WO2017186943A1 - Detergent compositions and uses thereof - Google Patents

Detergent compositions and uses thereof Download PDF

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Publication number
WO2017186943A1
WO2017186943A1 PCT/EP2017/060265 EP2017060265W WO2017186943A1 WO 2017186943 A1 WO2017186943 A1 WO 2017186943A1 EP 2017060265 W EP2017060265 W EP 2017060265W WO 2017186943 A1 WO2017186943 A1 WO 2017186943A1
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WO
WIPO (PCT)
Prior art keywords
seq
polypeptide
sodium
polypeptides
item
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/EP2017/060265
Other languages
English (en)
French (fr)
Inventor
Christian B OEHLENSCHLAEGER
Dorotea R SEGURA
Rebecca M VEJBORG
Henrik M GEERTZ-HANSEN
Lilian E T BALTSEN
Jesper SALOMON
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 AS
Original Assignee
Novozymes AS
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
Priority to EP20154615.7A priority Critical patent/EP3693449A1/en
Priority to MX2018013139A priority patent/MX391044B/es
Priority to JP2018555897A priority patent/JP6959259B2/ja
Priority to CN201780026089.0A priority patent/CN109312271A/zh
Priority to BR112018072282-0A priority patent/BR112018072282A2/pt
Priority to EP17723032.3A priority patent/EP3448978B1/en
Application filed by Novozymes AS filed Critical Novozymes AS
Priority to US16/094,740 priority patent/US10626354B2/en
Publication of WO2017186943A1 publication Critical patent/WO2017186943A1/en
Anticipated expiration legal-status Critical
Priority to US16/815,281 priority patent/US11680231B2/en
Priority to US18/310,817 priority patent/US12241045B2/en
Priority to US19/038,219 priority patent/US20250171717A1/en
Ceased legal-status Critical Current

