Basic Studies on the Functional Properties and Physiological Properties of Egg Proteins.

从分子的角度研究了鸡蛋蛋白的功能特性和生理特性。各研究总结如下：1。低密度脂蛋白的乳化特性：从蛋黄中分离低密度脂蛋白，研究其乳化特性。低密度脂蛋白具有很高的乳化活性，主要取决于其特有的脂-蛋白复合物结构。作为本研究的应用，通过与大豆卵磷脂形成络合物，改善了一些乳化性能较差的蛋白质。溶菌酶的成胶特性：在通常的加热条件下，溶菌酶不会成胶，但加入适量的还原剂可以改变溶菌酶的这一特性，在少量盐的存在下，溶菌酶会形成发育良好的凝胶。在这种情况下，还原剂的用量是关键，大量的还原剂不会形成凝胶。卵泡样液的致敏活性：卵泡样液的碳水化合物部分与从鸡蛋过敏患者获得的IgE抗体发生强烈反应。化学脱糖也可大大降低卵黏液样物质的过敏活性。此外，为了降低类卵粘液的抗原性，在不同条件下研究了热处理和消化酶消化对类卵粘液的影响。酶消化卵清蛋白的抗原性：从胰酶消化的卵清蛋白中分离出具有强抗原性的高分子量组分（Mol. Wt. Ca 24000）。在先前在胃中注射卵清蛋白的小鼠的小肠内容物中检测到相同的分数。

Both functional properties and physiological properties of egg proteins were studied from the molecular point of view. Summaries of each study are as follows;1. Emulsifying properties of low density lipoprotein: Low density lipoprotein was separated from egg yolk and its emulsifying properties were studied. The emulsifying activity of low density lipoprotein was very high and was shown to be mostly depended on its characteristic lipid-protein complex structrure. As the application of this study, improvement was made about some proteins having low emulsifying properties by the complex formation with soy lecithin.2. Gel-forming properties of lysozyme: Lysozyme has been shown not to be gelled under usual heating condition, but addition of adequate amount of reducing agents could change this property of lysozyme and geve well-developed gel in the presence of small smount of salt. In this case, the amount of reducing agent was critical and gel formation was not occurred with large amount of reducing agent.3. Allergenic activity of ovomucoid: Carbohydrate moiety of ovomucoid was shown to srongly react with IgE antibody obtained from the patient of egg ellergy. Allergic Activity of ovomucoid was also shown to be greatly reduced by chemical desugaring. Furthermore, to reduce the antigenicity of ovomucoid, the effects of both heat treatment and peptic digestion were studied under various conditions.4. Antigenicity of enzymatically digested ovalbumin: A high-molecular weight fraction (Mol. Wt. Ca 24,000) having a strong antigenicity was isolated from ovalbumin digested with pancreatin. Same fraction was detected in the contents of small intestine about the rets to which ovalbumin was previously injected in the stomach.