| Project/Area Number |
13660205
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Fisheries chemistry
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| Research Institution | Fukui Prefectual University |
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Principal Investigator |
YOSHINAKA Reiji Fukui Prefectural University, Department of Marine Bioscience, Professor, 生物資源学部, 教授 (70026483)
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| Co-Investigator(Kenkyū-buntansha) |
MIZUTA Shoshi Fukui Prefectural University, Department of Marine Bioscience, Associate Professor, 生物資源学部, 助教授 (30254246)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2002: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2001: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | fish / collagen / primary structure / heat-induced degradation / gelatin / peptide |
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| Research Abstract |
It is widely known that collagen subunits may degraded to be peptide segments by relatively intense heat treatment. In the present study, we examined the heat-induced degradation of fish collagen and the properties of the peptide products using acid-soluble collagen preparations from skin tissues of three fish species, rainbow trout, Japanese amberjack, and Japanese founder.
Existence of two styles of heat-induced degradation was observed; one is limited degradation exhibiting reproducible band pattern on SDS-PAGE, and the other random degradation showing continuous band on SDS-PAGE. Heat treatment under acidic and neutral conditions mainly induced the former and latter degradation styles, respectively. Heat-induced degradation was relatively heavy in acidic or alkaline pH, while collagen subunits were fairly stable against heating in the range of pH 5 - 7. The heat-induced degradation was effectively inhibited in the presence of NaCl or urea. Addition of protease inhibitor cocktail did not affect the degree of heat-induced degradation, suggesting little involvement of some endogenous proteases to the heat-induced degradation. The collagen peptides generated after heat-treatment had mainly two amino acids, glycine and proline at N-terminal. N-terminal analysis after enzymatic deblocking, however, suggested that a considerable level of N-terminal amino acid might be formylated or acetylayed during heat treatment.
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