臺灣博碩士論文加值系統

本研究乃探討鹹鴨蛋之蛋白部份，經電透析脫鹽或粉末化加工處理後之理化性質與功能特性，以及其粉末對吳郭魚煉製品之質感特性的影響。
鴨蛋鹽漬8週後，其蛋白液的pH值由9.34下降至7.12；食鹽含量由0.49 %增加至7.32%；疏水性基含量由177增加至372(So/100 mg protein)；界達電位由-48.3mV下降至-26.4mV。但可溶性蛋白質含量並無顯著改變。鹹鴨蛋蛋白液以電透析法進行脫鹽處理。當食鹽去除率達95%時，蛋白液之pH略為回升，可溶性蛋白質的保留率達95%以上，而疏水性基含量則下降約30﹪。經由SDS-PAGE電泳圖譜得知，鹽漬與電透析脫鹽處理對鴨蛋蛋白中各種蛋白質分子分佈並無顯著影響。除了新鮮鴨蛋組在電透析處理前、後有較高乳化活性外，各組間乳化安定性並無顯著差異。隨著鹽漬時間的增加，蛋白液之起泡性與泡沫安定性呈下降趨勢。電透析脫鹽處理後，雖能提高蛋白液的起泡性與泡沫安定性，但仍比未鹽漬的蛋白液低。鴨蛋蛋白加熱後膠體的破斷力會隨鹽漬時間增加而下降，但蛋白膠體的破斷點會增加。如經電透析脫鹽，膠體的破斷力與破斷點皆明顯下降。
不同乾燥方法對粉末化的鹹鴨蛋蛋白的一般組成，並無顯著影響。粉末化的鹹鴨蛋蛋白中粗蛋白質與食鹽含量分別為62與36％。凍結乾燥組的可溶性蛋白質含量99.8﹪為最高，而滾筒乾燥組只有7.5﹪。噴霧乾燥組有較高的表面疏水基348 So/100 mg powder，為滾筒乾燥組的4倍。以示差掃描熱分析鹹鴨蛋蛋白粉末之變性吸熱波峰的溫度，除滾筒乾燥組因在乾燥時已完全變性而無吸熱波峰外，其他各組皆比新鮮蛋白粉末約提高10℃。各粉末溶液經SDS-PAGE電泳分析，除滾筒乾燥組外，各組間之各種蛋白質分子分佈皆相似。鹹鴨蛋蛋白粉末之起泡性比原鹹鴨蛋蛋白液或新鮮鴨蛋蛋白液下降為1/4∼1/8。各組間除滾筒乾燥組之乳化能力下降與加熱無法成膠外，其他各組在乳化與質感特性值上，並無顯著差異。
以鹹鴨蛋蛋白粉末的水溶液抽取吳郭魚鹽溶性蛋白質，其中以滾筒乾燥組有最高的抽取率，而其餘各組與對照組（單獨食鹽與新鮮鴨蛋蛋白粉）並無差異。鹹鴨蛋蛋白粉末添加於吳郭魚肉鹽溶性蛋白質溶液中，當加熱溫度達 70℃後，除滾筒乾燥組外，各組之溶液濁度上升趨勢皆大於單獨魚肉鹽溶性蛋白質溶液或鹹鴨蛋蛋白粉末溶液。抽取液經SDS-PAGE電泳分析，除對照組有較高之myosin heavy chain含量外，其餘各組間的蛋白質分子組成與比例並無顯著差異。滾筒乾燥的鹹鴨蛋蛋白粉末添加於吳郭魚煉製品中，可得到最高的膠強度為 657 g.cm，但剛性度與硬度則低於其餘各組。
鴨蛋、雞蛋蛋白之蛋白質含量分別為13.1與10.6％；蛋白質組成中ovalbumin與conalbumin的含量分別為75.6 與2.6％、59.4與14.5％；疏水性基含量分別為168與205 So/100 mg protein；表面硫氫基為1.76與4.13 mmole/g。隨著加熱溫度的增加（10－80℃），兩者的疏水性基與表面硫氫基含量隨之上升。當加熱溫度達90℃時，雞蛋的疏水性基與表面硫氫基含量分別為鴨蛋的1.4倍與2.5倍。雞蛋蛋白質中的conalbumin凝聚的程度比鴨蛋高，但鴨蛋蛋白加熱成膠後的膠強度為208g.cm是雞蛋的1.5倍。
吳郭魚肉鹽溶性蛋白質溶液中分別混合鹹鴨蛋蛋白、鴨蛋蛋白、雞蛋蛋白。當加熱溫度大於90℃時，混合液的疏水性基分別下降13.2、73.5與62.3﹪；表面硫氫基分別下降4.9、88.7與86.0﹪；蛋白質的凝聚程度分別為29.6、85.8與82.4﹪。且皆比各單獨溶液之下降量為大。混合鹹鴨蛋蛋白與吳郭魚魚肉鹽溶性蛋白質，當加熱後生成的不溶性凝聚物，主要的鍵結為疏水性基的交互作用，其次才是雙硫鍵。

