Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 67, Issue 50, Pages 13978-13985Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.9b05843
Keywords
soy protein isolate; oxidation; in vitro digestion; FRAP; pepsin diffusivity
Funding
- National Natural Science Foundation of China [31671870]
- Pearl River S&T Nova Program of Guangzhou [201610010105]
- Science and Technology Program of Guangzhou [201807010102]
- Special Support Project of Guangdong Province for Science and Technology Innovative Young Talents [2014TQ01N538]
- 111 Project [B17018]
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Protein oxidation results in structural modification which affects its digestion. The objective of this work was to investigate the influence of lipoxygenases (LOX) catalyzed linoleic acid (LA) oxidation on the structure and in vitro gastric digests of soybean protein isolate (SPI). Fluorescence recovery after photobleaching (FRAP) was used to evaluate the relationship between pepsin diffusion and gastric digestion. Results indicated that oxidation induced carbonyl formation and loss of free sulfhydryl. Increased surface hydrophobicity and zeta-potential verified the protein unfolding and thus resulted in a small particle size and low fluorescence intensity. Fourier transform infrared spectroscopy (FTIR) showed that oxidation caused the increases in beta-sheets mostly at the expense of alpha-helix and random coils. Fluorescein isothiocyanate (FITC)-pepsin in SPI solution modified with 3 mL LA showed a faster diffusion rate with 80.51 mu m(2)/s as well as a higher DH value of 9.11%, showing that pepsin diffusivity might play an important role in protein gastric digestion.
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