Phosphopeptides from casein-based material

Drug – bio-affecting and body treating compositions – Fermentate of unknown chemical structure – Having a known elemental analysis

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260113, 260115, 260119, 424131, 424140, 424144, 424145, 424147, 426 42, 426 56, 426657, 426491, 435 69, 435272, 514 7, A61K 3342, A61K 3324, C07G 700, C12P 2106

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044951760

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.

REFERENCES:
patent: 3974294 (1976-08-01), Schwille et al.
patent: 4172072 (1979-10-01), Ashmead
patent: 4303580 (1981-12-01), Hidalgo et al.
patent: 4358465 (1982-11-01), Brule
West, D. W., A Simple Method for the Isolation of a Phosphopeptide from Borine Alpha.sub.gl -Casein, Journal of Dairy Research, No. 2, vol. 44, 1977, (pp. 373-376).
Roozen et al., Enzymatic Protein Hydrolysis in a Membrane Reactor Related to Taste Properties, Enzyme Microb. Technol., vol. 1, 1979, (pp. 122-124).
Brule et al., Preparation of "Native" Phosphocaseinate by Combining Membrane Ultrafiltration and Ultracentrifugation, J. Dairy Sci., vol. 62, 1979, (pp. 869-875).

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