Mechanizm of an unique degrading behavior of bivalve molluscan collagen by protease digestion
| Project/Area Number |
20580223
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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 Prefectural University |
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Principal Investigator |
MIZUTA Shoshi 福井県立大学, 海洋生物資源学部, 准教授 (30254246)
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| Project Period (FY) |
2008 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2011: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2010: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2009: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | コラーゲン / 二枚貝 / ホタテガイ / サブユニット / 塩酸グアニジン / ペプシン / 二枚具 / ホタテガ |
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| Research Abstract |
To elucidate the mechanism of an unique degrading behavior of bivalve molluscan collagen by protease digestion, the major twoα chains, named a and bchains, were isolated from the intact collagen preparation, prior to protease digestion, from scallop mantle, and their biochemical properties were investigated. Moreover, pepsin-solubilized collagen was found to have unusual solubility for collagens, showing high solubility around weak-basic pH. Based on this solubility, the major molecular species of collagen was successfully purified from pepsin-solubilized collagen preparation. It is necessary to identify the criticalα component for the unique degrading behavior by chasing the behavior of each majorα component on protease digestion.
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Report
(6 results)
Research Products
(11 results)
