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
  • C11D3/38663—Stabilised liquid enzyme compositions

Definitions

• the present invention relates to enzymatic liquid detergent compositions. More particularly, it relates to enzymatic liquid detergent compositions which incorporate proteolytic enzyme.
• proteolytic enzymes in liquid detergent compositions is well known; although these proteolytic enzymes can be of various types and sources, the proteolytic enzymes commonly used are those produced by Bacillus strains. Although with such proteolytic enzymes satisfactory results as regards performance can be achieved, it is frequently necessary to include enzyme-­stabilizing systems in the liquid detergent compositions to provide a satisfactory enzyme stability during storage of the enzymatic liquid detergent composition.
• Serine proteases from Bacillus subtilis are very widely known and used in detergent compositions.
• WO 88/03946 discloses, as detergent additives, combinations of Bacillus proteases with alkaline fungal or actinomycete proteases, e.g. those proteases obtainable from the genera Paecilomyces, Fusarium, and Nocardiopsis.
• the disclosure extends to the use of the detergent additive as a liquid, with a known enzyme stabiliser such as propylene glycol, for addition to a liquid detergent.
• USP 3 707 504 discloses detergents for laundry and dishwashing, comprising protease from Thermoactinomyces vulgaris ATCC 15734, which are formulated as solid or liquid detergent compositions. This document mentions surprising stability of protease from Thermoactinomyces vulgaris in highly-alkaline detergent systems.
• Proteinase K (E.C. 3.4.21.14) is a known alkaline serine protease. It is a fungal proteinase produced by the mould Tritirachium album (Limber). It has been the subject of several academic investigations, and relevant publications include Eur J Biochem 47 (1974), pages 91-97; and Hoppe-Seyler's Zeitschrift f Physiol Chemie 357 (1976), pages 937-947. In EMBO Journal 3(6), pages 1311-1314 (1984), A Pähler et al show the crystallographic 3D structure of proteinase K at a level of resolution that displays its secondary and tertiary protein structure. Furthermore, K-D Jany et al have published its full primary sequence in FEBS Letters 199(2) (1986) pages 139-144.
• JP 47-35192 describes the use of glycerol or sorbitol with borax under certain conditions and proportions, to stabilise enzyme preparations including liquid washing materials.
• GB 2 079 305 (Unilever) describes the use of polyols together with boric acid and/or borate and polyacrylate polymers as stabilising agents
• EP 0 080 223 (Unilever) describes the combined use of boric acid or borate and polyol or polyamino compounds with reducing salts
• EP 0 126 505 (Unilever) describes the use of boric acid or borate and reducing salts, together with succinic or other dicarboxylic acids.
• Other prior art deals with the use of stabilisers such as calcium formate/acetate.
• a further aim of this invention is to provide liquid detergent compositions incorporating enzymes which need less than normal amounts of such enzyme stabilisers as those mentioned above, and/or which can be formulated without such stabilisers, for useful storage stability.
• enzymes of the Proteinase K type are of particular value as proteolytic enzymes in enzymatic liquid detergent compositions.
• a liquid detergent composition comprising a surfactant concentrate and a proteolytic enzyme derived from a microorganism, characterised in that the proteolytic enzyme is a fungal alkaline protease of the proteinase K type, for improved storage stability in the liquid state.
• proteolytic enzymes can provide liquid detergent compositions with an improved enzyme storage stability compared with the aforementioned Bacillus-originating proteases, and also in comparison with the above-mentioned alkaline protease from Thermoactinomyces, even in the absence (or presence in lower amounts than previously proposed) of enzyme-­stabilizing systems.
• proteinase K is especially effective in breaking down native keratin and other native proteins.
• equivalents of the proteinase K from Tritirachium album are considered to be those fungal alkaline serine proteinases which show substantial homology with proteinase K itself, and possess the following characteristics: (i) presence of cysteine close to the protease active site; (ii) a content of tightly-bound calcium, bound with an affinity corresponding to dissociation pK (calcium) the order of about 5.5 to 8; (iii) presence of an SS (cystine) bridge in the protease tertiary structure; (iv) substantial resistance to inhibition of the protease activity by PCMB (parachloromercuribenzoate).
• proteinase K itself also has a content of SS (cystine) bridges in the molar ratio 2:1 to its content of (free) cysteine, and a further content of weakly-bound calcium substantially equal to its content of tightly-bound calcium.
• proteases produced by rDNA manipulation on the basis of genetic material corresponding to a protease of the proteinase K type, with or without modifications.
• Genetic engineering of the enzymes can be achieved by extraction of an appropriate alkaline serine protease gene, e.g. the gene for proteinase K from Tritirachium album Limber itself or from a mutant thereof, and introduction and expression of the gene or derivative thereof in a suitable producer organism.
• an appropriate alkaline serine protease gene e.g. the gene for proteinase K from Tritirachium album Limber itself or from a mutant thereof.
• analogues e.g. analogues made by mutant organisms
• derivatives and conjugates of the proteinases are also within the scope of the invention as equivalent to the use of the proteinases mentioned above.
