1996 Fiscal Year Final Research Report Summary
Biochomistry and Food Chamistry of Exracellular matrix components of fish and Shell-fish
| Project/Area Number |
06303013
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 総合 |
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| Research Field |
Fisheries chemistry
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SAKAGUCHI Morihiko Kyoto Univ.Dept.Agric, 農学部, 教授 (00027187)
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| Co-Investigator(Kenkyū-buntansha) |
WATABE Shugo Tokyo Univ.Dept.Agric.and Life Sci.Professor, 農学生命科学研究科, 教授 (40111489)
UCHIDA Naoyuki Nippon Univ.Dept.Bioresources Professor, 生命資源学部, 教授 (80151885)
TSUCHIYA Takahide Sophia Univ.Dept.Sci.and Technol.Professor, 理工学部, 教授 (90053694)
KIMURA Shigeru Tokyo Fisheries Univ.Dept.Fisheries Professor, 水産学部, 教授 (10017056)
YOSHINAKA Reiji Fukui Pref.Univ.Dept.Bioresoorces Professor, 生物資源学部, 教授 (70026483)
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| Project Period (FY) |
1994 – 1996
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| Keywords | Extracellular matrix / collagen / fibronectin / gelatinase / proteoglycan / texture |
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| Research Abstract |
In the present study, we identified the components present in the extracellular matrix of fish and marine vertebrates and examined their structure and properties. We also studied the enzymes involved in the breakdown of collagen, a major matrix component, in association with post-mortem change in the muscle texture. Major results obtained are as follows : (1) Molecularspecies of sea urchin and sea cucumber collagens are composed of (alpha1) _2alpha2. (2) Composition of fish proteoglycan is studied, and mitogenic activities of liver and bone in rat tested by the oral administration were detected. (3) Fibronectins were purified from various fish serum and the conditioned medium of carp fibroblast cells. By comparing the biological activity, the difference in the cell spreading activity was demonstrated between serum and cellular fibronectins. (4) Subunit composition of type V collagen of rainbow trout muscle was clarified and the degradation of high molecular substance of type V collagen during ice-storage was demonstrated. (5) Collagenolytic activity was not detected in serum, but various gelatinolytic activities derived from serine-type proteinases (70kDa-120kDa) and metallo-type proteinases (<100kDa) were detected in the extracts of various fish tissues. (6) Tenderization of muscle tissue possibly due to the solubilization of skin collagen was demonstrated for common squid. (7) Subunit composition of kuruma prawn and Antarctic krill was studied and disintegration of pericellular connective tissues of kuruma prawn during chill-storage was shown to be partly due to the biochemical change of alpha2 (AR-I) component. (8) Gelationlytic activity derived from a 148kDa factor most active in acidic pH range was detected in abalone muscle and the N-terminal amino acid sequence was determined.
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[Publications] K.Sato, M.Ando, S.Kubota, K.Origasa, H.Kawase, H.Toyohara, M.Sakaguchi, T.Nakagawa, Y.Makinodan, K.Ohtsuki, and M.Kawabata: "Involvement of type V collagen in softening of fish muscle during short-term chilled storage" J.Agric.Food Chem.(in press). (1997)
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