Mechanism of cross-linking of casein by colloidal calcium phosphae in casein micelles
| Project/Area Number |
02660146
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
製造化学・食品
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| Research Institution | Faculty of Agriculture, Kagoshima University |
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Principal Investigator |
AOKI Takayoshi Agriculture Biochem. Sci. & Tech. Associate Prof., 農学部, 助教授 (70034460)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1991: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1990: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | Casein / Casein micelle / Calcium phosphate / Colloidal calcium phosphate / 卵白フラボプロテイン / 人βーカゼイン |
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| Research Abstract |
Calcium and inorganic phosphate are present in excess of their Solubility and interact with casein. Calcium phosphate ity casein micelles, which is associated with casein, is called colloidal calcium phosphate(CCP). Although CCP cross-links caseins through phosphate groups, the mechanism of cross-linking has not yet been elucidated sufficiently. In the present study following results were obtained.
A small amount of the 3-P component of human beta-casein and a considerable amount of the 4-P and 5-P components were found in the CCPcross-linked casein separated from artificial casein micelles of whole human casein. CCP-cross-linked casein was formed in artificial casein micelles of tlie 3-P and 4-P components of human beta-casein with kappa-casein. In contrast, no cross-linitage was formed in artificial casein micelles of the 1-P and 2-P coutponeiits. It was concluded that at least three phosphate groups were need fGr cross-linking of casein by CCP.
CCP-cross-linked casein taras formed when calcium, phosphate and citrate were added to sodium caseinate solution. This suggested that the submicelle structure and ordered structures of casein were unnecessary for caseins to be cross-linked by CCP.
When amino groups of alpha_<s1>-casein were acetylated, citraconilated, orsuccinylated, modified alpha_<s1>-casein was somewhat more hardly cross-linked by CCP than native one.
Egg white ribofravin-binding protein is also cross-linked through its phosphate groups by CCP.
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Report
(3 results)
Research Products
(8 results)
