Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Patent
1991-07-08
1992-05-12
Lee, Lester L.
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
435 681, 530343, 530407, 530833, C07K 710
Patent
active
051128128
DESCRIPTION:
BRIEF SUMMARY
The present invention concerns a peptide preparation from hydrolysis of whey, a process for producing it by ultrafiltration and hydrolysis of whey as well as use of the peptide preparation as a substitute for milk or milk protein.
In the population there are increasing problems with allergy, i.e. milk allergy, just as there are some people who cannot absorb lactose. The problems are particularly great in case of infants, since milk and milk products constitute a significant proportion of their nutrition if they are not breast-fed for some reason.
It has been attempted to produce mother's milk substitutes from e.g. whey by a combination of enzymatic hydrolysis, heat treatment and ultrafiltration, cf., the U.S. Pat. No. 4,293,571. The peptides obtained hereby have a size of 1,000-10,000 Dalton. However, it is well-known that peptides of 5,000-10,000 Dalton are often allergenic, see e.g. Immunochemistry, Pergamon Press 1967, 4, p. 1-10.
The process described in the mentioned U.S. patent comprises denaturation of the proteins, which is performed by a heat treatment, e.g. at 100.degree.-140.degree. C. for from 10 seconds to 4 minutes or at 75.degree.-100.degree. C. for 2-60 minutes. Such a strong denaturation involves a great risk of destruction of sulfur-containing amino acids, formation of Maillard reaction products which are often allergenic (hapten effect), just as the taste of the product is impaired. See e.g. Otani, H. and Tokita, F., Jap. J. Zootechn. Sci., 1982, 53, p. 344, Otani et al., Jap. J. Zootechn. Sci., 1985, 56, p. 987 and Matouda, T. et al., J. Food Sci., 1985, 50 p. 618.
It has now been found that if a whey-based peptide preparation comprising peptides with a molecular weight of up to 6,000 Dalton is provided, it may be incorporated as a component in food products and stimulants for allergics. The preparation is useful in mother's milk substitutes for infants as well as in food products and stimulants for persons liable to develop allergy, persons with lactose malabsorption, as a liquid diet for patients having gone through gastric/intestinal surgery, as well as a protein source for athletes, in particular weight lifters, throwers and bodybuilders. It is useful in stimulants such as ice and protein beverages.
Thus, the preparation of the invention is characterized by comprising peptides with a molecular weight of up to 6,000 Dalton and by being free of allergenic substances, such as Maillard reaction products and lactose.
A particularly preferred peptide preparation is characterized by substantially consisting of peptides with a molecular weight of 2,000-6,000 Dalton, in particular 2,000-2,500 Dalton, since small molecules, such as free amino acids and salts tend to cause diarrhoea because of their osmotic effect, which is undesirable of course.
The invention also concerns a process for producing the present peptide, which is characterized by
a) diafiltrating essentially casein-free whey with water on an about 20,000 Dalton membrane, if desired after a preceding concentration of the whey,
b) enzymatically hydrolyzing the whey protein retentate from a) in one or more steps, each hydrolysis step being terminated with ultrafiltration through an about 6,000 Dalton membrane to harvest the resulting peptides in the permeate.
If the whey as a starting material is not essentially casein-free, it must, prior to performing the process of the invention, be subjected to coarse filtration, centrifugation or other treatment for removal of casein residues which may perhaps be present as complexes. The whey is expediently purified on a 200,000 Dalton membrane, i.e. a membrane with a cut-off value of 200,000 Dalton, or by a pH adjustment to about 4.6 and addition of a precipitant, preferably calcium chloride. Any membrane with the desired cut-off value may be used here and throughout the description and claims. Usually, commercially available membranes are preferred, produced from high-resistant synthetic polymers which are also useful for clean-in place, CIP cleaning, i.e. cleaning on site, with e.g. acid an
REFERENCES:
patent: 4107334 (1978-08-01), Jolly
patent: 4293571 (1981-10-01), Olofsson et al.
Liu, C. et al, "Immunochemical Studies of the Tryptic, Chymotryptic and Peptic Peptides of Heat Denatured Bovine Serum Albumin", Immunochemistry, Pergamon Press 1967, vol. 4, pp. 1-10.
Otani, H. et al, "Studies on the Antigenicity of the Browning Product between .beta.-Lactoglobulin and Lactose: Antigenic Activities of Peptides Obtained by Cleavage at Arginine Peptide Bonds in Regions 25-107 and 108-145", Jpn. J. Zootech. Sci., 56 (12): pp. 987-993.
Otani, H. et al, "Contribution of the Sugar Moiety in the Browning Product between .beta.-Lactoglobulin and Lactose as an Antigenic Determinant", Jpn. J. Zootech. Sci., 53 (5): pp. 344-350.
Matsuda, T. et al, "Immunochemical Properties of Proteins Glycosylated Through Maillard Reaction: .beta.-Lactoglobulin-Lactose and Ovalbumin-Glucose Systems", Journal of Food Science, vol. 50 (1985), pp. 618-621.
Poulsen Otto M.
Samuelsson Ernst-Gunnar
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