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研究生:陳雪芳
研究生(外文):Chen, Hsueh-Fang
論文名稱:熱不凝固雞蛋蛋白之製備研究
論文名稱(外文):Studies on the thermostability of chicken egg white
指導教授:楊勝欽楊勝欽引用關係
指導教授(外文):Sheng-Chin Yang
學位類別:碩士
校院名稱:靜宜大學
系所名稱:食品營養學系
學門:醫藥衛生學門
學類:營養學類
論文種類:學術論文
論文出版年:1997
畢業學年度:85
語文別:中文
論文頁數:119
中文關鍵詞:雞蛋蛋白熱不凝固食鹽酸鹼值稀釋度
外文關鍵詞:egg whitethermal non-coagulationNaClpHdilution
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本研究主要探討不同稀釋程度的雞蛋蛋白(蛋白:水=1:1-1:5)經水煮
加熱,於不同加熱溫度及加熱時間下,觀察蛋白液之熱凝集現象,並探討pH
值及食鹽濃度對蛋白液熱凝集的影響,分析理化性質並觀察外觀變化,以確
立熱不凝固的雞蛋蛋白之製備條件。結果顯示蛋白質濃度、加熱條件及pH
值都會影響蛋白的凝集程度。蛋白質濃度及加熱溫度愈高,蛋白凝及程度
愈高,隨著稀釋度增加,可得熱不凝固的蛋白pH值範圍亦愈大。4倍水以上
的稀釋蛋白液在高溫下(90℃以上),當調整蛋白液之pH 為3.0,可減低蛋白
質之熱凝集程度,較易產生熱不凝固的混濁蛋白液;在3倍水以上的稀釋蛋
白液,調整pH值為9.3時,較易產生熱不凝固的澄清蛋白液。添加食鹽溶
液(0.01 -0.35 M NaCl )會影響蛋白的凝集程度,於低溫(60 ℃)時,2
倍水稀釋蛋白液隨著食鹽濃度增加,其凝集程度隨之降,並隨著食鹽濃度
的增加,其凝集物分子量愈大,硫氫基濃度及疏水基含量愈低。4倍水稀
釋蛋白液則隨著食鹽濃度增加,其凝集程度亦隨之增加,於60℃加熱下硫
氫基濃度減少,僅pH 7.0之蛋白在0.35M食鹽濃度時及pH 9.0與9.5之蛋白
易形成可溶性凝集物,但由於4倍水斥力環境與離子強度之間相抗衡,使
得疏水基含量有所不同;於高溫(90及120℃)加熱時,2及4倍水稀釋蛋白
則隨著食鹽濃度增加其凝集程度隨之增加,疏水基交互作用及硫氫基氧化
或硫氫基/雙硫鍵交換 ,使得疏水基及硫氫基含量減少,電泳圖變化亦較
大,並由分子量分布可知可溶性凝集物的分子量較大。就加熱不凝固的雞
蛋蛋白進行硫氫基及疏水基含量分析,結果顯示蛋白的凝集程度愈高,其
蛋白質濃度愈低,硫氫基及疏水基含量愈少,由實驗結果推測雞蛋蛋白蛋
白質加熱過程中視逐漸變化的],經聚合方式形成凝集物。首先蛋白質經
去胺作用或B-elimination反應,水解兩側之汰鍵,再藉由疏水基交互作
用及硫氫基氧化,將太鍵及粘度大分子量高且粘度大的可溶性凝集物。由
實驗結果可知蛋白質濃度、pH值、硫氫基及疏水基含量皆會影響到熱不凝
固蛋白液的蛋白質凝集程度及澄清度。
The objective of this syudy was to investigate the effect of
dilution of chicken egg white (EW)(EW:H2O=1:1-1:5), water
cooking temperature and cooking time, pH and salt (sodium
chloride) concentration on the thermal aggregation of egg white.
The physiochemical properties and changes of egg white
appearance were also observed. Results showed that protein
concentration, heating conditions and pH have effects on the
degree of aggregation. That is, the higher the protein
concentration and heating temperature in egg white, the greater
the degree of aggregation. Increasing the degree of dilution,
the pH range of thermal non-coagulated egg white was also
increased. With four times diluted EW (DEW)adjust to pH 3.0, and
heated at high temperature(>90℃ ), the degree of protein
aggregation was reduced, and more likely to obtain turbid liquid
of thermal non-coagulation. With three times DEW and adjust pH
to 9.3, it is more likely to become transparent liquid of
thermal non-coagulation.The addition of NaCl at 0.01-0.35 M
affected the degree of EW aggregation. Icreeasing the
concentration of NaCl will decrease the degree of aggregation of
two times DEW at 60℃ .In addition, the molecular weight of EW
aggregate was increased and the concent of SHs and
hydrophobicity were decreased. When heated at 60 , the SH
concent of egg white decreased, and soluble aggregates were
obtained only pH 7.0(0.35 M NaCl), pH 9.0 and pH 9.5.The
hydrophobicity was varied, becausethe repulsion environment
against the ionic strength of four times DEW. When heated
athigher temperature(90℃ and 120℃ ), the increase of NaCl
concentration resulted inthe increase degree of aggregation. The
hydrophobicity interaction and SH oxidation or SH/SS exchange
resulted in the reduction of SH content and hydrophobicity. From
the variation of electrophoregram and the distribution of
molecular weight indicatingthe molecular weight of soluble
aggregates is larger. Results showed that the higher the degree
of aggregation, the lower the protein concentration, SHs content
and hydrophobicity of the thermal non-coagulated egg white. It
is proposed that egg white protein gradually changes while
heating and becomes aggregates by polynerization.First,
hydrolyze two side polypeptide bonds the polymerize with the
formation ofhigh molecular weight and viscosity of aggregates by
hydrophobicity interaction and SH oxidation. The results showed
that protein concentration, pH, SH group and hydrophobicity all
effected the degree of aggregation and transparency of
thermalnon-coagulated egg white.
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