Abstract: Non-phosphorylated peptides and phosphopeptides useful as alimentary products or medicaments are produced by proteolytic enzyme hydrolysis of a casein-based material. Membrane ultrafiltration is used to separate phosphopeptides which are retained by the membrane in a retentate from the non-phosphorylated peptides which pass through the membrane in an ultrafiltrate. The phosphopeptides in the retentate are disaggregated and are subjected to further membrane ultrafiltration where the phosphopeptides pass through the membrane and are separated from the enzyme. The non-phosphorylated peptides have nutritive value and can be used to form compositions for providing nutrition. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Abstract: Non-phosphorylated peptides and phosphopeptides useful as alimentary products or medicaments are produced. A hydrolyzate containing non-phosphorylated peptides and phosphopeptides is prepared by proteolytic enzyme hydrolysis of a casein-based material. The hydrolyzate is subjected to ultrafiltration with a membrane which allows peptides to pass through to produce a permeate containing the non-phosphorylated peptides and phosphopeptides. A bivalent cation-containing salt capable of aggregating the phosphopeptides is added to the permeate to produce a mixture containing phosphopeptide aggregates and non-phosphorylated peptides. The mixture is subjected to ultrafiltration with a membrane that retains the phosphopeptide aggregates and separates them from the non-phosphorylated peptides. The non-phosphorylated peptides have nutritive value and can be used to form compositions for providing nutrition.

Abstract: Nonphosphorylated peptides and phosphopeptides useful as alimentary products or medicaments are produced by proteolytic enzyme hydrolysis of a casein-based material. Membrane ultrafiltration is used to separate phosphopeptides which are retained by the membrane in a retentate from the nonphosphorylated peptides which pass through the membrane in an ultrafiltrate. The phosphopeptides in the retentate are disaggregated and are subjected to further membrane ultrafiltration where the phosphopeptides pass through the membrane and are separated from the enzyme. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Abstract: Non-phosphorylated peptides and phosphopeptides useful as alimentary products or medicaments are produced. A hydrolyzate containing non-phosphorylated peptides and phosphopeptides is prepared by proteolytic enzyme hydrolysis of a casein-based material. The hydrolyzate is subjected to ultrafiltration with a membrane which allows peptides to pass through to produce a permeate containing the non-phosphorylated peptides and phosphopeptides. A bivalent cation-containing salt capable of aggregating the phosphopeptides is added to the permeate to produce a mixture containing phosphopeptide aggregates and non-phosphorylated peptides. The mixture is subjected to ultrafiltration with a membrane that retains the phosphopeptide aggregates and separates them from the non-phosphorylated peptides. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Abstract: Casein phosphopeptide salts of calcium, magnesium or both are produced having less than 4% by weight of aromatic amino acids, greater than 8% and less than 20% by weight serine, less than 3% free amino acid content and a ratio of total calcium, magnesium and phosphorus to total nitrogen greater than 0.2. The phosphopeptides are produced by subjecting a casein material to proteolytic enzyme hydrolysis ultrafiltering the resulting hydrolyzate to produce a permeate containing phosphopeptides, adding a bivalent cation salt to the peptides to form phosphopeptide aggregates and separating by ultrafiltration the phosphopeptide aggregates from non phosphorylated peptides. The phosphopeptides obtained are useful as aliments for dietetic or therapeutic nutrition and as medicines.

Abstract: The method consists in subjecting the raw material (milk or retentate) to enzymatic hydrolysis by means of at least one proteolytic enzyme able to reproduce the proteic digestion occuring in vivo in the human body; recovering the thus obtained hydrolyzate; subjecting the latter to at least one ultrafiltration step on membranes able to retaining the phosphopeptides while letting the peptides pass therethrough, the ultrafiltrate thus containing the non phosphorylated peptides; recovering the ultrafiltration retentate; disaggregating the phosphopeptides in the retentate; and subjecting the latter to at least one further ultrafiltration step on membranes which do not retain the phosphopeptides, these being thus separated from the enzyme and available to be recovered as product. The resulting products are useful as dietetic aliments, therapeutic nutriments or medicaments.

Abstract: A casein phosphopeptide composition is prepared containing less than 4% phenylalanine, tyrosine and tryptophan, greater than 8% and less than 20% serine, a ratio of Ca+Mg+P/N.sub.T greater than 0.2, wherein N.sub.T is the total nitrogen content times 6.38, and free amino acids of less than 3%. The composition is useful as an ailment for dietetic or therapeutic nutrition or as a medicament. Salts of the phosphopeptides may be formed from macroelements such as calcium and/or magnesium and/or from oligoelements such as iron, zinc and copper. The composition is produced by proteolytic enzyme hydrolysis of a casein-based material, and using ultrafiltration and aggregration with a bivalent cation salt to isolate the phosphopeptide composition.

