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Study on the aggregation mechanism of walleye pollack myosin

Research Project

Project/Area Number 09660216
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Fisheries chemistry
Research InstitutionHOKKAIDO UNIVERSITY

Principal Investigator

OJIMA Takao  Hokkaido Univ., Fac. of Fish., Asso. Pro., 水産学部, 助教授 (30160865)

Co-Investigator(Kenkyū-buntansha) NISHITA Kiyoyoshi  Hokkaido Univ., Fac. Of Fish., Pro., 水産学部, 教授 (20001620)
Project Period (FY) 1997 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1999: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1998: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1997: ¥1,400,000 (Direct Cost: ¥1,400,000)
KeywordsWalleye pollack / myosin / polymer / aggregation / cross-linking / protein denaturation / gelation / fish meat paste
Research Abstract

Walleye pollack Theragra chalcogramma is one of the major sources for food processing industries in Japan. In the present study, the heat-induced aggregation mechanism for the walleye pollack myosin was investigated by using isolated pollack myosin, HMM, and LMM. According to the circular dichroism spectrometry and α-chymotryptic digestion of the walleye pollack LMM, the α-helices of N-terminal 2/3 and C-terminal 1/3 regions of the LMM were revealed to be reversibly and irreversibly unfolded, respectively, by the heat-treatment at 5O℃ for 5 min. The LMM region of intact pollack myosin showed similar denaturation process to the isolated LMM upon heat-treatment. Then, the changes in hydrophobicity of the myosin, HMM, and LMM during heat-treatment were investigated by means of ANS-fluorescent spectrometry. The ANS-fluorescence of myosin and HMM showed significant increase at temperatures higher than 40℃, however, that of LMM showed practically no change. This indicates that the increase in hydrophobiclty of the myosin by the heat-treatment is mainly due to the denaturation of HMM region. Concomitantly with the increase in hydrophobicity, turbidity of the myosin and HMM significantly increased, however, that of the LMM showed no increase. These results indiccate that the myosin and HMM form aggregates upon the heat-treatment, however, the LMM is incapable of aggregating upon the same treatment although some parts of the a-helices of the LMM unfolds irreversibly. On the other hand, it was found that the LMM formed coaggregates with myosin when heated at 40℃ for 10 min together with myosin, while it did not form coaggregates with the HMM. Thus, the LMM seemed to form coaggregates with the myosin through the interaction with the tail regions of myosin. Based on these results, we presented a schematic model for the pollack myosin aggregation by the heat-treatment.

Report

(4 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • 1997 Annual Research Report
  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] T.Ojima: "Reversibility of unfolding of walleye pollack LMM by heat-treatment"Fisheries Science. 65・3. 459-465 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Takao Ojima: "Reversibility of unfolding of walleye pollack light meromyosm by heat-treatment"Fisheries Sci.. 65(3). 459-465 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] T.Ojima: "Reversibility of unfolding of walleye pollack LMM by heat-treatment"Fisheries Science. 65,3. 459-465 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] A.Inoue, T.Ojima,and K.Nishita: "Partial nucleotide sequence of a cDNA encoding C-terminal polymerizable region of akazara scallop tropomyosin" Fisheries Science. 64・1. 164-165 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] A.Inoue, T.Ojima,and K.Nishita: "Cloning and sequence of a cDNA for troponin-T of ezo-giant scallop striated muscle" Fisheries Science. 64・3. 459-463 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] T.Ojima, N.Kawashima, A.Inoue, A.Amauchi, M.Togashi, S.Watabe,and K.Nishita: "Determination of primary structure of heavy meromyosin region of walleye pollack myosin" Fisheries Science. 64・5. 812-819 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] H.Tanaka, T.Ojima,and K.Nishita: "Amino acid sequence of troponin I from Akazara scallop striated adductor muscles" Journal of Biochemistry. 124・5. 304-310 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] T.Ojima, S.Yoshikawa, and K.Nishita: "Isolation and characterization of myosin from walleye pollack surimi" Fisheries Science. 63・5. 811-815 (1997)

    • Related Report
      1997 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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