This study was to investigate the physico-chemical and functional properties of salted duck egg white (SDEW) which was treated by electrodialysis desalination or powderization processing. And, the effect of SDEW powder on textural characteristics of tilapia surimi product has been studied.
The protein content of duck egg white (DEW) and chicken egg white (CEW) were 13.1 and 10.6 %; the ovalbumin and conalbumin were 75.6, 2.6% and 59.4, 14.5%; the surface hydrophobic intensity were 168 and 205 (So/100mg protein); the surface sulfhydryl group were 1.76 and 4.13 (mM/g), respectively. Both of surface hydrophobic intensity and surface sulfhydryl group were increased with increasing heating temperature from 10 to 80℃. When heating temperature up to 90℃, the surface hydrophobic intensity and surface sulfhydryl group of CEW were 1.4 and 2.5 times higher than DEW. The conalbumin of CEW had a higher aggregation than DEW during heating, but the gel strength of DEW was 208 g.cm, being 1.5 times higher than CEW.
As the duck egg was pickled for 8 weeks, the egg white''s pH was decreased from 9.3 to 7.1; the NaCl content increased from 0.49 to 7.32%; the surface hydrophobic intensity increased from 177 to 372 (So/100mg protein); the Zeta potential was decreased from -48.3 to -26.4 (mV); but the soluble protein content was not significantly changed.
The SDEW was desalinized by electrodialysis. When the NaCl was removed by 95%, the pH of SDEW was slightly increased and surface hydrophobic intensity decreased by 30％, the soluble protein was remained at 95 %, and the similar distribution of protein molecules'' pattern was observed by SDS-PAGE. In the emulsion stability, except that fresh duck egg white showed a higher value, the various SDEW''s samples had no significant differences even by electrodialysis desalination treatment. Both foamability and foam stability of SDEW decreased with increasing pickling time, but the values increased after electrodialysis desalination treatment. The breaking force of SDEW''s gel decreased with pickling time, but the breaking point increased. After electrodialysis desalination treatment, both the breaking force and point of SDEW''s gel significantly decreased.
There were no significant changes in proximate composition of salted duck egg white powder (SDEWP) with different drying methods, which contained 36 % of NaCl and 62% of crude protein. The protein solubility of SDEWP with freeze drying and drum drying were 99.8 and 7.5 %, respectively. The surface hydrophobic intensity of SDEWP with spray drying was 347.9 (So/100mg protein), being 4 times higher than drum dried sample. Except the drum dried sample, all the SDEWP showed one transition temperature at 94℃, which 10℃higher than DEW was analyzed by Differential Scanning Calorimeter. Also, the SDS-PAGE pattern showed the similar distribution of protein molecules of SDEWP with different drying methods, except the drum dried sample. The foaming properties of SDEWP were decreased 4-8 times after drying treatment. There were no significant differences in emulsifying activity and gel strength among the different sample, except the drum dried sample had a lowest emulsifying ability and could not form a gel.
Extraction of tilapia salt-soluble protein (TSSP) with drum dried sample showed the highest relative extraction ratio. And, there are no significant differences in the relative extraction ratio of TSSP among with other samples and control (mix of fresh duck egg white powder and NaCl). When the heating temperature up to 70℃, the turbidity of the TSSP solution mixed with SDEWP (except the drum-dried sample) were sharply increased than TSSP solution or SDEWP solution alone. As the extracts were analyzed by SDS-PAGE, a higher quantity of myosin heavy chain was obtained with the mix of fresh duck egg white powder and NaCl. And, there are no significant differences among each kind of protein molecules and ratio in the TSSP''s extracts when different SDEWP were applied. The tilapia surimi added with drum dried SDEWP to obtain a highest gel strength being 657 g.cm, but the lowest in rigidity and hardness than other samples was found.
When each mixtures of TSSP/CEW, TSSP/DEW and TSSP/SDEW solution were heated at 90℃, the surface hydrophobic intensity was decreased to 13.2, 73.5 and 62.3%; the surface sulfhydryl group was decreased to 4.9, 88.7 and 86.0%; the protein solubility was decreased to 29.6, 85.8 and 82.4 %, respectively. These values decreased sharply than each individual of TSSP, CED, DEW and SDEW solution. As an insoluble aggregates was produced from TSSP/SDEW mixture solution after heating at 90℃, it was suggested that the hydrophobic interaction between the two kinds of protein molecules was primary, then the disulfide bonding was secondary.

封面
目錄
表次
圖次
中文摘要
英文摘要
第一章、前言
第二章、文獻整理
2-1.鴨蛋
2-2.鹹鴨蛋
2-3.蛋白的功能性質
2-4.電透析分離技術
2-5.乾燥對蛋白功能性質的影響
2-6.魚肉肌原纖維蛋白質
第三章、材料與方法
3-1.材料
3-2.製備方法
3-3.分析方法
第四章、結果與討論
4-1.鹽漬時間對鹹鴨蛋蛋白液理化性質與功能特性的影響
4-2.電透析脫鹽對鹹鴨蛋蛋白液理化性質與功能特性的影響
4-3.粉末化之鹹鴨蛋蛋白理化與功能特性
4-4.不同乾燥方法的鹹鴨蛋蛋白粉對吳郭魚煉製品質感特性的影響
4-5.鴨蛋與雞蛋蛋白液的理化性質
4-6.吳郭魚肉鹽可溶性蛋白質與鹹鴨蛋蛋白混合液在加熱過程中蛋白質分子性質的變化
第五章、結論
參考文獻
附錄﹝本論文已發表部分之全文﹞

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