equipment as known in the art.
  • the solution may contain no surfactants other than those produced from fats and proteins either in situ and/or from an earlier cleaning, or it may contain a small amount of a surfactant as described above.
  • the time needed for effective cleaning depends on many factors such as the process unit to be cleaned, the kind of soil, the thickness and hardness of that soil, and the temperature and pH of the solution containing the enzymes.
  • a sufficient period of time will normally be from 10 minutes to 10 hours, preferably from 30 minutes to 3 hours;
  • a sufficient temperature of the solution will typically be in the range of from 10°C to 90°C, preferably in the range of from 20°C to 80°C, more preferably in the range of from 40°C to 80°C, a typical temperature will be around 50°C;
  • the pH of the solution will typically be above 7, preferably be in the range of from pH 8 to pH 10.
  • a typical CIP-sequence according to the invention may consist of the following steps: I: Rinse with water - Enzymatic treatment - Rinse with water. II: Rinse with water - Enzymatic treatment - Rinse with water - Acid treatment - Rinse with water.
  • the pH-value is kept above 7, preferably above 8.
  • Buffers with high capacity and/or in high concentrations e.g. > 0.1 M
  • Esperase 8.0 L available from Novo Nordisk A/S
  • Lipolase 100 L available from Novo Nordisk A/S
  • the aim of cleaning milking machines was that the hydrolytic effect of the enzymes (protease + lipase) should match that of alkali (NaOH) .
  • Cone of Cone, of m eqv. 15 Esperase 8.0 L Lipolase 100 L NaOH/g of dry (% w/w) (% w/w) matter
  • the viscosity was measured on diluted solutions (0.4% and 0.8%) of unhomogenized milk by use of a Hoebbler viscosimeter at 25°C.
  • the milk was tested alone, after addition of 0.025% Esperase 8.0 L + 0.025% Lipolase 100 L, and 0 after addition of 2.5 g NaOH/1.
  • the results are presented below:
  • the nominal water flux was according to the data sheet: 250-350 l/m2/h at 20°C, 4 Bar. This is recalculated to 17°C and 3.1 Bar (Avg) corresponding to 175-250 l/m 2 /h.
  • the membranes were soiled by ultrafiltration of 2 litre 5 whole milk at 50°C for 120 minutes to approximately 25% dry matter (refraktometer) using an inlet pressure of 3.2 Bar and an outlet pressure of 3.0 Bar.
  • the flow through the pump was 3.5-4 litre per minutes.
  • the recirculation vessel was rinsed with water at 50 C. When it was clean the water was flowed through the module at no back pressure. This secures maximal flow through the module. This rinsing was carried out for 5 minutes. Hereafter the flux and the temperature were measured.
  • Recirculation was initiated. Also the permeate was recirculated to the vessel. Recirculation was carried out for 60 minutes at 50 ° C by low pressure (means maximal flow) . The flux and temperature were measured for control purposes during the cleaning operation.

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Wood Science & Technology (AREA)
  • General Health & Medical Sciences (AREA)
  • Zoology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biochemistry (AREA)
  • Genetics & Genomics (AREA)
  • Health & Medical Sciences (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Mechanical Engineering (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Food Science & Technology (AREA)
  • Polymers & Plastics (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

Procédé de nettoyage en place d'équipement de transformation souillé qui consiste à faire circuler une solution comprenant une protéase et une lipase pendant un laps de temps suffisant pour permettre l'action des enzymes.
PCT/DK1996/000301 1995-07-12 1996-07-03 Nettoyage en place a l'aide d'une solution contenant une protease et une lipase WO1997002753A1 (fr)

Priority Applications (3)

Application Number Priority Date Filing Date Title
AU65129/96A AU695776B2 (en) 1995-07-12 1996-07-03 Cleaning-in-place with a solution containing a protease and a lipase
EP96924788A EP0840553A2 (fr) 1995-07-12 1996-07-03 Nettoyage en place a l'aide d'une solution contenant une protease et une lipase
US09/003,768 US6071356A (en) 1995-07-12 1998-01-07 Cleaning-in-place with a solution containing a protease and a lipase

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
DK0819/95 1995-07-12
DK81995 1995-07-12
DK1221/95 1995-11-02
DK122195 1995-11-02

Related Child Applications (1)

