Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2000-09-20
2002-01-22
Davenport, Avis M. (Department: 1653)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S012200, C530S359000, C530S300000, C530S350000, C530S345000
Reexamination Certificate
active
06340669
ABSTRACT:
The present invention relates to a lipoprotein complex at the same time formed by one or more protein fractions from animal and/or vegetable sources (and/or peptides obtained by hydrolysis of the proteins themselves) together with one or more phospholipid species, as well as to pharmaceutical and dietetic compositions, and food containing said lipoprotein complex.
More particularly, the present invention relates to a lipoprotein complex comprising:
a lipase-inhibiting protein or peptide component, and/or
an amylase-inhibiting protein or peptide component, and
a phospholipid component.
More specifically, the present invention relates to compositions of lipase- and/or amylase- inhibiting proteins and phospholipids as well as to compositions of fibers, lipase- and/or amylase- inhibiting proteins and phospholipids, which surprisingly proved to reduce the weight increase following hypercaloric diets, while exerting effective hypocholesterolemizing, hypotriglyceridemizing and antioxidant activities. These surprising activities of the lipoprotein complexes can further be enhanced by combining them with polysaccharide matrices consisting of one or more species of vegetable and/or animal fibers.
Some specific proteins (and/or some peptides obtained by hydrolysis therefrom) capable of inhibiting the activities of lipases and amylases (the enzymes capable of promoting digestion and therefore the absorption and bioavailability of fats and carbohydrates which recognizedly are the main source of calories for human body), have been studied and identified in common food, both from animal and vegetable sources. In view of these evidences, these protein purified fractions and/or peptides therefrom can be used for the treatment of overweight and obesity. Known examples of lipase-inhibiting proteins and/or peptides are:
a) the protein and/or peptide fractions extracted from wheat flour according to the procedures by H. Tani et al. (1994, J. Agric. Food Chem., vol. 42, page 2382)
b) the globin protein and/or peptide fractions extracted and purified from animal erythrocytes and tested according to the procedures by K. Kayawa et al. (1996, Life Sci, vol. 58 n. 20, page 1745)
c) the protein and/or peptide fractions extracted and purified from soy-bean and tested according to the procedures by Gargouri Y. et al. (1984, J. Lipid Res., vol. 25, page 1214) and by K. Satouchi et al. (1974, Agr. Biol. C 38, 1, page 97)
d) the protein and/or peptide fractions deriving from animal or egg serum albumins, from animal lactoglobulins and myoglobins obtained and tested according to the procedures by Gargouri Y. et al. (1985, J. Biol. Chem., vol. 260 n. 4, page 2268)
Examples of amylase-inhibiting proteins and/or peptides are:
a) the protein and/or peptide fractions of vegetable albumins extracted from the caryopsis of a number of cereals, in particular wheat and barley, and tested according to the procedures by Silano V. et al. (1975, Biochim. Biophys. Acta, vol. 391, page 170) and by O'Donnell M. D. et al. (1976, Biochim. Biophys. Acta, vol. 422, page 159)
b) the protein and/or peptide fractions extracted from leguminous plants, in particular bean, and tested according to the procedures by Marshall J. T. et al. (1975, J. Biol. Chem., vol. 250 n. 20, page 8030).
Furthermore, a number of dietetic preparations for the control of overweight are already marketed which make use of one or more of the above cited protein and/or peptide components capable of inhibiting the activities lipases and/or the amylases, selected from those described above and used together with other widely known, already used nutrients capable promoting the control of overweight, such as different species of fibres, some minerals, vitamins, etc.
Examples of these commercial preparations are:
a) Half Sitoal by Nihon Clinic (Japan)
b) Napple by Hankyu Kyoei Bussan (Japan)
c) Sweet Cut Diet by Tokyo Nagai (Japan)
d) Triple Block by Yuuki System (Japan)
e) Fast Slim Ladia by Kenbisha (Japan)
f) Peptide FM by Strength System (Germany)
g) Citrisan by Swedish Makronova AB (Sweden)
h) Bean Rep by Cheil Food & Chemical (South Korea)
i) Allure, after dinner tablets by Kernpharm-Ultra Vit. BV (the Netherlands)
l) Fat cut by Sentose (Taiwan)
m) Oligo Peptide by Pharmafood (The Netherlands).
