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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
  • 27 Downloads

Abstract

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.

Keywords

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

Notes

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).

References

  1. Akishev, Y. S., et al. (2006). Generation of a nonequilibrium plasma in heterophase atmospheric-pressure gas-liquid media and demonstration of its sterilization ability. Plasma Physics Reports, 32(12), 1052–1061.CrossRefGoogle Scholar
  2. Bandekar, J. (1992). Amide modes and protein conformation. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1120(2), 123–143.CrossRefGoogle Scholar
  3. Beveridge, T., et al. (2010). Determination of SH-and SS-groups in some food proteins using Ellman’s reagent. Journal of Food Science, 39(1), 49–51.CrossRefGoogle Scholar
  4. Cheng, S. Y., et al. (2010). Influence of atmospheric pressure plasma treatment on various fibrous materials: performance properties and surface adhesion analysis. Vacuum, 84(12), 1466–1470.CrossRefGoogle Scholar
  5. Dalsgaard, T. K., et al. (2007). Changes in structures of milk proteins upon photo-oxidation. Journal of Agricultural & Food Chemistry, 55(26), 68–76.CrossRefGoogle Scholar
  6. Dong, S., et al. (2018). Surface modification via atmospheric cold plasma (ACP): improved functional properties and characterization of zein film. Industrial Crops and Products, 115, 124–133.CrossRefGoogle Scholar
  7. Fahmy, H. M., et al. (2018). Effect of cold plasma on the bilayer lipid membrane. Journal of Bionanoscience, 12(2), 233–239.CrossRefGoogle Scholar
  8. Govindaraju, K., & Srinivas, H. (2006). Studies on the effects of enzymatic hydrolysis on functional and physico-chemical properties of arachin. LWT - Food Science and Technology, 39(1), 54–62.CrossRefGoogle Scholar
  9. Guo, H., et al. (2015). Localized etching of polymer films using an atmospheric pressure air microplasma jet. Journal of Micromechanics & Microengineering, 25(1), 015010.CrossRefGoogle Scholar
  10. Haskard, C. A., & Li-Chan, E. C. Y. (1998). Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANSÀ) fluorescent probes. Journal of Agricultural & Food Chemistry, 46, 2671–2677.CrossRefGoogle Scholar
  11. He, X. H., et al. (2014). Effects of high pressure on the physicochemical and functional properties of peanut protein isolates. Food Hydrocolloids, 36(5), 123–129.CrossRefGoogle Scholar
  12. Hullberg, A., & Bertram, H. C. (2005). Relationships between sensory perception and water distribution determined by low-field NMR T2 relaxation in processed pork--impact of tumbling and RN- allele. Meat Science, 69(4), 709–720.PubMedCrossRefPubMedCentralGoogle Scholar
  13. Ji, H., et al. (2018). Effects of dielectric barrier discharge (DBD) cold plasma treatment on physicochemical and functional properties of peanut protein. Food & Bioprocess Technology, 11(2), 344–354.CrossRefGoogle Scholar
  14. Kong, B., & Xiong, Y. L. (2006). Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action. Journal of Agricultural & Food Chemistry, 54(16), 6059–6068.CrossRefGoogle Scholar
  15. Lakemond, C. M. M., et al. (2003). Gelation of soy glycinin; influence of pH and ionic strength on network structure in relation to protein conformation. Food Hydrocolloids, 17(3), 365–377.CrossRefGoogle Scholar
  16. Li, C., et al. (2013). Physicochemical properties of dry-heated peanut protein isolate conjugated with dextran or gum Arabic. Journal of the American Oil Chemists Society, 90(12), 1801–1807.CrossRefGoogle Scholar
  17. Li, T., et al. (2014). Water distribution in tofu and application of T2 relaxation measurements in determination of tofu’s water-holding capacity. Journal of Agricultural & Food Chemistry, 62(34), 8594–8601.CrossRefGoogle Scholar
  18. Lii, C. Y., et al. (2002). Behaviour of granular starches in low-pressure glow plasma. Carbohydrate Polymers, 49(4), 499–507.CrossRefGoogle Scholar
  19. Lin, W. J., et al. (2015). Effect of glycosylation with xylose on the mechanical properties and water solubility of peanut protein films. Journal of Food Science &Technology, 52(10), 6242–6253.CrossRefGoogle Scholar
  20. Liu, W., et al. (2010). The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin. Food Chemistry, 123(3), 616–621.CrossRefGoogle Scholar
  21. Ma, T., et al. (2017). Influence of extraction and solubilizing treatments on the molecular structure and functional properties of peanut protein. LWT - Food Science and Technology, 79, 197–204.CrossRefGoogle Scholar
  22. Matsumiya, K., et al. (2017). Protein-surfactant interactions between bovine lactoferrin and sophorolipids under neutral and acidic conditions. Biochemistry and Cell Biology, 95(1), 126–132.PubMedCrossRefPubMedCentralGoogle Scholar