Application Number Title Priority Date Filing Date
US09/003,768 Continuation US6071356A (en) 1995-07-12 1998-01-07 Cleaning-in-place with a solution containing a protease and a lipase

Publications (1)

Publication Number Publication Date
WO1997002753A1 true WO1997002753A1 (fr) 1997-01-30

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Country Status (4)

Country Link
EP (1) EP0840553A2 (fr)
AR (1) AR002835A1 (fr)
AU (1) AU695776B2 (fr)
WO (1) WO1997002753A1 (fr)

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WO2000011962A1 (fr) * 1998-08-27 2000-03-09 Henkel Ecolab Gmbh & Co. Ohg Procede de nettoyage de chauffe-lait
WO2002047484A1 (fr) * 2000-12-15 2002-06-20 Laboratoires Anios Composition pour le traitement d'objets destines a etre desinfectes
WO2002050233A1 (fr) * 2000-12-21 2002-06-27 Ecolab Inc. Utilisation de produits a base d'acide percarboxylique, contenant des tensio-actifs et moussant peu pour la desinfection en circuit ferme
WO2002081755A1 (fr) * 2001-04-04 2002-10-17 West Agro, Inc. Procede de nettoyage de la tuyauterie d'une laiterie par pre-traitement enzymatique
US6624132B1 (en) 2000-06-29 2003-09-23 Ecolab Inc. Stable liquid enzyme compositions with enhanced activity
US7795199B2 (en) 2000-06-29 2010-09-14 Ecolab Inc. Stable antimicrobial compositions including spore, bacteria, fungi, and/or enzyme
US20100233333A1 (en) * 2007-09-04 2010-09-16 Elizabeth Varriano-Marston Method for controlling banana and plantain quality by packaging
WO2010125315A1 (fr) * 2009-04-30 2010-11-04 Roquette Freres Procede de purification de polymeres de glucose destines aux solutions de dialyse peritoneale
WO2011003968A1 (fr) 2009-07-08 2011-01-13 Ab Enzymes Oy Protéase fongique et son utilisation
US8232088B2 (en) 2008-09-05 2012-07-31 TransAlgae Ltd Genetically engineered herbicide resistance for maintaining axenic cultures
WO2013120515A1 (fr) 2012-02-15 2013-08-22 Ecolab Usa Inc Procédé d'inactivation enzymatique
US8603795B2 (en) 2009-04-30 2013-12-10 Ab Enzymes Oy Fungal protease and use thereof
US8609390B2 (en) 2009-04-30 2013-12-17 Ab Enzymes Oy Fungal serine protease and use thereof
US8906839B2 (en) 1997-01-13 2014-12-09 Ecolab Usa Inc. Alkaline detergent containing mixing organic and inorganic sequestrants resulting in improved soil removal
US8945900B2 (en) 2010-10-29 2015-02-03 Ab Enzymes Oy Variants of fungal serine protease
CN105169953A (zh) * 2015-09-29 2015-12-23 唐山沃德环保技术有限公司 用于清洗反渗透膜微生物污染的酶质清洗剂及其使用方法
WO2016046334A1 (fr) * 2014-09-25 2016-03-31 Novozymes A/S Utilisation d'enzyme pour le nettoyage
WO2016096996A1 (fr) 2014-12-16 2016-06-23 Novozymes A/S Polypeptides ayant une activité n-acétylglucosamine oxydase
US9404164B2 (en) 2011-03-31 2016-08-02 Ab Enzymes Oy Protease enzyme and uses thereof
WO2017066510A1 (fr) 2015-10-14 2017-04-20 Novozymes A/S Nettoyage de membranes de filtration d'eau

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US20240110131A1 (en) * 2021-02-10 2024-04-04 Bl Technologies, Inc. Enhanced enzymatic cleaner for membranes and method of cleaning thereof

