食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 食品化学 •    下一篇

生物解离大豆乳状液中蛋白质结构特征研究

王立敏1,陈思2,丁俭1,齐宝坤1,王中江1,江连洲1,隋晓楠1,李杨2   

  1. 1. 东北农业大学
    2. 东北农业大学食品学院
  • 收稿日期:2017-06-10 修回日期:2018-04-23 出版日期:2018-07-25 发布日期:2018-07-16
  • 通讯作者: 李杨 E-mail:liyanghuangyu@163.com
  • 基金资助:
    霍英东教育基金;国家重点研发计划项目;国家自然科学基金重点项目

The structure study on protein in emulsion formed during the enzyme-assisted aqueous extraction from soybean

, ,dingjian , , , , ,李杨 li yang   

  • Received:2017-06-10 Revised:2018-04-23 Online:2018-07-25 Published:2018-07-16
  • Contact: 李杨 li yang E-mail:liyanghuangyu@163.com

摘要: 乳状液破除是普及生物解离技术的重要途径,而具有特殊功能性质的乳状液蛋白质是乳状液失稳的关键因素。本试验以不同酶解时间(1、2、3h),不同酶添量(1%、2%)生物解离大豆过程中形成的乳状液蛋白质为研究对象,采用扫描电镜、EAI和ESI、表面疏水性、氨基酸分析及傅里叶红外光谱等表征乳状液蛋白/多肽表面性质及结构特征。结果显示:随着酶解的进行,乳状液中蛋白质由致密有序的网状结构变为疏松、多孔结构,EAI和ESI呈逐渐降低趋势;同时,疏水性氨基酸比例增多,表面疏水性(S0)下降,由于疏水性残基之间通过疏水相互作用发生聚集,对蛋白质的疏水区域产生屏蔽作用,导致S0下降;傅里叶红外光谱结果显示,随着酶解程度的增加,α-螺旋、β-折叠结构减少,无规则卷曲结构增加,表明酶解过程中引起的分子间作用力变化,导致乳状液蛋白质的构象变化。上述结果是酶解过程中乳状液失稳主要原因之一,为生物解离乳状液破乳机制提供理论支持。

关键词: 乳状液蛋白质, 表面疏水性, 氨基酸分析, 傅里叶红外光谱, 结构特征

Abstract: The study on emulsion demulsification is an important way to popularize the enzyme-assisted aqueous extraction, emulsion proteins with special functional properties is the key factors to demulsification. In this article, the emulsion protein formed during the enzyme-assisted aqueous extraction from soybean were studied under different enzymatic conditions (1, 2, 3h, 1% enzyme, 2% enzyme). The surface properties and structural characteristics of the emulsion protein / polypeptide were characterized by scanning electron microscopy, EAI and ESI, surface hydrophobicity (S0), amino acid analysis and Fourier transform infrared spectroscopy. The results showed that with the enzymatic hydrolysis continue, the emulsion protein changed from a dense and orderly network structure to a loose and holes structure, the EAI and ESI gradually decreased, at the same time, amino acid proportion increased and surface hydrophobicity (S0) decreased due to hydrophobic residues aggregated through the interaction between the hydrophobic interaction, which blocked the hydrophobic groups, resulting in S0 declined. Fourier transform infrared spectroscopy results showed that the α-helix, β-sheet structure reduced and the irregular structure increased with the increase of the degree of enzymatic hydrolysis, indicating that the changes of intermolecular force caused by the enzymatic hydrolysis lead to the conformational changes of protein in emulsion. The above results are one of the main reason of emulsion instability during enzymatic hydrolysis, which provides theoretical support for the mechanism of emulsion demulsification during the enzyme-assisted aqueous extraction.

Key words: emulsion protein, surface hydrophobicity (S0), amino acid analysis, Fourier transform infrared spectroscopy, structure characteristic

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