EP1248534A1 - Pressurisation hyperbare de proteines et utilisations therapeutiques des proteines ainsi pressurisees - Google Patents
Pressurisation hyperbare de proteines et utilisations therapeutiques des proteines ainsi pressuriseesInfo
- Publication number
- EP1248534A1 EP1248534A1 EP01901095A EP01901095A EP1248534A1 EP 1248534 A1 EP1248534 A1 EP 1248534A1 EP 01901095 A EP01901095 A EP 01901095A EP 01901095 A EP01901095 A EP 01901095A EP 1248534 A1 EP1248534 A1 EP 1248534A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- protein
- proteins
- group
- whey
- protein composition
- 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.)
- Withdrawn
Links
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/015—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with pressure variation, shock, acceleration or shear stress or cavitation
- A23L3/0155—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with pressure variation, shock, acceleration or shear stress or cavitation using sub- or super-atmospheric pressures, or pressure variations transmitted by a liquid or gas
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/30—Physical treatment, e.g. electrical or magnetic means, wave energy or irradiation
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Definitions
- the invention relates to hyperbaric pressurization of proteins and therapeutical uses of such pressurized proteins as stimulatory growth and/or antioxidant and tissue glutathione inducing agents.
- dietary proteins such as whey to undergo digestion can greatly affect their physiological properties.
- Increased insoluble or poorly digested protein in the upper intestine decreases the bioavailability of bioactive peptides hidden in an inactive state inside the polypeptide chain (Meisel H, Frister H, Schlimme E. Z. Ernahrungswiss 1989; 28:267- 278) .
- TBARS plasma thiobarbituric acid reacting substances
- GSH-promoting and antioxidant activities of whey proteins have been related to their capability to provide GSH precursors in the form of peptides, such as ⁇ -glutamylcysteine, which can readily cross cell membranes (Baruchel, S., Viau, G. Anticancer Res . 1996; 16:1095-1100).
- ⁇ -glutamylcysteine groups has been indicated to be rare in food proteins except for whey and egg albumin (Bounous G., Gold P., 1991, Clin . Invest . Med. 14:296- 301).
- Cow's milk allergy is believed to be due to interaction between ⁇ -lactoglobulin and other milk proteins and the immune system, which is generally IgE or IgG mediated (Pediatr 121: S16, (1992)).
- the antigenicity of a protein molecule is a function of both its primary structure and the conformation of the molecule. Food allergens are resistant to digestion and thus can be presented to the immune system in the gut (Astwood JD et al . Nature Biotech 14:1269 (1996)). In particular, proteins with a high disulphide content are highly resistant to digestion and have been strongly implicated in the allergenic responses (Del Val G. et al., J Allergy Clin Immunol 103:690-7, (1999)).
- Disulphide-rich whey proteins such as ⁇ -lactoglobulin are particularly resistant to both digestion due to their rigid and compact tertiary structure and conformation (Hagemeister H, Antila P. J. Anim . Physiol . Anim . Nutr. 1994; 72:86-91). These proteins apparently remain intact after their passage through the stomach (Hagemeister H, Antila P. J. Anim . Physiol . Anim . Nutr. 1994; 72:86-91).
- ⁇ -lactoglobulin to digestive enzymes such as pepsin has been related to the simultaneous presence of two disulfide bridges and one free thiol group which give a rigid structure to this protein, allowing many exchanges with the S-S bonds (Schimdt DG, Poll JK. Neth. Milk Dairy J 1991 45:240-255).
- Schimdt DG Poll JK. Neth. Milk Dairy J 1991 45:240-255
- the cleavage of the S-S bonds is required to decrease the surface polarity of the molecule and to expose the hydrophobic groups to the polar environment, which could, in turn, increase the digestibility of the protein as well as decrease its allergenic
- U.S. Patent No 5,476,677 there is disclosed a single pressure treatment of rice between 1000 atm to 9000 atm, to reduce cooking time by denaturing rice proteins. Their processing also refers to drying after with pressurization to exert the treating rice via pressure for human consumption as opposed to cooking via heating.
- the U.S. Patent No. 5,476,677 also claim that the pressure treatment of rice induce hypoallergenic effects on the rice.