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US8906839B2 (en) 1997-01-13 2014-12-09 Ecolab Usa Inc. Alkaline detergent containing mixing organic and inorganic sequestrants resulting in improved soil removal
WO2000011962A1 (fr) * 1998-08-27 2000-03-09 Henkel Ecolab Gmbh & Co. Ohg Procede de nettoyage de chauffe-lait
US7795199B2 (en) 2000-06-29 2010-09-14 Ecolab Inc. Stable antimicrobial compositions including spore, bacteria, fungi, and/or enzyme
US6624132B1 (en) 2000-06-29 2003-09-23 Ecolab Inc. Stable liquid enzyme compositions with enhanced activity
US7553806B2 (en) 2000-06-29 2009-06-30 Ecolab Inc. Stable liquid enzyme compositions with enhanced activity
FR2818150A1 (fr) * 2000-12-15 2002-06-21 Anios Lab Sarl Composition pour le traitement d'objets destines a etre desinfectes
WO2002047484A1 (fr) * 2000-12-15 2002-06-20 Laboratoires Anios Composition pour le traitement d'objets destines a etre desinfectes
WO2002050233A1 (fr) * 2000-12-21 2002-06-27 Ecolab Inc. Utilisation de produits a base d'acide percarboxylique, contenant des tensio-actifs et moussant peu pour la desinfection en circuit ferme
US7226898B2 (en) 2000-12-21 2007-06-05 Ecolab Inc. Use of low foam percarboxylic acid based products containing surfactants for cip-disinfection
WO2002081755A1 (fr) * 2001-04-04 2002-10-17 West Agro, Inc. Procede de nettoyage de la tuyauterie d'une laiterie par pre-traitement enzymatique
US6472199B1 (en) * 2001-04-04 2002-10-29 West Agro, Inc. Method of cleaning dairy pipelines using enzyme pretreatment
US20100233333A1 (en) * 2007-09-04 2010-09-16 Elizabeth Varriano-Marston Method for controlling banana and plantain quality by packaging
US10687539B2 (en) 2007-09-04 2020-06-23 Windham Packaging, Llc Modified atmosphere packaging for transportation and ripening of bananas and plantains with extended quality preservation
US10010089B2 (en) * 2007-09-04 2018-07-03 Windham Packaging, Llc Method for controlling banana and plantain quality by packaging
US8232088B2 (en) 2008-09-05 2012-07-31 TransAlgae Ltd Genetically engineered herbicide resistance for maintaining axenic cultures
US8603795B2 (en) 2009-04-30 2013-12-10 Ab Enzymes Oy Fungal protease and use thereof
US9353192B2 (en) 2009-04-30 2016-05-31 Roquette Freres Method for purifying glucose polymers for peritoneal dialysis solutions
US8609390B2 (en) 2009-04-30 2013-12-17 Ab Enzymes Oy Fungal serine protease and use thereof
US8877912B2 (en) 2009-04-30 2014-11-04 Ab Enzymes Oy Nucleic acids encoding fungal serine protease
WO2010125315A1 (fr) * 2009-04-30 2010-11-04 Roquette Freres Procede de purification de polymeres de glucose destines aux solutions de dialyse peritoneale
US8937170B2 (en) 2009-04-30 2015-01-20 Ab Enzymes Oy Nucleic acids encoding fungal protease
WO2011003968A1 (fr) 2009-07-08 2011-01-13 Ab Enzymes Oy Protéase fongique et son utilisation
US8362222B2 (en) 2009-07-08 2013-01-29 Ab Enzymes Oy Fungal protease and use thereof
US8945900B2 (en) 2010-10-29 2015-02-03 Ab Enzymes Oy Variants of fungal serine protease
US9404164B2 (en) 2011-03-31 2016-08-02 Ab Enzymes Oy Protease enzyme and uses thereof
US10221377B2 (en) 2011-03-31 2019-03-05 Ab Enzymes Oy Protease enzyme and uses thereof
WO2013120515A1 (fr) 2012-02-15 2013-08-22 Ecolab Usa Inc Procédé d'inactivation enzymatique
WO2016046334A1 (fr) * 2014-09-25 2016-03-31 Novozymes A/S Utilisation d'enzyme pour le nettoyage
WO2016096996A1 (fr) 2014-12-16 2016-06-23 Novozymes A/S Polypeptides ayant une activité n-acétylglucosamine oxydase
CN105169953A (zh) * 2015-09-29 2015-12-23 唐山沃德环保技术有限公司 用于清洗反渗透膜微生物污染的酶质清洗剂及其使用方法
WO2017066510A1 (fr) 2015-10-14 2017-04-20 Novozymes A/S Nettoyage de membranes de filtration d'eau
US10675589B2 (en) 2015-10-14 2020-06-09 Novozymes A/S Cleaning of water filtration membranes

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