Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide
Patent
1986-09-17
1990-04-17
Richman, Barry S.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Enzymatic production of a protein or polypeptide
514 7, 514 76, 514773, 514774, 514825, 514913, C12P 2106, A23J 300
Patent
active
049180088
DESCRIPTION:
BRIEF SUMMARY
The invention concerns a protein hydrolysate obtained from whey protein, lactalbumin, .alpha.-lactalbumin, lactoferrin, .beta.-lactoglobulin, lysozyme or serum albumin, a process for the preparation of this hydrolysate and its application for pharmaceutical purposes.
It is known that the proteins of milk consist of caseins and whey proteins. In addition the proteose-peptones with a proportion of the total nitrogen content of cow's milk of approximately 5% may be included in the proteins. The proportion of casein in the total protein content of cow's milk is about 80% and that of the whey proteins about 20%. The caseins represent some of the most intensively researched proteins. In contrast to the original assumptions, they are not uniform bodies. Several fractions have been distinguished to date. However, it is typical of all caseins that they contain phosphorus. They are much more complex and have a much higher molecular weight than the so-called whey proteins. At the present time it is known that they consist of .beta.-lactoglobulin, .alpha.-lactalbumin, serum albumin and immunoglobulin.
Investigations by Brantl and Teschemacher (Milchwissenschaft 37, pages 641-644, 1982) showed that opiate-like acting substances may be isolated from the casein fraction of cattle milk. Beginning with commecially available casein-peptone, these authors prepared a 65:35 (v/v) chloroform methanol extract, prepurified it on active carbon and XAD-2-polystyrene resin and further purified it with HPLC. The opiate activity of the material obtained in each case was determined on guinea pig ileum preparations and the enrichment and purification quantatively observed in this manner. The opiate effect was attributed to a heptapeptide and its fragments shortened at the C terminal by one or several amino acid radicals.
It is the object of the invention to prepare further pharmaceutically usable components from certain other proteins.
It was discovered surprisingly that beginning with whey proteins, lactalbumin, .alpha.-lactalbumin, lactoferrin, .beta.-lactoglobulin, lysozyme or serum albumin decomposition products may be obtained, which have surprising pharmacological effects.
In particular decomposition products of lactalbumin, .alpha.-lactalbumin, .beta.-lactoglobulin, lactoferrin or the mixture of all whey proteins and of denaturated lysozyme, show surprising pharmacological effects. In view of the aforementioned investigations, it has been believed that pharmacologically effective components of milk occur only in the casein fraction. Lysozyme resembles lactalbumin in its structure. In the two proteins, 51 amino acids are arranged identically and 24 in a similar manner. Lysozyme is present in small amounts in cow's milk and in larger proportions in egg protein and in mucous membranes.
The protein hydrolysate according to the invention may be obtained by preparing an approximately 1 to 10 weight % aqueous suspension of whey protein, lactalbumin, lactoferrin, .alpha.-lactalbumin, .beta.-lactoglobumin, lysozyme or serum albumin, treating the suspension at 35 to 38.degree. C. under agitation with at least one protease and optionally a lipase, continuing said treatment at approximately 60.degree. C. for several hours, heating the suspension to 80 to 90.degree. C., let it stand at this temperature for a short period of time, allow it to cool, concentrating it under a reduced pressure and isolating the residue as product (A); extracting the residue with a polar solvent or mixture of solvents at room temperature or a slightly elevated temperature, filtering it and obtaining from the filtrate by evaporation to dryness the product (AP).
Advantageously, a 2 to 5% by weight suspension of the initial material in water is used.
The treatment is carried out preferably at 35 to 38.degree. C. over approximately 1 to 4 h, advantageously about 2 h, and the elevated temperature of approximately 60.degree. C. is advantageously maintained for about 2 to 3 h.
As the polar solvent, preferably ethanol, chloroform or isopropanol and as the mixture of polar
Richman Barry S.
Wallen T. J.
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