  23. Misra, N. N., et al. (2015). Atmospheric pressure cold plasma (ACP) treatment of wheat flour. Food Hydrocolloids, 44, 115–121.CrossRefGoogle Scholar
  24. Neucere, N. J., & Conkerton, E. J. (1978). Some physicochemical properties of peanut protein isolates. Journal of Agricultural & Food Chemistry, 26(3), 683–690.CrossRefGoogle Scholar
  25. OchoaRivas, et al. (2017). Microwave and ultrasound to enhance protein extraction from peanut flour under alkaline conditions: effects in yield and functional properties of protein isolates. Food & Bioprocess Technology, 10(3), 1–13.Google Scholar
  26. Pelton, J. T., & McLean, L. R. (2000). Spectroscopic methods for analysis of protein secondary structure. Analytical Biochemistry, 277(2), 167–176.PubMedCrossRefPubMedCentralGoogle Scholar
  27. Piemontese, L., et al. (2017). Effect of gaseous ozone treatments on DON, microbial contaminants and technological parameters of wheat and semolina. Food Additives & Contaminants Part A, 35(4), 760–771.Google Scholar
  28. Prakash, V., & Rao, M. S. (1986). Physicochemical properties of oilseed proteins. Crc Critical Reviews in Biochemistry, 20(3), 265–363.PubMedCrossRefPubMedCentralGoogle Scholar
  29. Qin, P., et al. (2012). Probing the binding of two fluoroquinolones to lysozyme: a combined spectroscopic and docking study. Molecular Biosystems, 8(4), 1222–1229.PubMedCrossRefPubMedCentralGoogle Scholar
  30. Saul, R.,. T., et al. (2007). Increasing protein conformational stability by optimizing beta-turn sequence. Journal of molecular biology, 373(1), 211–218.PubMedPubMedCentralCrossRefGoogle Scholar
  31. Schmidt, V., et al. (2005). Thermal stability of films formed by soy protein isolate–sodium dodecyl sulfate. Polymer Degradation and Stability, 87(1), 25–31.CrossRefGoogle Scholar
  32. Segat, A., et al. (2015). Atmospheric pressure cold plasma (ACP) treatment of whey protein isolate model solution. Innovative Food Science & Emerging Technologies, 29, 247–254.CrossRefGoogle Scholar
  33. Shen, L., & Tang, C.-H. (2012). Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Research International, 48(1), 108–118.CrossRefGoogle Scholar
  34. Shuang, D., et al. (2017). Effects of dielectric barrier discharges (DBD) cold plasma treatment on physicochemical and structural properties of zein powders. Food & Bioprocess Technology, 10(3), 434–444.CrossRefGoogle Scholar
  35. Sinha, E. (2009). Effect of cold plasma treatment on macromolecular structure, thermal and mechanical behavior of jute fiber. Journal of Industrial Textiles, 38(4), 317–339.CrossRefGoogle Scholar
  36. Sun, C., et al. (2016). Effect of heat treatment on physical, structural, thermal and morphological characteristics of zein in ethanol-water solution. Food Hydrocolloids, 58, 11–19.CrossRefGoogle Scholar
  37. Tabassum, S., et al. (2012). Interaction and photo-induced cleavage studies of a copper based chemotherapeutic drug with human serum albumin: spectroscopic and molecular docking study. Molecular Biosystems, 8(9), 2424–2433.PubMedCrossRefPubMedCentralGoogle Scholar
  38. Takai, E., et al. (2012). Protein inactivation by low-temperature atmospheric pressure plasma in aqueous solution. Plasma Processes & Polymers, 9(1), 77–82.CrossRefGoogle Scholar
  39. Terpiłowski, K., et al. (2017). Surface properties of ion-inducted whey protein gels deposited on cold plasma treated support. Food Hydrocolloids, 71, 17–25.CrossRefGoogle Scholar
  40. Tipa, R. S., & Kroesen, G. M. W. (2011). Plasma-stimulated wound healing. IEEE Transactions on Plasma Science, 39(11), 2978–2979.CrossRefGoogle Scholar
  41. Wan, Z., et al. (2017). High voltage atmospheric cold plasma treatment of refrigerated chicken eggs for control of Salmonella enteritidis contamination on egg shell. LWT - Food Science and Technology, 76, 124–130.CrossRefGoogle Scholar
  42. Wang, X., et al. (2012). Application of glow discharge plasma for wastewater treatment. Electrochimica Acta, 83, 501–512.CrossRefGoogle Scholar
  43. Wang, T., et al. (2015). Mechanistic insights into solubilization of rice protein isolates by freeze–milling combined with alkali pretreatment. Food Chemistry, 178, 82–88.PubMedCrossRefPubMedCentralGoogle Scholar
  44. Yu, J., et al. (2007). Peanut protein concentrate: production and functional properties as affected by processing. Food Chemistry, 103(1), 121–129.CrossRefGoogle Scholar
  45. Yu, L., et al. (2015). Preparation, characterisation and physicochemical properties of the phosphate modified peanut protein obtained from Arachin conarachin L. Food Chemistry, 170(1), 169–179.PubMedCrossRefPubMedCentralGoogle Scholar
  46. Zhao, G., et al. (2011). Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry, 127(4), 1438–1443.CrossRefGoogle Scholar

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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