• the preferred protease for use in this invention is Proteinase K from Tritirachium album (Limber).
• the proteinase K type enzyme can be used either alone or together with Bacillus or other common proteases, e.g. Savinase, Maxatase or Alcalase (Trade Marks) and/or other proteolytic enzymes, as well as with other types of enzymes such as lipases, amylases, cellulases and alcohol oxidases. Mixtures of the various other enzymes may also be present.
• Bacillus or other common proteases e.g. Savinase, Maxatase or Alcalase (Trade Marks) and/or other proteolytic enzymes, as well as with other types of enzymes such as lipases, amylases, cellulases and alcohol oxidases. Mixtures of the various other enzymes may also be present.
• the proteinase defined above can preferably be included according to the present invention in an amount of 1 to 100 GU/mg liquid detergent.
• a GU is a Glycine Unit, which is defined as the proteolytic enzyme activity which, under standard conditions, during a 15-minute-incubation at 40 deg C, with N-acetyl casein as substrate, produces an amount of NH2-group equivalent to 1 micromole of glycine.
• the amount ranges from 2 to 50 and particularly preferably from 5 to 20 GU/mg.
• liquid detergent compositions in which the proteinase is incorporated according to the present invention can be aqueous or non-aqueous, built or unbuilt liquid detergents which on their own are well known in the art. They have been amply described in the following patent specifications, hereby incorporated by reference : European patent 0 126 505 (Unilever) and European patent application 0 225 654.
• aqueous liquid detergent compositions comprise from 1-60% by weight of one or more detergent-active compounds, from 0-60% by weight of one or more organic and/or inorganic builders, and optionally other conventional ingredients such as soil-suspending agents, hydrotropes, corrosion inhibitors, dyes, perfumes, silicates, optical brighteners, suds depressants, germicides, anti-tarnishing agents, opacifiers, fabric softening agents, oxygen-liberating bleaches such as hydrogen peroxide, sodium perborate, diperisophthalic anhydride, with or without bleach precursors, buffers and the like.
• the liquid medium is usually an aqueous medium.
• the detergent-active compounds in the compositions can for example be anionic and/or nonionic surfactants, and the pH of the liquid detergent compositions can be chosen at will from a wide range, e.g. from about pH 7 upwards, e.g. a milder alkaline range from about pH 7.5 to about pH 9 or a stronger alkaline range from about pH 9 upwards.
• non-aqueous liquid detergent compositions the above ingredients and ranges also apply mutatis mutandis.
• these compositions contain a suspending medium for the other ingredients, the suspending medium comprising usually a nonionic detergent together with a suspending agent such as silica, a copolymer and the like.
• liquid detergent compositions contain inorganic or organic electrolyte salts
• liquid detergent compositions incorporating the defined protease as well as an enzyme-stabiliser, possibly in a lower amount than those amounts hitherto proposed.
• compositions may also comprise other detergent additives, for example without limitation polysaccharides such as pectinates and alginates chosen for compatibility with the pH and pI of the enzyme in use, and polycarboxylates, e.g. polyacrylates.
• detergent additives for example without limitation polysaccharides such as pectinates and alginates chosen for compatibility with the pH and pI of the enzyme in use, and polycarboxylates, e.g. polyacrylates.
• the invention is further illustrated by way of Example.
• Such a formulation can if desired be prepared in accordance with EP 0 266 199 (Unilever).
• the enzymes were dosed at 30 GU/ml wash liquor.
• the soils were AS 10, cocktail 1 and cocktail 2.
• the enzymes used were: -- Savinase (Bacillus protease), from Novo; -- an alkaline protease from Streptomyces griseus, from Calbiochem-Behring, which is reported to act on various keratinous proteins (as also applies to Proteinase K).
• Stability tests were performed in a liquid according to Example 1 with Savinase, Streptomyces griseus protease, a 1:1 mixture of Savinase with Strept. gris. protease and Proteinase K.
• the storage temperature was 37 deg C.
• the pH was adjusted to 10 with citric acid.
• the stability at 37 deg C of the following enzymes was as follows: % RA Savinase 10 after 1 day Alcalase 15 after 29 hours Proteinase K 26 after 9 days
• Example 4 The wash test of Example 4 was repeated, with the liquid detergent (pH v 10.8) as used in Example 4. By addition of NaCl the ionic strength was increased, and the wash performance was compared (expressed in % reflectance at 460 nm).

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• Chemical & Material Sciences (AREA)
• Life Sciences & Earth Sciences (AREA)
• Engineering & Computer Science (AREA)
• Chemical Kinetics & Catalysis (AREA)
• Oil, Petroleum & Natural Gas (AREA)
• Wood Science & Technology (AREA)
• Organic Chemistry (AREA)
• Detergent Compositions (AREA)
• Cosmetics (AREA)

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Citations (3)

• 1987
  • 1987-11-18 GB GB878726999A patent/GB8726999D0/en active Pending
• 1988
  • 1988-11-17 BR BR888806028A patent/BR8806028A/pt not_active Application Discontinuation
  • 1988-11-17 NO NO885128A patent/NO171993C/no unknown
  • 1988-11-17 AU AU25683/88A patent/AU610286B2/en not_active Ceased
  • 1988-11-17 EP EP19880310846 patent/EP0317307A3/de not_active Withdrawn
  • 1988-11-18 JP JP63292248A patent/JPH02153999A/ja active Pending
  • 1988-11-18 ZA ZA888661A patent/ZA888661B/xx unknown

Patent Citations (3)

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