WO1996012730A1 - Separation d'acides amines et de peptides a partir d'hydrolysats proteiques - Google Patents

Separation d'acides amines et de peptides a partir d'hydrolysats proteiques Download PDF

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Publication number
WO1996012730A1
WO1996012730A1 PCT/NZ1995/000107 NZ9500107W WO9612730A1 WO 1996012730 A1 WO1996012730 A1 WO 1996012730A1 NZ 9500107 W NZ9500107 W NZ 9500107W WO 9612730 A1 WO9612730 A1 WO 9612730A1
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WO
WIPO (PCT)
Prior art keywords
resin
anion exchange
amino acids
peptides
protein
Prior art date
Application number
PCT/NZ1995/000107
Other languages
English (en)
Inventor
Roger Anthony Stanley
Dawn Marie Scott
Elizabeth Emma Doolin
Original Assignee
Industrial Research Limited
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 Industrial Research Limited filed Critical Industrial Research Limited
Priority to AU38180/95A priority Critical patent/AU3818095A/en
Publication of WO1996012730A1 publication Critical patent/WO1996012730A1/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4732—Casein
    • 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
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • 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
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • A23J3/343—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy proteins
    • A23J3/344—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy proteins of casein
    • 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
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
    • A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
    • A23L5/27—Removal of unwanted matter, e.g. deodorisation or detoxification by chemical treatment, by adsorption or by absorption
    • A23L5/273—Removal of unwanted matter, e.g. deodorisation or detoxification by chemical treatment, by adsorption or by absorption using adsorption or absorption agents, resins, synthetic polymers, or ion exchangers
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
    • B01J41/00—Anion exchange; Use of material as anion exchangers; Treatment of material for improving the anion exchange properties
    • B01J41/04—Processes using organic exchangers
    • B01J41/07—Processes using organic exchangers in the weakly basic form
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14—Extraction; Separation; Purification
    • C07K1/16—Extraction; Separation; Purification by chromatography
    • C07K1/18—Ion-exchange chromatography
    • 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 a method of separating amino acids and peptides from protein hydroiysates.
  • the invention relates to the removal of hydrophobic amino acids
  • Hydroiysates are produced by enzymatic cleavage of proteins to manufacture products with
  • hydroiysates of casein, whey and soy proteins are produced commercially.
  • Such hydroiysates are desirable products for use with both humans and animals.
  • such hydroiysates are useful when the subject has digestive problems such as an incapability to break down whole proteins in the digestive tract.
  • the action of the enzymes during the hydrolysis process causes the release of hydrophobic peptides which are perceived as bitter.
  • the maximum level of incorporation of such hydroiysates is limited by the bitter taste. Therefore for oral administration, it is desirable that the amount of these compounds in the product be lowered to achieve an acceptable taste.
  • bitter hydrophobic peptides can be lowered in concentration or removed by the use of adsorbents such as activated carbon, or synthetic resins such as XAD4 and XAD7 (Rohm and Haas) or HP20 and HP21 (Mitsubishi Kasei Corporation) where the base matrix is composed of a polymer with hydrophobic properties such as styrene-divinyl benzene, acrylate or methacrylate.
  • adsorbents such as activated carbon, or synthetic resins such as XAD4 and XAD7 (Rohm and Haas) or HP20 and HP21 (Mitsubishi Kasei Corporation) where the base matrix is composed of a polymer with hydrophobic properties such as styrene-divinyl benzene, acrylate or methacrylate.
  • Japanese Patent 59-159792 to Meiji Confectionary KK entitled "Manufacture of Casein Phosphopeptide” is directed to a new method of manufacture of Casein Phosphopeptide via the hydrolysis of casein by trypsin.
  • the bitter taste, which is caused by the presence of peptides in the trypsin hydrolysate is removed by the use of activated carbon or cation exchange resins.
  • Anion exchange resins are disclosed as being unsuitable for use in the removal of the bitter peptides from the mixture.
  • the patent discloses the reclaiming of the column through the suitable treatment with acid/alkali or by calcination regeneration.
  • the invention in a first aspect comprises a method for separating hydrophobic amino acids and peptides containing aromatic groups from protein hydroiysates using anion exchange media.
  • the invention further comprises a method for separating hydrophobic amino acids and peptides containing aromatic groups from a mixture of protein hydroiysates comprising:
  • the hydrophobic peptides separated from the protein hydroiysates contain one or more amino acid unit(s) with an aromatic group.
  • the anion exchange resin is a hydrophobic base matrix with a weak base ion- exchange functionality.
  • the weak base ion-exchange functionality has a pK a or pK a 's in the pH range of substantially 2.0 to substantially 9.0, more preferably between 2.0 and 6.0.
  • the ion-exchange resin is regenerated by removing the bound amino acids and peptides from the ion exchange resin using a combination of low pH and high temperature.
  • the pH at which the resin is used to bind the amino acids and peptides is greater than the pH required to completely ionise the weak base functionality.
  • this pH is between substantially 4.0 to substantially 9.0 and more preferably between 6.5 and 8.0.
  • the pH used to remove the bound compounds from the ion exchange resin is sufficiently low to create an ionised form of the weak base functionality.
  • this is between substantially 1.5 and substantially 6.0 and more preferably between substantially 1.5 and substantially 4.0.
  • the temperature used in the regeneration of the ion exchange resin is between substantially 45°C and 100°C, more preferably between substantially 50°C and substantially 100°C, and most preferably between substantially 60°C and substantially 80°C.
  • the protein hydroiysates are derived from animal products or plants.
  • the protein hydroiysates are hydroiysates of casein, whey, or soy protein.
  • the invention further comprises a process for the separation of hydrophobic amino acids and proteins containing aromatic groups from protein hydroiysates using a hydrophobic anion exchange resin with a weak base functionality comprising the steps of:
  • the invention is directed to the separation of hydrophobic amino acids and peptides containing aromatic groups from protein hydrolysate mixtures using anion exchange media.
  • ion exchange resins generally have not been thought to be suitable for use in large scale separation processes for this purpose as it was thought that sufficient selectivity of binding the compounds of concern to the surface of the resins did not exist for practical industrial production purposes.
  • anion exchangers with a weak base functionality and hydrophobic base matrix at a substantially neutral pH will bind hydrophobic amino acids and peptides containing aromatic groups to the surface of the resin and thus remove them from the hydrolysate mix (an adsorption stage).
  • the types of amino acids and peptides that can be selectively removed are in general terms the hydrophobic amino acids and peptides containing aromatic groups. Such compounds include phenylalanine, tyrosine, tryptophan and peptides thereof as well as others as are well known in the art. When used in the dairy industry, this separation method can be advantageously used to de-bitter hydroiysates of casein or whey for example. The bitter taste caused by combinations of amino acids having hydrophobic end groups can be removed if
  • hydrophobic base matrices (1) hydrophobic base matrices
  • the ion-exchangers useful in the process of the invention are generally comprised of a weak base group such as a primary, secondary or tertiary amine with a pK, or pK s in the range of pH 2.0 to pH 9.0 that are attached to a particulate matrix with hydrophobic character such
  • Anion exchange resins are subtantially neutral in charge when the pH of the equilibrating solution is above the pK a of the base ligand.
  • the preferred anion exchange resins are those with weak base ion-exchange groups that are substantially neutral at neutral pH. The more the equilibrating pH is above the pK a of the weak anion exchange resin, the lower the density of charged groups on the surface of the resin.
  • the preferred resins for this invention are substantially neutral, enhancing the interaction between the hydrophobic amino acids and peptides and the resin.
  • the pH range can be as wide as pH 4.0 to pH 9.0 depending on requirements as will be known in the art. More neutral pH's between substantially 6.5 and 8.0 are however preferred.
  • Suitable resins will have all the above properties.
  • Exemplary commercial resins include: Relite A329 from Sybron/Relite, which is the best of the surveyed resins. Others, such as Purolite A 103, Purolite A 100 (Purolite International), Amberlite IRA93SP (Rohm and Haas), Dowex MWA1 (Dow Chemical Company) are also suitable, but are not as effective as Relite A329 because their binding capacities are less.
  • Other suitable resins as will be known in the art may also be used.
  • the process of the invention includes the ability to regenerate the anion exchange resin. This relies on the ability to alter the surface charge of the resin, and thus the hydrophobicity and strength of adsorption of the hydrophobic substances onto the resin. This is achieved by lowering the pH of the solution to substantially lower than the pK avail of the ion-exchange groups on the resin. This induces charged groups on the resin surface thus releasing the bound substances.