Links

Classifications

    • 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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • 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
    • C11D3/38663—Stabilised liquid enzyme compositions
    • 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
    • C11D3/38681—Chemically modified or immobilised enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • 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)
    • C12Y302/01052—Beta-N-acetylhexosaminidase (3.2.1.52)
    • 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
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • Biofilm may also be present on laundry items, such as fabrics, other hard surfaces, such as dish wash utensils, dish washers and washing machines where they may cause malodor, which is difficult to remove even after wash.
  • the application WO9850512 (Procter and Gamble) disclose laundry or cleaning products comprising one or more hexosaminidase enzymes.
  • the present invention provides suitable enzymes for use in detergents and for deep cleaning of items such as laundry and cleaning process.
  • Figure 3 A phylogenetic tree of the polypeptides of the invention
  • a fragment contains at least 300 amino acid residues (e.g., amino acids 1 to 300 of SEQ ID NO 4), at least 305 amino acid residues (e.g., amino acids 1 to 305 of SEQ ID NO 4), at least 310 amino acid residues (e.g., amino acids 1 to 310 of SEQ ID NO 4), at least 315 amino acid residues (e.g., amino acids 1 to 315 of SEQ ID NO 4), or at least 320 amino acid residues (e.g., amino acids 1 to 320 of SEQ ID NO 4).
  • the Terribacillus clade comprises homologous sequences.
  • the polypeptides with hexosaminidase activity of the present invention having the mature amino acid sequences SEQ ID 7, 8 and 9 can be pairwise aligned using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443- 453). The percent identities resulting from such alignments are shown in Table 1 below.
  • One aspect of the invention relates to a polypeptide comprising the amino acid sequence shown in SEQ ID NO 9 or is a polypeptide having at least 95 %, such as at least 96%, such as at least 97%, such as at least 98%, such as at least 99% or 100% sequence identity hereto, wherein the polypeptide has hexosaminidase activity.
  • the polypeptides of the invention comprise the [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 19) motif.
  • the polypeptides of the invention comprise the motif [VI M][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO: 20).
  • the polypeptides of the invention comprise the motif WND[SQR][IVL][TLVM] (SEQ ID NO: 21 ).
  • the polypeptides of the invention comprise the motif QSTL (SEQ ID NO 22).
  • the polypeptides of the invention comprise the motif NKFFY (SEQ ID NO: 23).
  • the polypeptides of the invention comprise the motif NLD[DR]S (SEQ ID NO: 24).
  • some aspects of the invention relate to cleaning compositon e.g. detergent compositions comprising: a) at least 0.0001 ppm e.g. 0.001 ppm polypeptide of the Terribacillus clade, optionally comprising one or more motif selected from the group consisting of GXDE (SEQ ID NO 18), [EQ][NRSHA][YVFL][AGSTC][IVLF][EAQYN][SN] (SEQ ID NO 19),
  • [VIM][LIV]G[GAV]DE[VI][PSA] (SEQ ID NO: 20), WND[SQR][IVL][TLVM] (SEQ ID NO: 21 ), QSTL (SEQ ID NO 22), NKFFY (SEQ ID NO: 23), NLD[DR]S (SEQ ID NO: 24), wherein the enzyme polypeptide is selected from the group consisting of SEQ ID NO 7, SEQ ID NO 8, SEQ ID NO 9, SEQ ID NO 10, SEQ ID NO 1 1 and polypeptides having at least 60%, such as at least 70%, such as at least 80% or such as at least 90% sequence identity hereto, wherein the polypeptide has hexosaminidase activity, and optionally b) from about 10 wt% to about 50 wt% builder preferably selected from citric acid, methylglycine-N, N-diacetic acid (MGDA) and/or glutamic acid-N, N-diacetic acid (GLDA) and mixtures
  • One aspect of the invention relates to the use of a polypeptide of the Terribacillus clade having hexosaminidase activity for preventing, reducing or removing re-deposition of soil during a wash cycle. Further, one aspect of the invention relates to the use of a polypeptide of the Terribacillus clade having hexosaminidase activity for preventing, reducing or removing the adherence of soil to an item. In one embodiment, the item is textile. When the soil does not adhere to the item, the item appears cleaner. Thus, the invention further concerns the use of a polypeptide of the Terribacillus clade having hexosaminidase activity for maintaining or improving the whiteness of the item.
  • insolens W096/13580
  • lipase from strains of Pseudomonas e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp. strain SD705 (WO95/06720 & WO96/27002), P.
  • SEQ ID NO 8, SEQ ID NO 9, SEQ ID NO 10, SEQ ID NO 1 1 or a polypeptide having hexosaminidase activity and having at least 60% sequence identity hereto the cleaning composition of the invention may further comprise amylases which can be used together with a polypeptide of the invention.
  • the amylase may be an alpha-amylase or a glucoamylase 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.
  • More preferred polypeptides of SEQ ID NO 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 I, T165I, K178L, T182G, M201 L, 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 polypeptides of SEQ ID NO 2 are those having the substitutions:
  • 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.
  • the present invention relates to polypeptides of the clade of Terribacillus having a sequence identity to the mature polypeptide of SEQ ID NO 13 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, 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%, which have hexosaminidase activity.
  • the polypeptides differ by up to 10 amino acids, e.g., 1 , 2, 3, 4, 5, 6, 7, 8, 9, or 10, from the mature polypeptide shown in SEQ ID NO 10.
  • E. coli lac operon E. coli trc promoter (Egon et al., 1988, Gene 69: 301 -315), Streptomyces coelicolor agarase gene ⁇ dagA), and prokaryotic beta-lactamase gene (Villa- Kamaroff et al., 1978, Proc. Natl. Acad. Sci. USA 75: 3727-3731 ), as well as the tac promoter (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA 80: 21 -25).
  • Preferred terminators for yeast host cells are obtained from the genes for Saccharomyces cerevisiae enolase, Saccharomyces cerevisiae cytochrome C (CYC1 ), and Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Other useful terminators for yeast host cells are described by Romanos et al., 1992, supra.
  • the control sequence may also be an mRNA stabilizer region downstream of a promoter and upstream of the coding sequence of a gene which increases expression of the gene.
  • the recombinant expression vector may be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA procedures and can bring about expression of the polynucleotide.
  • the choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced.
  • the vector may be a linear or closed circular plasmid.
  • bacterial selectable markers are Bacillus licheniformis or Bacillus subtilis dal genes, or markers that confer antibiotic resistance such as ampicillin, chloramphenicol, kanamycin, neomycin, spectinomycin, or tetracycline resistance.
  • Suitable markers for yeast host cells include, but are not limited to, ADE2, HIS3, LEU2, LYS2, MET3, TRP1 , and URA3.
  • origins of replication for use in a yeast host cell are the 2 micron origin of replication, ARS1 , ARS4, the combination of ARS1 and CEN3, and the combination of ARS4 and CEN6.
  • the prokaryotic host cell may be any Gram-positive or Gram-negative bacterium.
  • Gram- positive bacteria include, but are not limited to, Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, and Streptomyces.
  • Gram-negative bacteria include, but are not limited to, Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.
  • polypeptide is selected from the group consisting of polypeptides having at least 60% e.g. 80%, 85%, 90%, 95%, 98%, 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO 7, SEQ ID NO 8, SEQ ID NO 9, SEQ ID NO 10 and SEQ ID NO 1 1.
  • the concentration of the polypeptide of the invention is 0.00001 % to 2 wt %, such as 0.0001 to 0.1 wt%, such as 0.0005 to 0.1 wt%, such as 0.001 to 0.1 wt%, such as 0.001 to 0.5 wt%, such as 0.002 to 0.5 wt% or 0.0002 to 0.09 wt% in the total detergent concentration.
  • polypeptide of paragraph 46 or 47 having at least 60%, at least 65%, at least 70%, at least 75%, 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 mature polypeptide of SEQ ID NO 2 or to the mature polypeptide shown in SEQ ID NO 7.
  • a nucleic acid construct or expression vector comprising a gene encoding a protein operably linked to the polynucleotide of paragraph 57, wherein the gene is foreign to the polynucleotide encoding the signal peptide.
  • the S.aureus culture was diluted (1 :100) in fresh TSB + 1 % glucose (24563; Roquette Freres) and 2 mL aliquots were added to the wells of 12-well polystyrene flat-bottom microplates (3512; Costar, Corning Incorporated, Corning, NY, USA), in which round swatches (diameter 2 cm) of sterile polyester (WFK30A) had been placed. Sterile TSB + 1 % glucose was added to control wells. After 48 h at 37°C (static incubation), the swatches were rinsed twice with 15°dH water.
  • test tubes Five rinsed swatches (sterile or with S.aureus) were placed in 50 mL test tubes and 10 mL of wash liquor (15°dH water with 0.2 g/L iron(lll) oxide nanopowder (544884; Sigma-Aldrich) with 3.33g/L liquid model A detergent) and 0.2 ppm enzyme (mature polypeptide with SEQ ID NO 7, 8 and 9) were added to each tube. Washes without enzyme were included as controls. The test tubes were placed in a Stuart rotator and incubated for 1 hour at 37°C at 20 rpm. The wash liquor was then removed, and the swatches were rinsed twice with 15°dH water and dried on filter paper over night.
  • wash liquor 15°dH water with 0.2 g/L iron(lll) oxide nanopowder (544884; Sigma-Aldrich) with 3.33g/L liquid model A detergent
  • 0.2 ppm enzyme mature polypeptide with SEQ ID NO 7, 8 and 9 were
  • polypeptides in Glyco_hydro_20 can be separated into multiple distinct sub-clusters, or clades as listed below.
  • the distinct motifs for each clade are described in details below. Generation of IAS domain

