Structural basis for the functional properties of food Proteins

食品蛋白质功能特性的结构基础

• 批准号: 10460057
• 负责人: HIROSE Masaaki
• 金额: $ 10.24万
• 依托单位: KYOTO UNIVERSITY
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (B)
• 财政年份: 1998
• 资助国家: 日本
• 起止时间: 1998 至 1999
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-10460057/
• 关键词: food proteins; functional properties; ovalbumin; ovotransferrin; molecular structure; 機能持性; 食品蛋白質

Globular proteins assume different conformational states, namely the native, denatured, and molten-globule states. As model food proteins, we analyzed the mode of conformational transition of egg white ovalbumin and ovotransferrin and obtained the following results :1. About ovalbumin : the molten-globule state was formed during the refolding from the ureadenatured state as an intermediate and also in the disulfide-reduced state at acidic pH. Recombinant ovalbumin produced in E coli was found to assume essentially the same conformation as egg white ovalbumin but to lack the post-translational modification. According to the observation that the recombinant protein underwent the alkaline-dependent thermostabilization, the post-translational modification was not involved in the thermostabilization mechanism. An ovalbumin variant R339T was found to be transformed into a thermostabilized form following the cleavage at the P1-P1'site.2. About ovotransferrin : As a structural basis for the structural transition, crystal structure of the apo from of ovotransferrin was determined. Decreased formability of egg white following heat treatments was found to be due to the denaturation of ovotransferrin that can be minimized by addition of some anions.

球状蛋白呈现不同的构象状态，即天然状态、变性状态和熔球状态。作为模型食品蛋白，我们分析了蛋清卵清蛋白和卵转铁蛋白的构象转变模式，得到了以下结果： 1．关于卵清蛋白：熔球状态是在作为中间体的脲变性状态再折叠过程中形成的，并且在酸性pH下也以二硫化物还原状态形成。研究发现，大肠杆菌中产生的重组卵清蛋白具有与蛋清卵清蛋白基本相同的构象，但缺乏翻译后修饰。根据观察，重组蛋白经历了碱依赖性热稳定，翻译后修饰不参与热稳定机制。发现卵清蛋白变体R339T在P1-P1'位点裂解后转化为热稳定形式。2．关于卵转铁蛋白： 作为结构转变的结构基础，确定了卵转铁蛋白的apo晶体结构。发现热处理后蛋清的可成形性降低是由于卵转铁蛋白的变性，可以通过添加一些阴离子来最大程度地减少这种变性。

项目成果

H.Kurokawa: "Crysral structure of hen apo-ovotransferrin"The Journal of Biological Chemistry. 274. 28445-28452 (1999)

H.Kurokawa：“母鸡脱辅基卵转铁蛋白的晶体结构”《生物化学杂志》。

Honami Yamashita et al.: "Involvement of ovofransferns in the thermally induced gelation of egg white at around 65℃"Bioscience, Biotechnology, and Biochemistry. 62. 593-595 (1998)

Honami Yamashita 等：“卵清在 65℃ 左右热诱导凝胶化中的参与”生物科学、生物技术和生物化学 62. 593-595 (1998)。

K.Mizutani: "Crystal structure at 1.9A resolution of apo ovotransferrin N-lobe bound by suifate anions"Biochemistry. (印刷中). (2000)

K. Mizutani：“硫酸根阴离子结合的载脂蛋白卵转铁蛋白 N 叶的 1.9A 分辨率的晶体结构”（出版中）。

Mizutani,Kimihiko: "Crystal structure at 1.9A resolution of apoorotransferrin N-lobe bound by sulfate anions"Biochemistry. 39(12). 3258-3265 (2000)

Mizutani，Kimihiko：“硫酸根阴离子结合的脱辅铁转铁蛋白 N 叶的 1.9A 分辨率晶体结构”生物化学。

Y.Arii: "Structural properties of recombinant-oval bumin"Bioscience, Biotechnology, and Biochemistry. 63. 1392-1399 (1999)

Y.Arii：“重组卵形清蛋白的结构特性”生物科学、生物技术和生物化学。