{"created":"2023-07-25T08:13:49.010196+00:00","id":14729,"links":{},"metadata":{"_buckets":{"deposit":"efaf568c-5eea-4ee7-a6e1-a05d8e08a3f4"},"_deposit":{"created_by":18,"id":"14729","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"14729"},"status":"published"},"_oai":{"id":"oai:ir.kagoshima-u.ac.jp:00014729","sets":["70:72"]},"author_link":["133559"],"item_5_date_6":{"attribute_name":"作成日","attribute_value_mlt":[{"subitem_date_issued_datetime":"2019-03-29","subitem_date_issued_type":"Collected"}]},"item_5_date_granted_54":{"attribute_name":"学位授与年月日 ","attribute_value_mlt":[{"subitem_dategranted":"2019-03-15"}]},"item_5_degree_grantor_53":{"attribute_name":"学位授与機関","attribute_value_mlt":[{"subitem_degreegrantor":[{"subitem_degreegrantor_language":"ja","subitem_degreegrantor_name":"鹿児島大学"}],"subitem_degreegrantor_identifier":[{"subitem_degreegrantor_identifier_name":"17701","subitem_degreegrantor_identifier_scheme":"kakenhi"}]}]},"item_5_degree_name_42":{"attribute_name":"学位名","attribute_value_mlt":[{"subitem_degreename":"博士(水産学)","subitem_degreename_language":"ja"},{"subitem_degreename":"Doctor of Philosophy","subitem_degreename_language":"en"}]},"item_5_description_17":{"attribute_name":"ファイル(説明)","attribute_value_mlt":[{"subitem_description":"博士論文全文, 博士論文要旨(日本語), 博士論文要旨(English), 最終試験結果の要旨, 論文審査の要旨","subitem_description_language":"ja","subitem_description_type":"Other"}]},"item_5_description_4":{"attribute_name":"要約(Abstract)","attribute_value_mlt":[{"subitem_description":"The value of fisheries products is evaluated by freshness. Fish which are frozen pre rigor have a better quality on thawing than fish of lower initial freshness. On the other hand, there have been few scientific reports on why muscle protein of fresh fish is more stable during frozen storage than that of less fresh ones. In this study, I focused on the protective effect of adenosine triphosphate (ATP) on fish muscle proteins.\nIn the 1st chapter, the suppressive function of ATP on freeze denaturation of myofibrillar protein from Alaska Pollack and croaker surimi was investigated. Freeze denaturation of myofibrillar protein was suppressed by the addition of ATP. The suppression effect of ATP on freeze denaturation depended on the ATP concentration, freezing temperature and fish species. In the 2nd chapter, the effect of ATP on the denaturation of myosin in “burnt meat” was investigated. The suppression effect of ATP on acidic thermal denaturation of tuna myosin subfragment 1 (S 1) by measuring the changes in turbidity of myosin S 1 solution and Ca ATPase activity. The increase of turbidity of myosin S 1 solution and the inactivation of myosin S 1 Ca ATPase during acidic thermal treatment were suppressed strongly with the presence of physiological concentration of ATP. The rapid reduction of ATP during the early postmortem stage may act as a trigger of the acceleration of acidic thermal denaturation of tuna myosin in burnt meat. In the 3rd chapter, the suppressive effect of ATP on urea denaturation of shark muscle was investigated. Urea is known as a powerful protein denaturant. Elasmobranches, such as sharks, retains large amount of urea in their body, but muscle proteins of sharks are maintained even in the presence of urea in vivo. The protection effect of ATP on fish muscle proteins was focused, and the suppressive effect of ATP on urea denaturation of myosin Ca ATPase from scalloped hammerhead was studied. Myosin was incubated at various temperature in the presence of both urea and ATP. Both urea and ATP were removed from the incubated myosin by dialysis, and then Ca--ATPase activity of the incubated myosin was assayed. In the case of myosin incubated with both ATP and urea, its Ca--ATPase activity was higher than incubated with urea. This result suggested that ATP suppressed urea denaturation of myosin Ca--ATPase. ATP may act as a safeguard of muscle protein against urea in vivo. In the 4th chapter, the procedure for freeze--thawing of olive flounder for consumption of high quality raw fish as sashimi was investigated. Freeze--thawed meat which was frozen containing a high concentration ATP immediately after instantaneous killing and then thawed by slow thawing method showed high quality for sashimi and properties of myofibrillar protein were maintained considerably.