- One aim of the present invention is to provide a specific unique pressurization technique on proteins resulting in potent stimulatory growth and antioxidant effects via increase in availability of SH group and increase in digestibility of proteins.
- a method to induce conformational changes in proteins to enhance their susceptibility to enzymes which comprises the step of: a) exposing a protein in a solution, having a concentration of about 0.01% to about 50%, to a pressurization treatment sufficient to induce permanent conformational changes in proteins.
- the enzymes may be digestive enzymes and when locate in vivo enhances digestibility of the protein.
- the method in accordance with a preferred embodiment of the present invention wherein the pressurization treatment is followed by about 3-5 minutes of holding time at 400 MPa.
- the method may further comprises a step effected prior to step a) , wherein the protein is solubilized in solution by adding a solubilization agent or by storing the protein solution at about 4°C for at least 12 hours .
- the protein is selected from the group consisting of whey, caseins, soy, egg, peanut, legume, nut, milk, fish, meat proteins, hormones and albumin such as egg albumin and Human Serum Albumin (HAS) .
- the protein may be solubilized in a solution selected from the group consisting of aqueous, saline, isoelectric, isotonic, and buffered solutions, nutrient-based solutions and formulas used in infant feeding and in enteral and parenteral nutrition.
- the preferred protein concentration is of about
- the preferred pressurization treatment is a mixture of pulse and continuous mode which is a combination of at least 2 cycles, preferably 3-6 cycles at 400 MPa and which may optionally be followed by a 5- 10 minutes of holding time, at 400 MPa.
- the optimal number of cycles, holding time and pressure treatment however will vary according to the protein concentration of the solution and the type of application.
- the pressurization treatment is effected at a temperature ranging between 0 and 80 °C, preferably 20°C.
- a protein composition having enhanced in vivo susceptibility to digestive enzymes for administration to an animal which comprises between 1% (w/w) to 100% (w/w) protein prepared by the method of the present invention; and an acceptable pharmaceutical carrier between 0% (w/w) to 99% (w/w) .
- the enhanced susceptibility of the protein composition may cause stimulatory growth effect, increased fur quality and/or calm behavior, antioxidant properties and/or tissue glutathione enhancing properties for the animal.
- the antioxidant properties of the protein composition may cause enhanced redness of the animal meat .
- the preferred protein composition contains 24% (w/w) protein; however, the effects can be exerted with a range of different protein concentrations .
- An acceptable pharmaceutical carrier may be selected, without limitation, from the group consisting of exipient for oral, topical, intravenous, systemic, intraperitoneal or subcutaneous administration to the animal .
- An oral exipient may be selected from the group consisting of food, water, juice, milk, carbonated and non-carbonated beverages, sweetened and unsweetened drinks, enteral, parenteral, infant formulas and health drinks .
- a method to stimulate growth, increase fur quality and/or calm behavior of an animal which comprises administering an effective amount the protein composition of the present invention.
- the protein composition of the present invention in the preparation of a medicament to stimulate growth, increase fur quality and/or calm behavior of an animal.
- a method to induce conformational changes in proteins to reduce their allergenic properties comprises the step of: a) exposing a protein in a solution, having a concentration of about 20% to about 24%, to a pressurization treatment sufficient to induce permanent conformational changes in proteins.
- pressurization treatment is of at least 100 MPa for at least 2 cycles.
- the pressurization treatment is of about 400 MPa for preferably 3 cycles.
- the method in accordance with another embodiment of • the present invention which further comprises a step effected prior to step a) , wherein the protein is solubilized in solution by adding a solubilization agent or by storing the protein solution at about 4°C for at least 2 hours.
- the protein during the pressurization treatment is at a temperature ranging from 0 to 80°C, preferably at 20°C.
- the following terms are defined below.
- protein is intended to mean any food or physiological proteins.
- food protein is intended to mean protein which is usually fed to humans and animals, including, without limitation, whey, caseins, soy, legume, egg, such as egg albumin, peanut, nut, milk, fish and meat proteins.
