碩士 / 國立屏東科技大學 / 食品科學系所 / 101 / The thermal gelation of cross-linked milkfish muscle proteins with 1-ethyl-3-（3-dimethylamino-propyl）carbodiimide（EDC）was studied by means of jelly-strength , ATP sensitivity , the activities of ATPases , SDS electrophoresis and chymotryptic digestibility. The treatment with EDC（0.1mg EDC/mg protein）gave higher jelly-strength values to the actomyosin for all the tested temperatures. Gel-disintegration for actomyosin and myosin was completely depressed by EDC. By treating the actomyosin with EDC（0.05 mg EDC / mg protein）, the activation of Mg-ATPase and inactivation of EDTA-ATPase occurred simultaneously while Ca-ATPase was unchanged. In EDC-treated actomyosin the decrease of myosin heavy chain and the formation of polymers were observed form SDS electrophoretograms. The EDC-treatment for actomyosins resulted in the decrease in the relative viscosity and the disappearance of ATP sensitivity.The desalting aggregation ability of actomyosins disappeared with EDC-treatment. The cross-linked myosin with EDC formed a polymerized complex. The thermal gelation of myosin by heating at 30-50℃ were enhanced in the presence of up to 25 mol EDC/105g protein and the EDC more than 25 mol effectively depressed gel-disintegration. The chymotryptic digestion of EDC-myosin suggested that there are two cross-linking sites with EDC above or below 1mM.
| Identifer | oai:union.ndltd.org:TW/101NPUS5253014 |
| Date | January 2013 |
| Creators | 李薏姍 |
| Contributors | 邱文貴 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 70 |
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