高压均质对大豆β-伴球蛋白结构及功能特性的影响

食品科学 ›› 0, Vol. ›› Issue (): 83-87.

高压均质对大豆β-伴球蛋白结构及功能特性的影响

郭丽，王鹏，赵东江，王广慧，周凤超，马雪

绥化学院生物与食品工程学院

收稿日期:2011-05-17 修回日期:2011-09-26 出版日期:2011-10-15 发布日期:2011-10-12
通讯作者: 郭丽 E-mail:guoli2138@163.com
基金资助:
黑龙江省教育厅科学技术研究项目

Effect of High-pressure Homogenization on Structure and Functional Properties of Soybean β-Conglycinin

Received:2011-05-17 Revised:2011-09-26 Online:2011-10-15 Published:2011-10-12

摘要/Abstract

摘要： 使用差示扫描量热仪、扫描电镜和傅里叶变换红外光谱仪研究高压均质后大豆β-伴球蛋白的结构和功能特性。结果表明：大豆β-伴球蛋白的变性温度为(74±1)℃，高压均质后大豆β-伴球蛋白粒径明显变小，经20MPa和30MPa均质处理后，大豆β-伴球蛋白结构发生了明显变化。高压均质可有效提高大豆β-伴球蛋白溶解性、乳化活性和乳化稳定性，并降低乳析率。经20MPa和35MPa压力处理的大豆β-伴球蛋白的保水性明显提高，经25MPa和30MPa压力处理的大豆β-伴球蛋白的持油性明显提高。

关键词: 大豆β-伴球蛋白, 高压均质, 结构, 功能特性

Abstract: The structure and functional properties of high-pressure homogenized β-conglycinin were investigated by differential scanning calorimetry (DSC), scanning electron microscope (SEM) and Fourier transform infrared spectroscopy (FTIR). The denaturation temperature of the β-conglycinin was determined by DSC to be (74 ± 1) ℃. The particle size of the protein after high-pressure homogenization became much smaller. FTIR spectroscopy showed the protein structure was changed significantly after homogenization at 20 MPa and 30 MPa. Moreover, the protein exhibited a high solubility, emulsifying activity and emulsion stability and low whey precipitation after homogenization. The β-conglycinin revealed an increase of its water-holding capacity at the pressure levels of 20 MPa and 35 MPa, and an enhanced oil-holding capacity at 25 MPa and 30 MPa of homogenization pressure.

Key words: soybean β-conglycinin, high-pressure homogenization, structure, functional properties

中图分类号:

TS201.1

郭丽，王鹏，赵东江，王广慧，周凤超，马雪 . 高压均质对大豆β-伴球蛋白结构及功能特性的影响[J]. 食品科学, 0, (): 83-87.

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