- physiological protein is intended to mean any physiological proteins found in body fluids of animals, including without limitation human and animal blood proteins, such as Human Serum Albumin (HAS) , and hormones .
- HAS Human Serum Albumin
- body fluids is intended to mean any physiological fluid including, without limitation, saliva, plasma and blood.
- animal is intended to mean human,, mammal, bird, amphibian, fish, reptile and insect.
- pressurization sufficient to induce permanent conformational change in protein mainly consists in repeated cycles of pressure or equivalent treatment.
- Fig. 1 illustrates food intake and weight gain in weanling rats following intake of native or pressurized whey proteins after 17 and 35 days;
- Fig. 2 illustrates the feed efficiency and protein efficiency ratios in Weanling rats following intake of native or pressurized whey proteins after 17 and 35 days;
- Fig. 3 illustrates serum levels of thiobarbituric acid reactive substances in Weanling rats following intake of native or pressurized whey proteins after 17 and 35 days;
- Fig. 4 illustrates variations in SH/SS ratio for several pressure treatment of a 3.1% whey protein solution
- Fig. 5 illustrates variations in SH/SS ratio for several pressure treatment of a 12.5% whey protein solution
- Fig. 6 illustrates variations in SH/SS ratio for several pressure treatment of a 25% whey protein solution
- Fig. 7 illustrates variations in SH/SS ratio for several pressure treatment of a 50% whey protein solution
- Fig 8 illustrates SH and SS levels in 3.1% native whey protein solution vs 3.1% pressurized whey protein solution under different cycles and holding time;
- Fig. 9 illustrates SH and SS levels in 12.5% native whey protein solution vs 12.5% pressurized whey protein solution under different cycles and holding time
- Fig. 10 illustrates SH and SS levels in 25% native whey protein solution vs 25% pressurized whey protein solution under different cycles and holding time
- Fig. 11 illustrates SH and SS levels in 50% native whey protein solution vs 50% pressurized whey protein solution under different cycles and holding time;
- Fig. 12 illustrates the ratio of reduced glutathione (GSH) to oxidized glutathione (GSSG) in rat hepatic tissue after 35-day feeding trial;
- Fig. 13 illustrates the ratio of reduces glutathione (GSH) to oxidized glutathione (GSSG) in rat hepatic tissue after 17-day feeding trial
- Fig. 14 illustrates the reduced glutathione concentrations in rat hepatic tissue after 17-day feeding trial
- Fig. 15 illustrates the reduced glutathione concentrations in rat hepatic tissue after 35-day feeding trial
- Fig. 16 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 1-4) and pressurized whey for 17 days
- Fig. 17 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 5-8) and pressurized whey for 17 days;
- Fig. 18 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 1-5) and pressurized whey (rats # 1-3) for 35 days;
- Fig. 19 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 6-8) and pressurized whey (rats # 4-8) for 35 days;
- Fig. 20 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 1-4) and pressurized whey (rats # 1-5) for 17 days;
- Fig. 21 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 5-8) and pressurized whey (rats # 6-9) for 17 days;
- Fig. 22 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 1-5) and pressurized whey (rats # 1-4) for 35 days;
- Fig. 23 illustrates the Western Blot Analysis of IgG-Mediated Antigenicity of Plasma proteins from rats fed native whey (rats # 6-9) and pressurized whey (rats # 5-9) for 35 days; and
- Fig. 24 illustrates the Fourier Transform Infrared (FTIR) Deconvolution Spectroscopic Data of a native 20% whey protein isolate solution before and after exposure to different applied modes of pressure at 400 MPa.
- FTIR Fourier Transform Infrared
- the weight gain, glutathione inducing effect and antioxidant findings in the animals were unexpected and unique. Also, the Applicants have developed a new type of processing using pressurization in conjugation with holding time and recycle of the pressure to enable the use of lower pressures to impact upon the secondary structure protein molecules in a greater magnitude than was observed via earlier work on whey proteins using a single application of pressure at a range of high- pressure treatments up to 1200 MPa.