  • the resin used in the process of the present invention can therefore be regenerated by lowering the pH surrounding the resin, preferably at high temperature, causing the amino acids and peptides to unbind from the resin surface thus regenerating the resin for further use (a regeneration step).
  • the pH can be lowered by the use of any suitable acid or buffer (eg HC1,
  • the pH is lowered to between substantially 1.5 to 6.0 although a pH between 1.5 and 4.0 is considered most suitable.
  • a temperature of between 45°C and 100°C enhances the regeneration step. This may be achieved by the use of hot water or the like as will again be known in the art. Temperatures between 50°C and 100°C are preferred with temperatures between 60°C and 80°C being considered most suitable.
  • the hydrophobic ion-exchangers with weak base functionality have been substituted for conventional non-ion exchange adsorbents with the amino acids binding to the ion- exchanger in the uncharged form (ie at the substantially neutral pH). A shift to lower pH to
  • the process of the present invention can be carried out with resins that have an established history and acceptability of use in food processes. Moreover, the resins can be readily regenerated for reuse without the application of strong caustic, acids or toxic solvents, again giving better acceptability in food applications for example.
  • the present invention requires only sufficient acid to alter the charge on the anion exchange resin to result in release of the bound substances. It does not require excessive amounts of acids that may be recommended to clean ion exchange media on an empirical basis. In conventional ion exchange processes anion exchange resins are regenerated by the use of strong alkali. While the method of the present invention operates preferentially at low temperatures for the adsorption stage and at high temperatures for elution (ie the regeneration step), the process will be carried out with resins that have an established history and acceptability of use in food processes. Moreover, the resins can be readily regenerated for reuse without the application of strong caustic, acids or toxic solvents, again giving better acceptability in food applications for example.
  • the present invention requires only sufficient acid to
  • ion exchange resins do not easily foul with large molecules because the charge on the resin covers most of the surface and only smaller molecules, such as the smaller peptides, will be able to bind in the spaces between the charges on the resin surface;
  • the ion exchangers can be operated in the neutral range and not in the hydroxide form eliminating base catalysed amino acid degradation which allows the recovery of the bound amino acids for potential later use.
  • the process is carried out by first washing the ion-exchanger according to manufacturer's recommendation and then washing in the presence of a salt (e.g. NaCl or the like).
  • a salt e.g. NaCl or the like.
  • the ion-exchanger is then washed with buffer or water to achieve the desired pH for adsorption of amino acids and peptides, which is above the pK a of the weak base ligands
  • the adsorption step be carried out at low temperature to promote adsorption of the hydrophobic amino acids, and that the regeneration be carried out at high temperature to facilitate elution of the hydrophobic amino acids.
  • the resins can be washed with water and re-used without further equilibration if the "irocess
  • hydrolysate has significant buffering capacity to result in an equilibrium at a substantially neutral pH. If this is not the case, sufficient alkali must be added to achieve this.
  • model bitter substances commonly associated with hydroiysates were used in the following examples.
  • Such substances include L-Tryptophan, an aromatic amino acid with hydrophobic properties, and its derivative L-Tryptophan methyl ester.
  • the carboxylic acid group is derivatised to the non-charged methyl ester form, eliminating any charge effects of this group.
  • Synthetic polymeric resins based on polystyrene and acrylic are more hydrophobic than resins based on agarose, for example.
  • L-Tryptophan (L-Trp) Binding of L-Tryptophan (L-Trp) to a number of synthetic weak and strong anion exchange resins, a synthetic hydrophobic adsorbent, and a hydrophilic weak anion exchange resin was tested as follows. Solutions of L-Trp (0.5% w/v) were prepared in 0.01M potassium phosphate, 0.5M NaCl buffer, pH 7.4, and mixed in batch mode with samples of each of the resins listed in Table 1 (10 mL/g wet resin) at 30°C for 16 hours.
  • Resin Matrix type Resin type L-Tryptophan bound - mg/g wet resin
  • the hydrophobic adsorbent and the eight synthetic weak anion exchange resins bound the greatest amounts of L-Trp with varying efficiencies.
  • the two synthetic strong anion exchange resins and the hydrophilic agarose resin bound very minimal amounts of L-Trp.