Abstract: Nonphosphorylated peptides and phosphopeptides useful as alimentary products or medicaments are produced by proteolytic enzyme hydrolysis of a casein-based material. Ultrafiltration is used to separate phosphopeptides and nonphosphorylated peptides after hydrolysis. A bivalent cation is added to form aggregates of the phosphopeptides, and the aggregated phosphopeptides are separated from the nonphosphorylated peptides by ultrafiltration. The phosphopeptides form salts, which have dietefic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Abstract: A fluid starting material based on white of egg is subjected to at least one microfiltration by bringing the said material into contact, under pressure and in tangential flow, with a membrane capable of separating off the particles having a size of between about 0.02 micron and 10 microns, giving, firstly, a microfiltrate which passes through the membrane and contains at least a fraction of the lysozyme of the starting material and, secondly, a product held back by the membrane, which retains the natural properties of the starting material based on white of egg but is depleted in lysozyme. The obtained lysozyme can be conventionally used in particular in cheese-making.

Abstract: A process of obtaining an .alpha.-lactalbumin enriched product from whey of various origins is disclosed. A first ultrafiltration is carried out on unpasteurized raw whey with membranes having cut-off greater that 5,000 (e.g. 50,000) at a pH between 6:3 and 7 (e.g. 6.6) and a temperature between 30.degree. and 60.degree. C. thereby retaining whey proteins. The ultrafiltrate then undergoes a second ultrafiltration with a membrane capable of retaining .alpha.-lactalbumin (cut-off about 1,200 and 2,000) which is preferably diafiltration. Depending on whether starting whey is acid whey or sweet whey the resulting product may contain practically no CMP or some (e.g. 25%). The resulting product is useful as a mother's milk substitute, pharmaceutical, intensive care or therapeutic food, or tryptophan enriched nutrient.

Abstract: Phosphopeptides useful as alimentary products or as medicaments are obtained by a method of subjecting phosphocaseinates of monovalent cations or paracasein derived therefrom to enzymatic hydrolysis with at least one proteolytic enzyme that simulates proteic digestion in vivo in the human body, ultrafiltering the resultant hydrolysate with a membrane that retains the enzyme to obtain a permeate containing phosphopeptides and non-phosphorylated peptides, adding to the permeate a bivalent cation salt to form aggregates of the phosphopeptides, subjecting the resultant solution to ultrafiltration with a membrane that retains the phosphopeptide aggregates, and recovering the retained phosphopeptides. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Abstract: A process of obtaining a .alpha.-lactalbumin enriched product from whey of various origins is disclosed. A first ultrafiltration is carried out on unpasteurized raw whey with membranes having cut-off greater than 5,000 (e.g. 50,000) at a pH between 6.3 and 7 (e.g. 6.6) and a temperature between 30.degree. and 60.degree. C. thereby retaining whey proteins. The ultrafiltrate then undergoes a second ultrafiltration with a membrane capable of retaining .alpha.-lactalbumin (cut-off about 1,200 and 2,000) which is preferably diafiltration. Depending on whether starting whey is acid whey or sweet whey the resulting product may contain practically no CMP or some (e.g. 25%). The resulting product is useful as a mother's milk substitute, pharmaceutical, intensive care or therapeutic food, or tryptophan enriched nutrient.

Abstract: A total enzymatic hydrolysate from whey proteins is disclosed comprising peptidic hydrolysate with substantially no residual proteins, at least 50% of the peptides containing 2 to 5 amino acids. 70 to 90% of the nitrogen present as peptides has a number of amino acids less than 10. A process for obtaining the total enyzmatic hydrolysate is disclosed comprising hydrolysis of whey proteins with proteolytic enzyme (e.g. pancreatin), which is continued until there is no precipitable nitrogen with 12% trichloroacetic acid. Enzymatic hydrolysis may be carried out continuously. The total enzymatic hydrolysate has uses as food supplement, diet food or intensive care food, and in therapeutic nutrition.

Abstract: Phosphopeptides useful as dietetic aliments, therapeutic nutriments or medicaments are produced by subjecting phosphocaseinates of bivalent cations to enzymatic hydrolysis with at least one proteolytic enzyme capable of substantially reproducing the proteic digestion which occurs in vivo in the human body to produce a hydrolysate containing phosphopeptides and non-phosphorylated peptides, subjecting the resultant hydrolysate to ultrafiltration to obtain a retentate containing the phosphopeptides and proteolytic enzyme and a permeate containing the non-phosphorylated peptides, disaggregating the phosphopeptides in the retentate and subjecting the resultant retentate containing disaggregated phosphopeptides to ultrafiltration to separate the phosphopeptides from the proteolytic enzyme. Salts of the phosphopeptides, which have dietetic uses, may be formed from macroelements such as calcium and/or magnesium and/or from oligoelements such as iron, zinc and copper.

Abstract: Phosphopeptides useful as alimentary products or as medicaments are obtained by a method of subjecting phosphocaseinates of monovalent cations or paracasein derived therefrom to enzymatic hydrolysis with at least one proteolytic enzyme that simulates proteic digestion in vivo in the human body, ultrafiltering the resultant hydrolysate with a membrane that retains the enzyme to obtain a permeate containing phosphopeptides and non-phosphorylated peptides, adding to the permeate a bivalent cation salt to form aggregates of the phosphopeptides, subjecting the resultant solution to ultrafiltration with a membrane that retains the phosphopeiptide aggregates, and recovering the retained phosphopeptides. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.