Structural properties associated with the emulsifying functionality of parvalbumin isoforms

与小清蛋白亚型的乳化功能相关的结构特性

• 批准号: 07660260
• 负责人: KAWAI Yuji
• 金额: $ 0.32万
• 依托单位: HOKKAIDO UNIVERSITY
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 1995
• 资助国家: 日本
• 起止时间: 1995 至 1996
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-07660260/
• 关键词: parvalbumin; sarcoplasmic protein; carp; emulsifying property; disulfide bond; surface hydrophobicity; isoelectric point; 乳化活性; 脂肪結合能

Parvalbumin (PA) was separated from carp sarcoplasmic protein fraction with Sephadex G-75 chromatography. When dispersed with triolein, PA fraction had superior emulsifying properties to the other sarcoplasmic protein (Sp-P) fraction. Fat-binding capacity of PA fraction was higher at lower protein concentration. Surface hydrophobicity of PA fraction was significantly less than Sp-P fraction. Superiority of emulsifying activity in PA was suggested to be independent of hydrophobicity.Three isoforms (a, b, c) of PA were obtained with DEAE-Sephacel chromatography in order of the elution time. Emulsifying activity of isoform c was the highest in the PA isoforms (c>b>a). Intermolecular disulfide bond was formed between the molecules of the isoforms to induce dimerization by heating above 80ﾟC.The dimerization somewhat affected the emulsifying activity. EDTA also led the PA isoforms to vary their emulsifying activity, surface hydrophobicity and electrostatic property (isoelectric point). Changes in the structural and electrostatic states of PA related to Ca^<2+> might have markedly affected the emulsifying properties.

白细胞蛋白（PA）与Sephadex G-75色谱法与鲤鱼肌质蛋白分数分离。当散布三利核酸时，PA馏分具有优质的乳化性能，其特性比其他肌浆蛋白（SP-P）馏分具有优势。在较低的蛋白质浓度下，PA级分的脂肪结合能力更高。 PA馏分的表面疏水性明显小于SP-P级分。建议在PA中乳化活性的优势与疏水性无关。使用DEAE-Sephacel色谱法获得了PA的三种同工型（A，B，C），按照洗脱时间顺序获得。同工型C的乳化活性是PA同工型中最高的（C> B> A）。分子间二硫键在同工型的分子之间形成，以通过加热80℃。二聚化在某种程度上影响乳化活性。 EDTA还导致PA同工型改变其乳化活性，表面疏水性和静电特性（等电点）。与Ca^<2+>相关的PA的结构和静电状态的变化可能显着影响乳化性质。