食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 食品化学 •    下一篇

氧化对大豆蛋白结构、乳液稳定性及消化特性的影响研究

沈鹏辉,樊诗堃,赵谋明,周非白   

  1. 华南理工大学
  • 收稿日期:2018-06-07 修回日期:2019-04-19 出版日期:2019-07-25 发布日期:2019-07-23
  • 通讯作者: 樊诗堃 E-mail:fskfate@163.com
  • 基金资助:
    国家自然科学基金青年科学基金项目

Influence of oxidation on soy protein structure,emulsion stability and lipid digestion

, ,Mou-Ming Mou-MingZHAO,Fei-Bai ZHOU   

  • Received:2018-06-07 Revised:2019-04-19 Online:2019-07-25 Published:2019-07-23

摘要: 本文以大豆分离蛋白(soy protein isolate,SPI)为原料,以脂质过氧化产物丙二醛(malondialdehyde,MDA)为氧化引发剂,逐级研究了氧化对大豆蛋白结构、乳液稳定性及乳液消化特性的影响。结果发现:随着MDA浓度的升高,蛋白羰基及席夫碱含量明显升高而巯基含量显著降低。同时,MDA可促进蛋白聚集并诱导β-伴大豆球蛋白(7S)组分形成二硫键和非二硫键诱导的共价交联。进一步制备O/W型乳液,发现不同浓度MDA处理蛋白对乳液的形成影响较小,但可以显著改变界面蛋白组成。其中经中高浓度(2.5-10 mmol/L)MDA氧化后,更多7S组分以聚集状态参与界面组成。体外模拟胃肠道消化实验进一步表明,乳液消化主要在肠道进行,氧化诱导的蛋白交联/聚集可延缓或降低胆盐在界面的替代,进而减缓乳液消化并降低脂质消化率。

关键词: 大豆分离蛋白, 丙二醛(malondialdehyde, MDA), 蛋白氧化, 乳液, 模拟消化

Abstract: In this study, malondialdehyde (MDA), a natural lipid peroxidation product, was used as an initiator to investigate the influence of MDA-induced protein structural modifications on stability and digestibility of emulsion stabilized by soy protein isolate (SPI). Results obtained showed that the content of protein carbonyl and Schiff base significantly increased along with increasing MDA concentrations, accompanied by a noticeable decrease in sulfhydryl group. Meanwhile, MDA promoted protein aggregation through disulfide/non-disulfide covalent bond, where β-conglycinin (7S) components were mainly involved in the latter case. O/W emulsion was further prepared from oxidatively treated SPI. It was found that MDA-induced protein oxidation has less influence on emulsion formation, but they could significantly alter the composition of protein at interface. Herein, for SPI treated with MDA above 2.5 mM, more fractions from 7S participated in interface formation in aggregated state. Results from in-vitro simulated gastrointestinal digestion further demonstrated that emulsion digestion occurs mainly in the intestinal tract, and oxidation-induced cross-linking/aggregation of proteins can delay or reduce the replacement of bile salts at the interface, which in turn slowed emulsion digestion and decreased lipid digestibility.

Key words: soy protein isolate (SPI), malondialdehyde (MDA), protein oxidation, emulsion, simulated digestion

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