Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/56355
DC FieldValueLanguage
dc.contributor.author柯文慶zh_TW
dc.contributor.other行政院國家科學委員會zh_TW
dc.contributor.other中興大學食品科學系zh_TW
dc.date2000zh_TW
dc.date.accessioned2014-06-06T09:05:54Z-
dc.date.available2014-06-06T09:05:54Z-
dc.identifierNSC88-2313-B005-066zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/56355-
dc.description.abstract吳郭魚myosin與其斷片(S-1及rod)經加壓處理後觀察其變性之情形。由物理性質測定發現,S-1最易發生凝集,myosin次之,rod最不容易形成凝膠;顯示myosin在凝膠過程中是由S-1先行凝集,再由rod形成網狀結構。由化學性質測定得知,無論是疏水基的暴露或反應硫氫基之減少,都是以S-1之變化最大,其次為myosin。顯示S-1的凝集是因加壓後內部疏水基之暴露造成硫氫基反應而產生雙硫鍵。而在以1,000 atm加壓處理時有明顯的效果,顯示吳郭魚肌肉形成凝膠的臨界壓力是1,000 atm。zh_TW
dc.description.abstractThe denaturation of tilapia myosin and its fragments (S-1 and rod) by high pressure (500-2,000 atm) was investigated. According to the changes of physical properties, S-1 aggregated the most easily. It indicated that S-1 aggregated at the early stage of myosin gelation, and then formed network structures by rod. After pressurization, the changes of hydrophobicity and reactive SH groups of S-1 were more than myosin and rod. It presented that myosin molecules formed disulfide bonds by S-1s. The pressure started to make myosin gel was about 1,000 atm.en_US
dc.language.isozh_TWzh_TW
dc.relation.urihttp://grbsearch.stpi.narl.org.tw/GRB/result.jsp?id=434981&plan_no=NSC88-2313-B005-066&plan_year=88&projkey=PD8802-0288&target=plan&highStr=*&check=0&pnchDesc=%E9%AB%98%E5%A3%93%E8%99%95%E7%90%86%E5%B0%8D%E5%90%B3%E9%83%AD%E9%AD%9A%E8%82%8C%E8%82%89%E8%82%8C%E5%87%9D%E8%9B%8B%E7%99%BD%E5%8F%8A%E5%85%B6%E6%96%B7%E7%89%87%E8%AE%8A%E6%80%A7%E4%B9%8B%E5%BD%B1%E9%9F%BFen_US
dc.subject食品科技zh_TW
dc.subject基礎研究zh_TW
dc.subjectGelatinen_US
dc.subject凝膠zh_TW
dc.subject肌凝蛋白zh_TW
dc.subject魚肉zh_TW
dc.subject高壓處理zh_TW
dc.subject吳郭魚zh_TW
dc.subject肌動凝蛋白zh_TW
dc.subjectMyosinen_US
dc.subjectFish meaten_US
dc.subjectHigh pressure treatmenten_US
dc.subjectTilapiaen_US
dc.subjectActomyosinen_US
dc.title高壓處理對吳郭魚肌肉肌凝蛋白及其斷片變性之影響zh_TW
dc.titleEffect of Hydrostatic Pressure on Denaturation of Myosin and Its Fragments from Tilapia Meaten_US
dc.typeResearch Reportszh_TW
item.grantfulltextnone-
item.openairetypeResearch Reports-
item.cerifentitytypePublications-
item.fulltextno fulltext-
item.languageiso639-1zh_TW-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:食品暨應用生物科技學系
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