WO2007115191A2 - Procédé pour accroître l'efficacité de collecteurs de graisse - Google Patents

Procédé pour accroître l'efficacité de collecteurs de graisse Download PDF

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Publication number
WO2007115191A2
WO2007115191A2 PCT/US2007/065666 US2007065666W WO2007115191A2 WO 2007115191 A2 WO2007115191 A2 WO 2007115191A2 US 2007065666 W US2007065666 W US 2007065666W WO 2007115191 A2 WO2007115191 A2 WO 2007115191A2
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WO
WIPO (PCT)
Prior art keywords
lipase
fog
grease
phospholipase
klu
Prior art date
Legal status (The legal status 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 status listed.)
Ceased
Application number
PCT/US2007/065666
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English (en)
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WO2007115191A3 (fr
Inventor
Jason W. Holmes
Julie Clemmons
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes North America Inc
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Novozymes North America Inc
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Filing date
Publication date
Application filed by Novozymes North America Inc filed Critical Novozymes North America Inc
Publication of WO2007115191A2 publication Critical patent/WO2007115191A2/fr
Anticipated expiration legal-status Critical
Publication of WO2007115191A3 publication Critical patent/WO2007115191A3/fr
Ceased legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F3/00—Biological treatment of water, waste water, or sewage
    • C02F3/34—Biological treatment of water, waste water, or sewage characterised by the microorganisms used
    • C02F3/342—Biological treatment of water, waste water, or sewage characterised by the microorganisms used characterised by the enzymes used
    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F1/00—Treatment of water, waste water, or sewage
    • C02F1/40—Devices for separating or removing fatty or oily substances or similar floating material

Definitions

  • TITLE METHOD FOR INCREASING THE EFFICIENCY OF GREASE TRAPS
  • the present invention relates to methods for enhancing the efficiency of grease traps or other similar devices.
  • FOG i.e., Fats, Oils and Grease
  • grease traps or grease interceptors
  • a grease trap works by slowing down the flow of warm/hot greasy water and allowing it to cool. As the water cools, the grease and oil separate and float to the top of the grease trap. The cooler water (less grease) continues to flow down the outlet pipe to the sewer.
  • Grease traps often contain baffles, which cover the inlet and outlet of the grease trap tank. The baffles trap the FOG and prevent FOG from flowing out of the trap. For the FOG to float to the top it is necessary to calm the water as turbulence only perplexes the separation. The FOG floating on the surface is periodically removed by hand or pump truck to avoid clogging of the grease trap.
  • US patent no. 6,649,401 -B2 discloses gram-positive Bacillus megaterium producing extracellular lipases that degrades fats, oils and grease (FOG).
  • the bacterium may be used in grease traps where fatty acid or grease needs to be degraded.
  • Fig. 1 shows the dose response of FOG treated with Lipase A dosed from 4.23 to 423 KLU/L.
  • Fig. 2 shows the response of Lipase A dosed at 2,112 KLU/L and the dose response of FOG treated with Phospholipase A dosed from 5 to 486 KLU/L.
  • the present invention relates to methods for enhancing the efficiency of grease traps, or other similar devices.
  • the inventors have found that when adding fungal lipase to a grease trap the
  • FOG layer that floats to the top of the grease trap is stabilized and hardened. This results in a decreased amount of FOG in the effluent leaving the grease trap and thus less FOG entering the public wastewater system.
  • the hardening of the FOG also facilitates handling and removal of FOG in the grease trap.
  • the invention relates to a method of enhancing the efficiency of grease traps, or other similar devices, wherein FOG in the grease trap is subjected to fungal lipase.
  • the fungal lipase and optionally other enzyme activities are added as mono-component enzyme products. Further, the FOG is not subjected to bacteria, especially lipase producing bacteria.
  • Lipases Suitable lipases according to the invention are of fungal origin. Chemically modified or protein engineered mutants (i.e., variants) are included.
  • the lipase belongs to the EC 3.1.1.3.
  • useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580.
  • fungal lipase variants are those described in WO 92/05249, WO 94/01541 , EP 407 225, EP 260 105, WO 95/35381 , WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079, WO 97/07202, and WO 00/60063.
  • the lipase used for treating FOG in the grease trap is a Humicola lanuginose lipase variant disclosed in WO 00/60063 selected from the group consisting of:
  • lipase enzymes include LipolaseTM, Lipoprime, Lipolase UltraTM, LipomaxTM, LiposamTM, and LipexTM (Novozymes AJS).
  • the fungal lipase is a phospholipase.
  • phospholipase is an enzyme which has activity towards phospholipids.
  • the phospholipase is a phospholipase A 1 (EC. 3.1.1.32). In another preferred embodiment of the invention the phospholipase is a phospholipase A 2 (EC.3.1.1.4.).
  • the fungal phospholipase may be derived from a strain of the class Pyrenomycetes, such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F. oxysporum.
  • the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be the one concerned in WO 98/026057 displayed in SEQ ID NO: 2 derived from Fusarium oxysporum DSM 2672, or variants thereof.
  • the phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus,
  • Preferred phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa.
  • the phospholipase may be a variant, such as one of the variants disclosed in WO 00/32758, which are hereby incorporated by reference.
  • Preferred phospholipase variants include variants listed in Example 5 of WO 00/32758, which is hereby specifically incorporated by reference.
  • the phospholipase is one described in WO 04/111216, especially the variants listed in the table in Example 1.
  • LECITASETM and LECITASETM ULTRA examples include LECITASETM and LECITASETM ULTRA, or LIPOPANTM F (available from Novozymes A/S, Denmark).
  • the lipase may be dosed in the range from 1-1 ,000 mg per kg FOG, preferably 5-800 mg/kg FOG, especially 10-600 mg/kg FOG; or 10-100,00 KLU per kg FOG, preferably 50-80,000 KLU per kg FOG, especially 100-60,000 KLU per kg FOG.
  • the lipase may be dosed in the range from 0.1-10,000 KLU/L grease traps influent, preferably 1-8,000 KLU/L grease traps influent, especially 2-5,000 grease traps influent.
  • protease may advantageously be added to disperse the FOG.
  • Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included.
  • the protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • 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 are trypsin (e.g.
  • proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274.
  • Preferred commercially available protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • enzyme activities may be present when practicing a method of the invention.
  • examples of such other enzymes are cellulases (endo-glucanases), beta- glucanases, hemicellulases, alpha-amylases, cutinases, pectinases, pectate lyases, or mixtures thereof.
  • Chemicals used as buffers and reagents were commercial products of at least reagent grade.
  • Lipase A is a variant of Humicola lanuginosa disclosed as SEQ ID NO: 2 in US patent no. 5,869,438 with the following amino acid substitutions: T231 R + N233R. The variant is also disclosed in the Example in WO 00/60063. Lipase A is available from Novozymes A/S, Denmark.
  • Phospholipase A is a variant of Humicola lanuginosa sequence disclosed as SEQ ID NO: 2 in US patent no. 5,869,438 with the following amino acid substitutions and C- terminal extension: G91A +D96W +E99K +G263Q +L264A +I265T +G266D +T267A +L269N+270AGGFS It is expressed in A. oryzae.
  • the variant is described in Example 5 in WO 0032758 which reference is hereby incorporated by reference.
  • FOG Actual FOG collected from a sanitary liftstation.
  • the FOG used in Example 2 was colleted from a Zebulon, NC, USA, liftstation directly downstream from a commercial "Hardee's" restaurant.
  • the liftstation is #151 under the care of the City of Raleigh Waste Water Authority; the physical address is 615 West Gannon Ave. Zebulon, NC 27597.
  • the lipolytic activity was determined using tributyrine as substrate. This method was based on the hydrolysis of tributyrin by the enzyme, and the alkali consumption is registered as a function of time.
  • One Lipase Unit is defined as the amount of enzyme which, under standard conditions (i.e. at 3O 0 C; pH 7.0; with Gum Arabic as emulsifier and tributyrine as substrate) liberates 1 micro mol titrable butyric acid per minute.
  • the FOG containing tubes were placed in a water bath at a temperature of 5O 0 C for 24 hours to revert the FOG into its liquid state; an oily, viscous emulsion.
  • Figs 1 and 2 The result of the treatment with Lipase A and Phospholipase A are shown in Figs 1 and 2.
  • Fig. 1 tubes from left to right:
  • Lipase A 106 KLU/L of Lipase A 1 212 KLU/L of Lipase A; and 423 KLU/L of Lipase A
  • Fig. 2 Tubes from left to right: 2,115 KLU/L of Lipase A;