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
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  • Oil, Petroleum & Natural Gas (AREA)
  • General Engineering & Computer Science (AREA)
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PCT/EP2017/060265 2014-04-29 2017-04-28 Detergent compositions and uses thereof Ceased WO2017186943A1 (en)

Priority Applications (10)

Application Number Priority Date Filing Date Title
US16/094,740 US10626354B2 (en) 2016-04-29 2017-04-28 Detergent compositions and uses thereof
MX2018013139A MX391044B (es) 2016-04-29 2017-04-28 Composiciones detergentes y sus usos.
JP2018555897A JP6959259B2 (ja) 2016-04-29 2017-04-28 洗剤組成物およびその使用
CN201780026089.0A CN109312271A (zh) 2016-04-29 2017-04-28 洗涤剂组合物及其用途
BR112018072282-0A BR112018072282A2 (pt) 2016-04-29 2017-04-28 composições detergentes e usos das mesmas
EP20154615.7A EP3693449A1 (en) 2016-04-29 2017-04-28 Detergent compositions and uses thereof
EP17723032.3A EP3448978B1 (en) 2016-04-29 2017-04-28 Detergent compositions and uses thereof
US16/815,281 US11680231B2 (en) 2016-04-29 2020-03-11 Detergent compositions and uses thereof
US18/310,817 US12241045B2 (en) 2016-04-29 2023-05-02 Detergent compositions and uses thereof
US19/038,219 US20250171717A1 (en) 2014-04-29 2025-01-27 Detergent compositions and uses thereof

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DKPA201600262 2016-04-29
DKPA201600262 2016-04-29

Related Child Applications (2)

Application Number Title Priority Date Filing Date
US16/094,740 A-371-Of-International US10626354B2 (en) 2016-04-29 2017-04-28 Detergent compositions and uses thereof
US16/815,281 Continuation US11680231B2 (en) 2014-04-29 2020-03-11 Detergent compositions and uses thereof

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WO2017186943A1 true WO2017186943A1 (en) 2017-11-02

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US (4) US10626354B2 (https=)
EP (2) EP3693449A1 (https=)
JP (1) JP6959259B2 (https=)
CN (1) CN109312271A (https=)
BR (1) BR112018072282A2 (https=)
MX (1) MX391044B (https=)
WO (1) WO2017186943A1 (https=)

Cited By (71)

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WO2019086528A1 (en) * 2017-11-01 2019-05-09 Novozymes A/S Polypeptides and compositions comprising such polypeptides
WO2020007875A1 (en) 2018-07-03 2020-01-09 Novozymes A/S Cleaning compositions and uses thereof
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WO2021122121A1 (en) 2019-12-20 2021-06-24 Henkel Ag & Co. Kgaa Cleaning compositions comprising dispersins ix
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WO2022235720A1 (en) 2021-05-05 2022-11-10 The Procter & Gamble Company Methods for making cleaning compositions and detecting soils
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WO2023138535A1 (en) * 2022-01-21 2023-07-27 Novozymes A/S Cleaning method, use of enzymes and cleaning composition
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