Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Casein or caseinate
Reexamination Certificate
1999-03-23
2001-01-30
Crouch, Deborah (Department: 1632)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Casein or caseinate
C530S350000
Reexamination Certificate
active
06180761
ABSTRACT:
FIELD OF THE INVENTION
The present invention is generally directed to a casein having a novel amino acid sequence and process for the preparation thereof. In particular, the present invention relates to a casein having a novel amino acid sequence which solubilizes minerals to promote an absorption thereof in the alimentary tract in animals, and process for the preparation thereof.
DESCRIPTION OF THE PRIOR ART
In general, minerals should be kept in a soluble state to be absorbed into animals. However, as contents moves through the small intestine in animals, a pH thereof shifts from a neutral to an alkaline state. In accordance with the change of pH in the small intestine, a large portion of minerals becomes insoluble to cause a precipitation. Concerning a calcium absorption, as a calcium moves through the small intestine, a portion of soluble calcium decreases in inverse proportion to an increase of pH therein. It is known that when a casein is supplied into animals together with calcium, a soluble calcium significantly increases in the small intestine in animals compared with a supply of calcium alone.
While an active transport prevails in the upper small intestinal tract in the calcium absorption, a passive transport is dominant in the lower small intestinal tract based on a concentration equilibrium. It is also suggested that vitamin D and lactose further promote the calcium absorption in animals. Although an absorption rate of calcium reveals high in the upper part of the small intestine, i.e., the duodena in animals, the retention time of contents is so short that the whole amount of calcium absorption therein is relatively low. In contrast, due to the long retention time of a diet, the ileum located in the lower part of the small intestine is an important part at which a large portion of calcium is absorbed. In fact, 62 or 88% of calcium is absorbed in the ileum in rats; and the calcium absorption in a human body excised with the ileum decreases greatly. It is accordingly understood that a casein phosphopeptide (hereinafter, referred to as “CPP”) plays an important role in a calcium absorption (Sato et al., “Casein phosphopeptide contributing to an absorption of Ca in dairy product,” Chemistry and Biology, Vol. 23, No. 7, p. 418 (1985)).
An obesity is one of the most dangerous hazard to threaten the health of modern people, which is largely due to high calory foods and beverages insufficient in vitamins and minerals. It is known that such unbalanced foodstuffs are responsible for diseases of adult people such as an osteoporosis. In order to prepare balanced foodstuffs, many researchers have tried to add one or more insufficient minerals to the foodstuffs. However, almost those attempts have been found unsuccessful because an addition of one mineral results in an absorption inhibition or decrease of other minerals in animals. Accordingly, it is desired to increase a mineral absorption rate in animals without adding minerals to foodstuffs. In the view of this respect, a casein has been considered as an important material.
A casein is one kind of protein contained in bovine or human milk, and &agr;, &bgr; and &ggr; types have been reported. In particular, &bgr;-casein have A
1
, A
2
, A
3
, B, C, D and E variants whose primary structures have been already suggested (W. N. Eigel, et al., Nomenclature of Proteins of Cow's milk (5th Revision), J. Dairy Sci. Vol. 67, No. 8, pp. 1607-8 (1984)).
The amino acid sequence of A
2
variant of representative &bgr;-casein is as follows (SEQ ID NO: 2):
Arg-Glu-Leu-Glu-Glu-Leu-Asn-Val-Pro-Gly-
5 10
Glu-Ile-Val-Glu-Ser-Leu-Ser-Ser-Ser-Glu-
15 20
Glu-Ser-Ile-Thr-Arg-Ile-Asn-Lys-Lys-Ile-
25 30
Glu-Lys-Phe-Gln-Ser-Glu-Glu-Gln-Gin-Gln-
35 40
Thr-Glu-Asp-Glu-Leu-Gln-Asp-Lys-Ile-His-
45 50
Pro-Phe-Ala-Gln-Thr-Gln-Ser-Leu-Val-Tyr-
55 60
Pro-Phe-Pro-Gly-Pro-Ile-Pro-Asp-Ser-Leu-
65 70
Pro-Gln-Asn-Ile-Pro-Pro-Leu-Thr-Gln-Thr-
75 80
Pro-Val-Val-Val-Pro-Pro-Phe-Leu-Gln-Pro-
85 90
Glu-Val-Met-Gly-Val-Ser-Lys-Val-Lys-Glu-
95 100
Ala-Met-Ala-Pro-Lys-His-Lys-Glu-Met-Pro-
105 110
Phe-Pro-Lys-Tyr-Pro-Val-Gln-Pro-Phe-Thr-
115 120
Glu-Ser-Gln-Ser-Leu-Thr-Leu-Thr-Asp-Val-
125 130
Glu-Asp-Leu-His-Leu-Pro-Pro-Leu-Leu-Leu-
135 140
Gln-Ser-Trp-Met-His-Gln-Pro-His-Gln-Pro-
145 150
Leu-Pro-Pro-Thr-Val-Met-Phe-Pro-Pro-Gln-
155 160
Ser-Val-Leu-Ser-Leu-Ser-Gln-Ser-Lys-Val-
165 170
Leu-Pro-Val-Pro-Glu-Lys-Ala-Val-Pro-Tyr-
175 180
Pro-
Han Sang Kee
Shin Yoo Cheol
Crouch Deborah
Han Sang Kee
Staas & Halsey , LLP
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