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  • Life Sciences & Earth Sciences (AREA)
  • Microbiology (AREA)
  • Biodiversity & Conservation Biology (AREA)
  • Hydrology & Water Resources (AREA)
  • Engineering & Computer Science (AREA)
  • Environmental & Geological Engineering (AREA)
  • Water Supply & Treatment (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

La présente invention concerne des procédés pour améliorer l'efficacité de collecteurs de graisse ou d'autres dispositifs similaires, en soumettant les matières grasses, les huiles et les graisses dans le collecteur à graisse à de la lipase fongique.
PCT/US2007/065666 2006-03-31 2007-03-30 Procédé pour accroître l'efficacité de collecteurs de graisse Ceased WO2007115191A2 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US78792806P 2006-03-31 2006-03-31
US60/787,928 2006-03-31

Publications (2)

Publication Number Publication Date
WO2007115191A2 true WO2007115191A2 (fr) 2007-10-11
WO2007115191A3 WO2007115191A3 (fr) 2008-12-24

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PCT/US2007/065666 Ceased WO2007115191A2 (fr) 2006-03-31 2007-03-30 Procédé pour accroître l'efficacité de collecteurs de graisse

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Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0258068B1 (fr) * 1986-08-29 1994-08-31 Novo Nordisk A/S Additif enzymatique pour détergent
US4849357A (en) * 1986-10-08 1989-07-18 Miles Inc. Method for the preparation of a hydrophobic enzyme-containing composition and the composition produced thereby
US5464766A (en) * 1994-04-04 1995-11-07 Enzyme Research & Development Corporation Multienzyme powdered composition containing bacteria for treatment of waste
US5536436A (en) * 1994-05-27 1996-07-16 The Procter & Gamble Company Liquid laundry detergent compositions containing lipolytic enzyme and specially selected soaps
US6162634A (en) * 1999-04-14 2000-12-19 Roebic Laboratories, Inc. Enzyme-producing strain of Bacillus bacteria

Also Published As

Publication number Publication date
WO2007115191A3 (fr) 2008-12-24

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