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Effects of different pH on the physicochemical properties of Solanum tuberosum L. protein
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Jia-Qi LI, Yi-Ming LEI, Sheng-Yun BI, Qiong-Ling CHEN, Zhen-Jia CHEN*
Journal of Food Safety & Quality | 2025, 16(5) : 246 - 254
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Journal of Food Safety & Quality | 2025, 16(5): 246-254
Food Analysis and Detection
Effects of different pH on the physicochemical properties of Solanum tuberosum L. protein
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Jia-Qi LI, Yi-Ming LEI, Sheng-Yun BI, Qiong-Ling CHEN, Zhen-Jia CHEN*
Affiliations
  • College of Food Science and Engineering, Shanxi Agricultural University, Jinzhong 030801, China
Published: 2025-03-15 doi: 10.19812/j.cnki.jfsq11-5956/ts.20241112005
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Objective To elucidate the influence of pH treatment on the structural and functional properties of Solanum tuberosum L. protein. Methods Solanum tuberosum L. protein was selected as the research subject, and the effects of pH on its physical and chemical properties, structure, and conformation were analyzed by fluorescence spectroscopy, Fourier transform infrared spectroscopy, particle size and potential analysis, and scanning electron microscopy. Results Significant differences were observed in the protein subunit composition, particle size distribution, and potential values following treatments at different pH levels. Compared to pH 7, pH 10 enhanced the electrostatic repulsion of Solanum tuberosum L. proteins, significantly increasing protein solubility and viscosity to 89.2% and 19625.0 mPa·s, respectively. Additionally, λmax in the endogenous fluorescence spectra of the proteins shifted to 343 nm, exposing more hydrophobic groups. The particle size of protein molecules decreased to 123.2 nm, while the absolute value of the Zeta potential increased to 41.3 mV. Protein molecules formed intramolecular disulfide bonds, leading to an increase in the denaturation temperature to 82.22 ℃. At pH 2, the protein aggregated and formed soluble aggregates while unfolding. However, viscosity decreased to 1860.6 mPa·s, λmax in the fluorescence spectrum shifted to 341 nm, particle size increased to 369.3 nm, the absolute value of the Zeta potential decreased to 8.97 mV, and the number of disulfide bonds did not change significantly. This resulted in insufficient stability of Solanum tuberosum L. protein under acidic conditions, with a tendency for aggregation. Conclusion Different pH treatments can enhance the physicochemical properties of Solanum tuberosum L. protein, and this study aims to offer scientific guidance for its application in food processing.

Solanum tuberosum L. protein  /  pH  /  hydrophobicity  /  aggregation  /  subunit composition
Jia-Qi LI, Yi-Ming LEI, Sheng-Yun BI, Qiong-Ling CHEN, Zhen-Jia CHEN. Effects of different pH on the physicochemical properties of Solanum tuberosum L. protein[J]. Journal of Food Safety & Quality, 2025 , 16 (5) : 246 -254 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20241112005
Year 2025 volume 16 Issue 5
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Article Info
doi: 10.19812/j.cnki.jfsq11-5956/ts.20241112005
  • Receive Date:2024-11-12
  • Online Date:2025-07-19
  • Published:2025-03-15
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  • Received:2024-11-12
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    College of Food Science and Engineering, Shanxi Agricultural University, Jinzhong 030801, China
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表12种不同金属材料的力学参数

Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)

Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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