Peptide mixture and products thereof

Details Peptide mixture and products thereof Peptide mixture and products thereof

1999-05-24

2002-05-28

Borin, Michael (Department: 1631)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Enzymatic production of a protein or polypeptide

C426S583000, C426S657000, C530S343000, C530S407000, C530S833000

Reexamination Certificate

active

06395508

ABSTRACT:

TECHNICAL FIELD
The present invention relates to a whey protein hydrolysate having specific physicochemical properties and a method for producing the same, and in particular to a novel whey protein hydrolysate which as exceptional gastrointestinal absorption properties and amino acid balance, which is effective in preventing and treating food allergies and has antioxidant action, which is palatable, and which can be used in a wide variety of applications, as well as to a method for producing the same.
The present invention also relates to a method in which a peptide mixture containing a specific amount of a free amino acid is produced with consistent quality in a state that is always stable.
The present invention furthermore relates to a method in which a peptide mixture with a low phenylalanine content that can be ingested daily by patients suffering from amino acid metabolic disorder, particularly, phenylketonuria, which is a disease requiring a limited intake of phenylalanine, is produced with consistent quality in a state that is always stable.
In the present specifications, percentages are based on weight, except for transmittance and inhibiting ratios, unless otherwise specified.
BACKGROUND ART
It has recently become clear that, in terms of digestion, oligopeptides have better absorption rates and a better balance of amino acids following absorption than do mixtures of free amino acids (Rakuno Kagaku-Shokuhin no Kenkyu [Dairy Sciences and Food Research], Vol. 39, No. A p. 283 (1990)). It is also clear that there has been a rapid increase in patients suffering from allergies induced by food proteins, and that many allergies caused by whey protein, particularly &bgr;-lactoglobulin, have appeared, particularly in infants (Rakuno Kagaku-Shokuhin no Kenkyu [Daily Sciences and Food Research], Vol. 39, No. A, p. 283 (1990)). There is a need to reduce the antigenicity of whey protein in food products for infants or to essentially remove whey protein antigen from food products for infants.
The hydrolysis of whey protein has been widely adopted as a means for reducing the antigenicity of whey protein in food products for infants or for essentially removing whey protein antigen from food products for infants, but hydrolysates with an extremely low percentage of free amino acids often taste bad, which can cause problems when they are ingested. Hydrolysates of whey protein are also sometimes unstable against heat, resulting in precipitation in a liquid state, browning, and other such disadvantages which have posed problems when conventional hydrolysates are used as oral nutrients and the like.
Preventing oxidation is another major issue when whey protein hydrolysates are used in food products, particularly in fatty foods (such as powder milk prepared for infants, which contains as much as 27% fat per 100 g). That is, the balance between saturated and unsaturated fatty acids is considered from a nutritional standpoint in food products that contain fats, but a drawback is that unsaturated d fatty acids are readily oxidized. DHA and the like which are contained in large amounts in the biological membranes of brain, neural, and retinal tissue and which have recently been believed to play a role in the manifestation of their functions release an extremely strong oxidation odor once they are oxidized, having a markedly adverse effect on product quality, and there is thus a need to prevent their further oxidation.
Ingested amino acids are degraded by transglutaminase, glutamate dehydrogenase, and the like to produce ammonia, but the ammonia thus produced is toxic and must be immediately treated by the liver, so it is essential that no ingested foods contain ammonia.
In this regard, it is extremely important that whey protein hydrolysates contain no ammonia.
In view of the nitrogen equilibrium in mature animals, nitrogen should be ingested in an amount corresponding to the minimum metabolic amount of nitrogen, but nitrogen is ineffective when just given in the form of ammonia, and it must be ingested in the form of essential amino acids. Foods that are ingested must therefore contain the necessary amounts of essential amino acids.
Many methods for producing hydrolysates by the enzymolysis of whey proteins have been developed in view of the nutritional and physiochemical background of the proteins and amino acids described above. Several examples are given below.
1) Whey protein is hydrolyzed either with two enzymes, one being a
Bacillus subtilis
-derived endopeptidase and one being trypsin, or with three enzymes, including a
Bacillus subtillis
-derived endopeptidase, trypsin, and chymotrypsin, to obtain an oligopeptide mixture with a molecular weight of no more than 2,000 daltons, antigen persistence of no more than 10
−4
, and a free acid content of no more than 5% (Japanese Laid-Open Patent Publication 4-248959).
2) Whey protein is hydrolyzed with an alkali protease to obtain a hydrolysate which has at least 75 mol % dipeptides and tripeptides, which has a free amino acid content of less than 5%, which consists of at least four amino acids, and which has less than 20 mol % peptides with an average chain length of 6.2 (Japanese Laid-Open Patent Publication 5-505304).
3) Whey, casein, and soybeans are hydrolyzed with pepsin, trypsin, and chymotrypsin, and ultrafiltration of the product results in an oligopeptide which has a molecular weight of no more than 60,000 daltons and which is 40 to 60% peptides containing 4 to 10 amino acids (Japanese Laid-Open Patent Publication 3-187348).
4) Whey protein is hydrolyzed by thermal denaturation at a pH of 6 to 10 and a temperature of 60 to 80° C., and the enzyme is inactivated by heat to obtain a hydrolysate which has a molecular weight of no more than 10,000 daltons, main peaks of 1,000 to 5,000, an average peptide chain length of 3 to 8, a free amino acid content of no more than 20%, and no more than {fraction (1/10,000)} &bgr;-lactoglobulin antigenicity (Japanese Laid-Open Patent Publication 4-112753).
5) Whey protein is hydrolyzed with trypsin, &agr;-chymotrypsin, and Aspergillus and Bacillus enzymes to obtain a low allergenic peptide with a molecular weight of no more than 10,000 daltons and the capacity to induce oral immunotolerance (Japanese Laid-Open Patent Publication 5-5000).
6) Casein is hydrolyzed with an acidic protease and is hydrolyzed with a neutral peptidase to obtain a peptide with a molecular weight of no more than 3,000 daltons, a free amino acid content of 30 to 55%, no more than 1 in 10,000 parts &agr;
s
-casein in an ELISA inhibition test for &agr;
s
-casein, and a 5% solution bitterness organoleptic value no greater than that corresponding to a 0.04% aqueous solution of caffeine (Japanese Laid-Open Patent Publication 6-113893).
7) A method has been disclosed in which whey is hydrolyzed at a pH of 5 to 11 using a neutral protease (Aspergillus) and then heated at a pH of 2 to 4, and the precipitate is removed to obtain 50% dipeptides and tripeptides (Japanese Patent Publication 5-82412).
Peptide mixtures obtained by the proteolysis of animal proteins (animal milk, eggs, meat, fish, and the like) or vegetable proteins (soybeans, wheat, and the like) are known to have properties such as thickening, foaming, antioxidant, digestive, mineral solubilizing, and low antigenicity properties, as well as epithelial cell growth factor, cell growth factor, calcium absorption promoting function, opioid-like activity, and other such physiologically active functions (Shokuhin to Kaihatsu [Food Products and Development], Vol. 26, No. 11, pp. 28-36 (1991)). They are an indispensable material in the manufacture of meat, fish paste, breads, sweets, mineral fortified food products, infant food products, sports beverages, general health foods, enteric nutrients, food products to combat protein allergies, special nutritional food products, medical drugs, and the like.
Methods for producing the peptide mixtures used in the manufacture of these food products and medical drugs vary, depending on the application, and

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