Analysis of Raman Spectroscopy and Fluorescence Spectroscopy for Soy Protein Isolate during Vitro Simulated Digestion Process

被引：0

作者：

Li Y. ^{[1
,2
]}

Sun Y. ^{[1
]}

Zhao C. ^{[3
]}

Tan Z. ^{[1
]}

Qi B. ^{[1
,2
]}

机构：

[1] College of Food Science, Northeast Agricultural University, Harbin

[2] Harbin Food Industry Research Institute, Harbin

[3] College of Food Science and Engineering, Jilin Agricultural University, Changchun

来源：

Journal of Chinese Institute of Food Science and Technology | 2019年 / 19卷 / 02期

关键词：

Fluorescence spectroscopy; In vitro digestion; Raman spectroscopy; Soy protein isolate;

D O I：

10.16429/j.1009-7848.2019.02.034

中图分类号：

学科分类号：

摘要：

Raman spectroscopy and fluorescence spectroscopy of SPI during vitro simulated digestion process were analyzed by using pepsin in vitro digestion of soybean protein isolate (SPI) at 37℃ and pH of 1.2. The digestion degree of protein increased gradually with the extension of digestion time. However, the digestion rate of protein slowed down when digestion reaction time was more than 2 h. The digestion reaction could increase α-helix content and decrease β-sheet content, while β-turn content increased at first and then decreased. The changes of random coil content were irregular, however, random coil content increased slightly after digestion reaction for long time. The tyrosine and tryptophan residues tended to be'exposed' in the entire process of digestion, which was related to protein denaturation and unfolding of molecular structure. The digestion reaction was able to decrease fluorescence intensity of SPI and increase maximum absorption wavelength (λmax). The bathochromic-shift of λmax indicated that the degree of exposure for tryptophan residues increased and the tertiary structure of SPI became looser. In addition, the degree of bathochromic-shift of λmax for SPI digestion products increased with the extension of digestion time. © 2019, Editorial Office of Journal of CIFST. All right reserved.

引用

页码：266 / 272

页数：6

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