- pressurization decreases the disulfide content of whey proteins while concurrently increasing the free sulfhydryl content of the proteins. This would suggest that pressurization could increase the bioavailability of sulfur amino acids towards glutathione synthesis by breaking the disulfide bonds. In this manner, pressurization of whey proteins could increase their digestibility to allow for an enhanced generation of small bioactive peptides such as ⁇ -glutamylcysteine that allow for a more rapid intracellular uptake of cysteine. This approach differs dramatically from earlier descriptions on the scientific literature and earlier patents that describe the importance of preserving whey proteins on their undenatured state in order to maintain the integrity.
- the new pressurization approach involved a high pressure machine which could produce pressures only as high as 400 MPa but gave large volumes (2 liters) .
- the technique allowed for a greater impact on the protein molecule's secondary structure than was observed in earlier studies using 1000-1200 MPa pressure.
- This approach would allow pressurization to be readily used on an industrial scale whereas the pressures involved in earlier work could not be readily transferred to an industrial scale due to the enormous pressures involved (1000-1200 MPa) .
- Protein concentrations and pressure treatment were optimized using the unique approach of: (Astwood, J.D. et al., Na ture Biotech 1996; 1269-1274) exposing the protein to recycles pressure; and (Baruchel, S., Viau, G. Anticancer Res . 1996; 16:1095-1100) holding the protein under pressure for an extended period of time to obtain the maximal changes in secondary structure in the amide I area as detected by FTIR spectroscopy .
- whey protein isolate solutions were formulated to contain a concentration of 25-40% protein and were stored at 4°C for 12 hours before being subjected to pressure treatment. Whey protein isolates were exposed to 400 MPa for 3 cycles ' with 10 minutes of holding time at 400 MPa.
- the samples were kept at a constant temperature of 20 °C during the pressure treatments although the method of pulse pressurization described in the present application can be carried out on proteins in solution using a wide range of temperatures (i.e. 0 to 80 °C) . Alternatively, to exert the same effect, an application of 6 cycles plus 3 minutes holding time also can be used.
- the proteins were added as 24% protein (w/w) in semi-purified diets and fed to 21 day-old newly weaned Sprague Dawley rats. Rats were fed either pressurized and unpressurized whey protein for either 17 or 35 days. Semi-purified diets were formulated according to the NRC requirements for the rat (National Research Council (1995) 4 th rev.
- the protein isolate solutions were formulated to contain a concentration of 25% protein.
- a significant lowering of plasma concentrations of an index of oxidative stress, thiobarbituric acid reactive substances (TBARS) was also observed with the group of rats fed the pressurized whey protein (Fig. 3) .
- the animals fed the pressurized whey were also observed to be calmer and had better general appearance including a thicker fur.
- the animals fed the pressure-treated .whey were more manageable, had more linear growth and showed no increase in adipose tissue despite their increased body weight.
- the tissues were observed to be redder in color in the pressurized treated rats, further suggesting a generalized antioxidative effect of tissues due to the preservation of hemoglobin from air oxidation.
- Western blotting was employed for the detection of antibodies of the native and pressurized whey protein to assess the antigenicity of the both proteins in the serum of the newly weaned rats, which were fed native and mixed mode pressurized whey as dietary protein for 17 and 35 days.
- Plasma proteins of the both group of the rats on the two diets for the two period of time were treated with sample loading buffer (SDS Reducing Buffer) at pH 6.8 and 5% ⁇ -mercaptoethanol and were heated at 95°C for 4 min.
- the treated samples were loaded to SDS-PAGE gels in Mini-protean II Electrophoresis System, using 4-15%, 10 wells ready gel.
- An electrode running buffer pH 8.3 containing 1% SDS was used to separate the proteins at a voltage of 110 and 62 mA current for 50-60 min for two gels. After the electrophoretic separation, the separated proteins were transferred to a nitrocellulose paper using transfer buffer at a pH of 8.3 at a voltage of 121 and 250 mA at the beginning to increase to 300 mA during 1 hour at the end of the transfer time. Immunodetection was carried out with peroxidase-conjugated affinity pure goat anti-rat IgG (H+L) from Jackson Immuno- Research (Cat . #112-035-062) in a dilution of 1:400.
- FIG. 24 A 20% solution of the whey protein isolate was exposed to different pressure cycles (Fig. 24) .