  • Relite A329 was washed with 0.5M NaCl for 1 hour, rinsed with distilled water, and then equilibrated into 0.01M potassium phosphate buffer, pH 7.4. Diaion HP20 was equilibrated into 0.01 M potassium phosphate buffer, pH 7.4. L-Tryptophan (L-Trp, 0.5% w/v in 0.01M potassium phosphate buffer, pH 7.4) was mixed with each resin in batch mode (10 mL L- Trp/g wet resin) at 30°C for 2 hours, and then filtered off. The resins were washed with the equilibration buffer. Samples of both resins, bound with L-Trp, were suspended in water and then titrated to the following pH values using either 0.1M HC1 or 0.1 M NaOH as appropriate:
  • Relite A329 and Diaion HP20 were prepared as outlined in Example 2, and L-Trp was again bound to both resins under the conditions described.
  • Half of the resin samples were titrated to pH 4 using 0.1M HC1 and the other half remained at pH 7.4.
  • Resin samples at both pH conditions were mixed at 20°C, 50°C and 70°C for 1 hour.
  • L-Trp released from the resins was removed by filtration and measured by OD at 270 nm.
  • a sample of each resin was suspended in 0.1M NaCl, instead of water, and was mixed at pH 7.4 and 20°C. Again the released L-Trp was measured by OD at 270 nm.
  • Table 3 The results are shown in Table 3.
  • L-Trp from the weak anion exchange resin was achieved with a combination of low pH (pH 4.0) and high temperature (70°C). Release of L-Trp from the adsorbent was significantly improved with increasing temperature, but unaffected by a drop in pH. As in Example 2, a shift in pH to ionise the weak anionic resin, provided a mechanism for release of the hydrophobic amino acid.
  • Relite A329 was treated in the following manner: washed with hot water (70°C), equilibrated in 0.5M NaOH, washed with cold distilled water (20°C), re-equilibrated into 0.5M NaCl and then given a final rinse with distilled water (20°C).
  • L-Tryptophan methyl ester L-Tryptophan methyl ester (L-TrpME, 0.5%w/v in 0.01M potassium phosphate buffer, pH 6.5) were added to 1 gram samples of washed resin and mixed for 1 hour at 20°C. The resin samples were filtered to remove unbound L-TrpME and washed with 0.0 IM potassium phosphate buffer, pH 6.5. A number of eluents were added to the resins and shaken for 1 hour at either 20°C or 80°C (see Table 4). L-TrpME released from the resin samples was removed by filtration and measured by OD at 270 nm against a standard curve of L-TrpME. The pHs of the final soltuions were measured. The results are shown in Table 4 and Figure 3.
  • the resins used in this example were washed in 0.5M NaOH, rinsed with distilled water, and equilibrated into 0.5M NaCl. Prior to use, they were given a final rinse in distilled water. 0.5%w/v solutions of L-TrpME in 0.01M potassium phosphate buffer, pH 6.5, were added to resin samples (lOmL/g wet resin) and mixed for 1 hour at 20°C. The resin samples were filtered to remove unbound L-TrpME, and were washed with buffer.
  • Desorption of the amino acid from the resins was performed by mixing the resin samples with either 0.05M HCl or 0.01 M potassium phosphate buffer, pH 6.5. for 1 hour at either 20°C or
  • the Macronet resins have either no surface charge (MN 200 and MN250) or only low densities of charged groups (MN100 and MN150, 0.4-0.6 mmoles/g dry resin), their regeneration properties at low pH were similar to the adsorbent resin, XAD 16. With Relite A329, 100% desorption of L-TrpME was achieved at low pH because of the much greater charge density of this resin (1.2 mmoles/g dry resin). Optimum desorption of the amino acid was achieved with low pH, high temperature and high density of charges on the resin.
  • the aim of this experiment was to investigate whether the bitter components in the casein and whey hydroiysates, ie the hydrophobic amino acids, di and tri peptides, could be as effectively removed from the hydroiysates using a synthetic weak anion exchange resin, as compared to
  • Relite Casein 1.0 10 0.543 1.990 Acceptable A329 hydrolysate Relite Casein 1.0 50 0.714 2.088 Bitter
  • the weak anion exchange resin (Relite A329) was as effective as the 2 adsorbents at reducing the bitter taste of whey and casein hydroiysates.
  • the capacity of all three resins to remove bitter components was exceeded at a ratio of 5g hydrolysate to lg resin.
  • Relite A 329 was equally as effective as Diaion HP20, but slightly less effective than Diaion HP21, at removing aromatic amino acids from the hydroiysates.
  • amino acids tryptophan, phenylalanine and tyrosine contain aromatic rings, whilst valine, leucine and glycine contain aliphatic straight chains. All of these amino acids, and peptides containing these, except glycine, have hydrophobic properties and hence contribute to the bitter taste of hydroiysates.
  • Relite A329 was washed with 0.5M NaOH and then rinsed with distilled water. The pH of
  • the resin was titrated to pH 7.0 using 0.5M HCl, and then rinsed again with distilled water. Amberlite XAD 16 was used as supplied.
  • Table 8 describes the various adsorbents and resins that have been used in the previous Examples.
  • the table details the name of the manufacturer, the resin type, the trade name of the resin, and the matrix type.
  • Purolite A100 Purolite Weak anion Styrene DVB International exchanger
  • Purolite A 103 Purolite Weak anion Styrene DVB International exchanger