The present invention surprisingly proved that lipoprotein complexes containing one or more of these protein components (or the peptides obtained by hydrolysis of these proteins), having inhibiting activity on digestive lipases and amylases, together with a phospholipid component from animal and/or vegetable sources, are an effective, well tolerated nutritional supplement capable of reducing simultaneously and with a surprising synergism: a) overweight and obesity; b) hypercholesterolemia; c) hypertriglyceridemia and d) increased formation of plasma and tissue peroxides in animals and humans following hypercaloric and/or unbalanced diets. Preferably, the lipase-inhibiting protein or peptide component is 10 to 40% by weight of the lipoprotein complex, the amylase-inhibiting component is 10 to 40% and the phospholipid component is 20 to 80% by weight of said complex.
Non-limiting examples of protein. fractions (and/or of peptides obtained by hydrolysis of said proteins) are the already listed preparations of proteins of vegetable and/or animal origin.
Non-limiting examples of phospholipid components from animal and/or vegetable sources are phosphatidylcholine, phosphatidylethanolamine, mono- and dimetilphosphatidylethanolamine, phosphatidylserine, phosphatidylinositol and derivatives, phosphatidylglycerol, cardiolipins, lysophospholipid analogues of the compounds mentioned above and/or mixtures thereof.
The lipoprotein complexes should be administered in a daily amount such as to reach an intake of 0.01-2000 mg, preferably 5-100 mg, of proteins per kg body weight and of 0.01-1000 mg, preferably 5-100 mg, of phospholipids per kg body weight.
The present inyention also relates to compositions obtained by combining the above cited lipoprotein complexes with a polysaccharide component selected from the group consisting of starches and flours, celluloses, chitins and chitosans, pectins, inulins, lignins and derivatives, cyclodextrins and derivatives, and mixtures thereof.
The present invention further relates to the pharmaceutical compositions (tablets, sugar-coated pills, lozenges, chewable tablets, effervescent tablets, syrups, chewing gums, etc.) as well as the various foods (bread, pasta, crackers, pizzas, pies, biscuits, juices, soft drinks, milk and derivatives, honey, butter and margarine, dressings and seasonings, mayonnaise, creams, and the like) containing the lipoprotein complexes and the compositions mentioned above, for the oral administration.
Finally, the invention relates to a process for the preparation of both the lipoprotein complexes as such and the compositions including the polysaccharide component.
The advantages of the complexes and compositions according to the present invention will be further evidenced by the following examples.
REFERENCES:
patent: 5411956 (1995-05-01), Miyazaki et al.
patent: 5643874 (1997-07-01), Bremer et al.
patent: 24 00 518 (1975-07-01), None
patent: 297 08 250 (1997-07-01), None
patent: 0 451 436 (1991-10-01), None
J. Agric. Food Chem., 1994, 42, 2382-2385, “Purification and Characterization of Proteinous Inhibitor of Lipase from Wheat Flour”, H. Tani et al.
Life Sciences, vol. 58, No. 20, pp. 1745-'755, 1996, Globin Digest, Acidic Protease Hydrolysate, Inhibits Dietary Hypertriglyceridemia and Val-Val-Tyr-Pro, etc., K. Kagawa et al.
Journal of Lipid Research, vol. 25, 1984, pp 1214-1221, “Studies on the inhibition of pancreatic and microbial lipases by soybean proteins”, Y. Gargouri et al.
Agr. Biol. Chem., 38(1), 97-101, 1974, “Characterization of Inhibitor Protein for Lipase in Soybean Seeds”, K. Satouchi et al.
The Journal of Biological Chemistry, vol. 260, No. 4, Issue of Feb. 25, pp. 2268-2273, “Inhibition of Lipases by Proteins A Kinetic Study with Dicaprin Monolayers”, Y. Gargouri et al.
Biochimica et Biop
Cestaro Benvenuto
Pistolesi Elvira
Davenport Avis M.
Griffin & Szipl, P.C.
Hunza di Maria Carmela Marazzita S.A.S.
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