\nThe above results indicate that ATP may protect of fish muscle protein against various denaturation in vivo and in fishery food processing. These results will contribute to keeping freshness and producing high quality fisheries products.","subitem_description_language":"en","subitem_description_type":"Other"},{"subitem_description":"水産物の価値は鮮度によって評価されることが多い。鮮度の良い水産物を凍結した場合,その品質は良い状態で保たれる。このことは水産業従事者の経験に基づ いた知見であるが,高鮮度水産物で冷凍耐性が高いことに関する科学的な研究はほとんど行われていない。本研究では,生体内に 5 10 mMの濃度で存在する高エネルギー物質であるアデノシン三リン酸( adenosine triphosphate ATP)のタンパク質安定化作用に着目し,魚類筋肉タンパク質の冷凍変性,熱変性,酸性 pH変性,尿素変性に対する ATPの変性抑制 作用について検討し,ATPのタンパク質安定化作用メカニズムの解明とその研究成果を高品質水産加工品の製造に応用することを目的とした。\n第1章で魚類筋原線維タンパク質( Mf)の冷凍変性に対する ATPの保護効果について検討した結果,生理的な ATP濃度下で Mfの冷凍変性抑制効果を確認することができた。その効果は, ATP濃度と凍結貯蔵温度に依存し,魚種差を示した。次に,マグロの「ヤケ肉」の発生と ATPのタンパク質安定化作用の関係について検討した。ヤケ肉は致死後の魚肉の酸性化と高体温が発生原因であり,同時に ATPは急速 に消失することが報告されて いる。第 2章では,酸性pH下でのマグロミオシンサブフラグメント 1 S 1)の熱変性に及ぼす ATPの作用について検討した。その結果,酸性 pH下のミオシン S 1の熱変性は,生理的な濃度の ATPで強く抑制された。マグロのヤケ肉発生は,致死後の魚肉の酸性化と高体温に加えて,急速な ATPの消失が引き金になると推察した。第3章では,サメミオシンの尿素変性に対する ATPの変性抑制作用について検討した。海産サメ類は,タンパク質変性作用を示す尿素を体内に高濃度で蓄積しているにも関わらず,筋肉は重篤 な筋疾患を起こさない。この ことについて,私は ATPのタンパク質安定化作用が働いているのではないかと考えた。アカシュモクザメのミオシンを尿素と ATP存在下で一定温度で保持した後,ミオシンCa-ATPase残存活性を測定した結果,ATPが存在することで尿素によるミオシンCa-ATPaseの失活は抑制されることを見出した。サメ類の生体内において,ATPは尿素によるタンパク質の変性を抑制する作用を有すことが示された。第4章では,ATPのタンパク質安定化作用を利用し,刺身の品質を示す高品質冷凍ヒラメの製造条件を検討した。活けしめ直後の高濃度ATPを含むヒラメ肉と,一晩冷蔵したヒラメ肉を凍結し,解凍後の魚肉の性状を測定した。ATPを高濃度に含んだ状態で凍結し緩慢解凍したヒラメ肉は,他の条件で凍結解凍したヒラメ肉よりも筋原線維タンパク質の塩溶解性とCa-ATPase比活性は高く,肉質が良いことを示した。また,官能評価においても高い評価が得られた。\n以上の結果から,ATPは魚肉タンパク質の安定化に寄与し,生体内や水産加工過程で起こりうる各種変性を抑制するとこが明らかとなった。本研究成果は水産物の鮮度維持と高品質水産加工品の製造に応用されることが期待される。","subitem_description_language":"ja","subitem_description_type":"Other"}]},"item_5_dissertation_number_55":{"attribute_name":"学位授与番号","attribute_value_mlt":[{"subitem_dissertationnumber":"乙連論第138号"}]},"item_5_publisher_23":{"attribute_name":"公開者・出版者","attribute_value_mlt":[{"subitem_publisher":"鹿児島大学 ","subitem_publisher_language":"ja"},{"subitem_publisher":"カゴシマ ダイガク","subitem_publisher_language":"ja-Kana"},{"subitem_publisher":"Kagoshima University","subitem_publisher_language":"en"}]},"item_5_subject_15":{"attribute_name":"NDC","attribute_value_mlt":[{"subitem_subject":"667","subitem_subject_scheme":"NDC"}]},"item_5_text_44":{"attribute_name":"備考","attribute_value_mlt":[{"subitem_text_value":"【指導教員:木村郁夫】"}]},"item_5_text_47":{"attribute_name":"date.appl","attribute_value_mlt":[{"subitem_text_value":"【学位申請日】2018-10-22"}]},"item_5_version_type_14":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"open access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_abf2"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"緒方, 由美","creatorNameLang":"ja"},{"creatorName":"オガタ, ユミ","creatorNameLang":"ja-Kana"},{"creatorName":"Ogata, Yumi","creatorNameLang":"en"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-08-22"}],"displaytype":"detail","filename":"Diss_緒方_由美_TO138_2019.pdf","filesize":[{"value":"1.8 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"Diss_緒方_由美_TO138_2019","objectType":"fulltext","url":"https://ir.kagoshima-u.ac.jp/record/14729/files/Diss_緒方_由美_TO138_2019.pdf"},"version_id":"b4ff3c8c-3c52-4f1c-8b44-4867799a70f2"},{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-06-19"}],"displaytype":"detail","filename":"Abstract_緒方_由美_TO_2019_日本語.pdf","filesize":[{"value":"142.2 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