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Nutrition Science (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Polymers & Plastics (AREA)
  • General Chemical & Material Sciences (AREA)
  • Zoology (AREA)
  • Biophysics (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Toxicology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Analytical Chemistry (AREA)
  • Peptides Or Proteins (AREA)

Abstract

Procédé de séparation d'acides aminés hydrophobes et de peptides renfermant des groupes aromatiques, à partir d'hydrolysats protéiques. Le procédé consiste à utiliser des milieux d'échange d'anions ayant un pH sensiblement neutre, et à régénérer les milieux en vue d'une utilisation ultérieure.
PCT/NZ1995/000107 1994-10-20 1995-10-20 Separation d'acides amines et de peptides a partir d'hydrolysats proteiques WO1996012730A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU38180/95A AU3818095A (en) 1994-10-20 1995-10-20 Separation of amino acids and peptides from protein hydrolysates

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Application Number Priority Date Filing Date Title
NZ26474094 1994-10-20
NZ264740 1994-10-20

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Publication Number Publication Date
WO1996012730A1 true WO1996012730A1 (fr) 1996-05-02

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2005047310A1 (fr) * 2003-11-07 2005-05-26 Novexin Limited Procedes de separation

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4075195A (en) * 1976-08-31 1978-02-21 Kraft, Inc. Debittered protein product and method for manufacture
AU7615081A (en) * 1980-10-09 1982-04-22 Hoechst A.G. Alpha amylase inhibitor
AU5510490A (en) * 1984-12-21 1990-10-25 Biogen, Inc. Purification, production and use of tumor necrosis factors
JPH04190797A (ja) * 1990-11-27 1992-07-09 Fuji Oil Co Ltd ペプチド混合物の製造法及びペプチド混合物を含有する飲料
JPH04341193A (ja) * 1991-05-14 1992-11-27 Kanebo Ltd ペプチド又はその塩の取得方法

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4075195A (en) * 1976-08-31 1978-02-21 Kraft, Inc. Debittered protein product and method for manufacture
AU7615081A (en) * 1980-10-09 1982-04-22 Hoechst A.G. Alpha amylase inhibitor
AU5510490A (en) * 1984-12-21 1990-10-25 Biogen, Inc. Purification, production and use of tumor necrosis factors
JPH04190797A (ja) * 1990-11-27 1992-07-09 Fuji Oil Co Ltd ペプチド混合物の製造法及びペプチド混合物を含有する飲料
JPH04341193A (ja) * 1991-05-14 1992-11-27 Kanebo Ltd ペプチド又はその塩の取得方法

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, Volume 114, No. 25, issued 24 June 1991, OHTA, HIDEAKI et al., "Amino-nitrogen Content and Free Amino Acids of Pineapple Juice Deacidified by Means of Ion Exhange Resins", page 655, Abstract No. 246141j; & KINKI CHUGOKU NOGYO KENKYU, 1990, (80), 59-63, (JAPAN). *
DERWENT WPAT ONLINE ABSTRACT, Accession No. 92-280115; & JP,A,04 190 797, (FUJI OIL CO LTD), 9 July 1992. *
DERWENT WPAT ONLINE ABSTRACT, Accession No. 93-13419; & JP,A,04 341 193, (KANEBO LTD), 27 November 1992. *
JOURNAL OF CHROMATOGRAPHY, Vol. 237, issued 1982, DIZDAROGLU M. et al., "Separation of Peptides by High - Performance Liquid Chromatography on a Weak Anion - Exchange Bonded Phase", pages 417-428. *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2005047310A1 (fr) * 2003-11-07 2005-05-26 Novexin Limited Procedes de separation

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