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Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
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Effect of Freezing on Soybean Protein Solution.
Wenhui Li1, Qiongling Chen1, Xiaowen Wang1
1College of Food Science and Engineering, Shanxi Agricultural University, Jinzhong 030801, China.
Foods (Basel, Switzerland)
|July 29, 2023
Summary
Frozen storage alters soybean protein properties. Extended freezing decreases solubility and sulfhydryl content, increases hydrophobicity and aggregation, and changes protein structure due to ice crystal formation.
Area of Science:
- Food Science
- Protein Chemistry
- Biophysics
Background:
- Soybean proteins are vital food components.
- Understanding freezing effects on protein structure is crucial for food processing and storage.
- Soybean isolate (SPI), 7S, and 11S globulins are key soybean protein fractions.
Purpose of the Study:
- To investigate how frozen storage impacts soybean protein physicochemical properties.
- To elucidate the mechanisms behind these changes.
Main Methods:
- Soybean protein solutions (SPI, 7S, 11S) were frozen for 1 and 5 days.
- Assessed protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interactions.
- Utilized UV spectrophotometry, Zeta potential, SDS-PAGE, FTIR, and fluorescence spectroscopy.
Main Results:
- Solubility and sulfhydryl content decreased with longer freezing times, with 11S affected most.
- Freezing increased protein hydrophobicity, aggregation, and particle size, shifting structure towards order.
- Protein microenvironment polarity increased, with red-shifted fluorescence emission spectra.
- Hydrogen bonding contribution increased, while hydrophobic interactions decreased.
Conclusions:
- Frozen storage significantly alters soybean protein structure and properties.
- Ice crystal growth causes protein unfolding, hydrophobic group exposure, and secondary structure modification.
- Changes in chemical forces, including hydrogen bonding and hydrophobic interactions, are key mechanisms.

