Behavioral Solubilization of Peanut Protein Isolate by Atmospheric Pressure Cold Plasma (ACP) Treatment

  • Hui JiEmail author
  • Fei Han
  • Shanli Peng
  • Jiaojiao Yu
  • Ling Li
  • Yunguo Liu
  • Yue Chen
  • Shuhong Li
  • Ye ChenEmail author
Original Paper


The solubilization of peanut protein isolate (PPI) powders modified by atmospheric pressure cold plasma (ACP) treatment was studied by scanning electron microscopy (SEM), energy dispersive X-ray spectroscopy (EDS), low-field nuclear magnetic resonance (low-field NMR) spectroscopy, and FTIR spectroscopy. Significant improvements in both the solubility and water holding capacity (WHC) of the PPI gel were observed after treatment with ACP. The PPI solubility reached a maximum value after 7 min of treatment, with a 12.17% increase over the values observed for the untreated samples. In addition, the WHC increased by 17.90% after 3 min of treatment. The SEM and EDS data revealed that following the 7-min treatment, the PPI surface was rougher and more loosely bound than that of the untreated sample. This indicated an increase in the PPI specific surface area and exposed protein–water binding sites on the treated PPI surface as well as a marked increase in its oxygen content, suggesting an increase in the hydrophilic groups on the PPI surface. The low-filed NMR measurements revealed that the trend in the T21 peak area of the relaxation time was consistent with the data observed for the WHC. The FTIR results revealed a decrease in the proportion of β-sheets and an increase in that of the β-turns within 3 min of treatment, suggesting that the polarity and hydrophilicity of the protein surface were enhanced. The protein structure changed from a compact folding to a loose unfolding configuration after ACP treatment.


Atmospheric cold plasma Peanut protein isolate powders Solubility Energy dispersive spectroscopy Low-field NMR 


Funding Information

This study was supported by National Science Foundation for Youth of China (Grant Nos. 31501503 and 31701526) and the National Science Foundation of China0020(Grant No. 31560719).


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.College of Life Science and BiotechnologyLinyi UniversityLinyiChina
  2. 2.Chinese Medicine HospitalLinyiChina
  3. 3.Linyi UniversityLinyiChina
  4. 4.Tianjin University of Science and TechnologyTianjinChina
  5. 5.Key Laboratory of Food Nutrition and Safety, Ministry of Education; College of Food Engineering and BiotechnologyTianjin University of Science and TechnologyTianjinChina

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