Institut National De La Recherche Agronomique

Piere Jouan Biotechnologies S.a.

Jacques Fauquant

Michel Piot

Gerard Brule

Loic Roger

Jean-Louis Joseph Maubois

Henri Y M Goudedranche

Pierre Jouan

Michel Bourtourault

Benoît Robert

Christelle Lopez

Roger Loic

The present invention relates to a treatment method for reducing the bacterial content of a food and/or biological medium of interest containing lipid droplets, which method comprises the following steps: (a) a step of homogenization applied to said medium of interest, (b) a step of microfiltration applied to said homogenized medium of interest resulting from step (a), on a membrane having a cut-off threshold which allows at least some of said lipid droplets to penetrate into the permeate, while at the same time retaining at least some of said bacteria in the retentate, and (c) the recovery of said permeate resulting from step (b), constituting a homogenized food and/or biological medium in which the bacterial content is lower than in the medium before the implementation of said method. The method according to the invention is characterized in that:&#x2014;firstly, said homogenization step (a) comprises at least two successive homogenization operations applied to said medium of interest, said homogenization operations each resulting in a reduction in the size of said lipid droplets, and&#x2014;secondly, said microfiltration step (b) consists of a tangential microfiltration process.

Method for reducing the bacterial content of a food medium containing lipid droplets

The invention concerns a method for obtaining a highly enriched TGF-beta protein fraction in activated form, from a liquid solution rich in proteins said to be soluble in the aqueous phase of milk and/or of whey, said method comprising the following steps; a) adjusting soluble proteins purified at a concentration between 5 and 30 g/liter of solution; b) precipitating part of the whey proteins by acidic treatment of the solution thus obtained to a pH ranging between 4 and 5.5 and at a temperature ranging between 55&#xb0; C. and 68&#xb0; C.; c) carrying out a microfiltration of the treated solution by diafiltration, so as to obtain respectively a microfiltration retentate and a microfiltrate; d) recuperating the microfiltration retentate containing the protein fraction highly enriched in TGF-beta; e) drying the microfiltration retentate which has been subjected to diafiltration to obtain a powder highly enriched in TGF-beta.

Method for obtaining a TGF-beta enriched protein fraction in activated form, protein fraction and therapeutic applications

Dairy product having a total fats content lower than or equal to 400 g/kg and the fat globule distribution of which is such that globules of lower diameter than 2.0 &mgr;m represent 10% to 60%, preferably 20% to 40%, in weight of the total fats, and the fat globules of higher diameter than to 6 &mgr;m represent 10% to 30%, preferably 15% to 20%, in weight of the total fats useful for converting milk into cheese or yogurt, light creams or consumption milks.

Products, in particular, milk products, comprising selected fractions of fat globules, method for obtaining same and uses

The invention concerns a method for selectively separating, according to size, fat globules present in food or biological medium, which consists in subjecting the medium to be treated to at least tangential flow microfiltration with a cut-point threshold ranging between 1.8 and 10 &mgr;m in substantially uniform transmembrane differential pressure and in recuperating the resulting concentrate and permeate.

Method for obtaining milk products containing selected fractions of fat globules

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.

Nutrient composition containing non-phosphorylated peptides from case in

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. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.

Nutrient composition containing non-phosphorylated peptides from

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.

Non-phosphorylated peptides from casein-based material

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.

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.

Casein phosphopeptide salts

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.

Phosphopeptides from casein-based raw material

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.

Casein phosphopeptide composition

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.

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.

Phosphopeptides from casein-based material

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.

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.

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Monfort, France

Jacques Fauquant