- Our hyperbaric-Fourier transform infrared (FTIR) deconvolution spectroscopic data show that our novel pressurization technique induced an irreversible major broadening in the Amide I area of the secondary structure of whey proteins, which is the result of a complete unfolding of the proteins (Fig. 24) .
- Figure 24 demonstrates that, in comparison to native whey protein, the exposure of the proteins to 1 cycle of pressure at 400 MPa did not change the structure of the molecule although a reduction in the intensity of the amide I bands (1600 - 1700 cm -1 ) was observed as a function of pressure due to the reduction of volume of the molecules.
- the present patent application shows for the first time a method by which protein structure can be irreversibly denatured, particularly in terms of disulphide bond breakage. Based on our chemical studies we have shown that pressurization alters the conformation of whey proteins such that the disulphide bonds are decreased concurrent with an increase with free sulfhydryl groups . Highly allergenic proteins such as ⁇ -lactoglobulin have a high disulphide content, which increases the resistance of the protein to digestion. The presence of disulfide bonds is also related to the allergenic properties of food proteins.
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Abstract
L'invention concerne la pressurisation hyperbare de protéines et des utilisations thérapeutiques de ces protéines pressurisées comme agents de stimulation de croissance et/ou antioxydants et/ou glutathions de tissus. Il est prévu une composition de protéine ayant une susceptibilité accrue aux enzymes pour l'administration à un animal, comprenant entre 1 % (m/m) et 100 % (m/m) d'une protéine préparée suivant le procédé de l'invention ; et un support pharmaceutiquement acceptable compris entre 0 % (m/m) et 99 % (m/m). L'invention concerne également des moyens permettant de provoquer des changements conformationnels dans des protéines en vue de réduire leurs propriétés allergènes, en soumettant ces protéines à un traitement hyperbare. L'invention permet d'obtenir une composition de protéine ayant des effets allergènes réduits pour l'administration à un animal, renfermant entre 1 % (m/m) et 100 % (m/m) d'une protéine préparée conformément au procédé de l'invention ; et un support pharmaceutiquement acceptable compris entre 0 % (m/m) et 99 % (m/m).
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
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US17537800P | 2000-01-11 | 2000-01-11 | |
US175378P | 2000-01-11 | ||
US25259200P | 2000-11-24 | 2000-11-24 | |
US252592P | 2000-11-24 | ||
PCT/CA2001/000031 WO2001050888A1 (fr) | 2000-01-11 | 2001-01-10 | Pressurisation hyperbare de proteines et utilisations therapeutiques des proteines ainsi pressurisees |
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EP01901095A Withdrawn EP1248534A1 (fr) | 2000-01-11 | 2001-01-10 | Pressurisation hyperbare de proteines et utilisations therapeutiques des proteines ainsi pressurisees |
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EP (1) | EP1248534A1 (fr) |
AU (1) | AU2001226606A1 (fr) |
CA (1) | CA2396103A1 (fr) |
WO (1) | WO2001050888A1 (fr) |
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WO2005067731A1 (fr) * | 2004-01-20 | 2005-07-28 | Technion Research & Development Foundation Ltd. | Procede et appareil pour reduire l'activite allergene |
US20080166466A1 (en) * | 2005-03-08 | 2008-07-10 | Fonterra-Co-Operative Group Limited | High Pressure Processing of Metal Ion Lactoferrin |
US20070092632A1 (en) * | 2005-10-21 | 2007-04-26 | Stan Kubow | Ultra high pressure modified proteins and uses thereof |
FR2986401B1 (fr) * | 2012-02-02 | 2014-03-07 | Financ Cormouls Houles Soc | Procede de preparation d'un aliment hypoallergenique |
-
2001
- 2001-01-10 CA CA002396103A patent/CA2396103A1/fr not_active Abandoned
- 2001-01-10 WO PCT/CA2001/000031 patent/WO2001050888A1/fr not_active Application Discontinuation
- 2001-01-10 AU AU2001226606A patent/AU2001226606A1/en not_active Abandoned
- 2001-01-10 EP EP01901095A patent/EP1248534A1/fr not_active Withdrawn
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