Skip to main content
SpringerLink
Log in

Effects of Dielectric Barrier Discharge (DBD) Cold Plasma Treatment on Physicochemical and Functional Properties of Peanut Protein

  • Published:
Food and Bioprocess Technology Aims and scope Submit manuscript

Abstract

Peanut protein isolate (PPI) solutions were modified by dielectric barrier discharge (DBD) cold plasma (CP) treatment. Effects of CP treatment on the solubility, emulsion stability, and water holding capacity (WHC) of peanut protein were studied. The results showed a significant improvement in solubility, emulsion stability, and WHC following CP treatment. CP treatment resulted in the unfolding of PPI structure, thereby increasing the β-sheet and random coil content and decreasing the α-helix and β-turn content, as analyzed by Fourier-transform infrared spectroscopy. Low-field nuclear magnetic resonance showed an increase in the peak area of T 21 relaxation time by CP treatment and the change in T 21 peak area was in agreement with the result of WHC. This study demonstrated that CP may be successfully applied as a method to modify the functionality of PPI.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

References

  • Attri, P., et al. (2013). Utility of plasma: a new road from physics to chemistry. RSC Advances, 3(31), 12540–12567.

    Article  CAS  Google Scholar 

  • Bertram, H. C., et al. (2002). Continuous distribution analysis of T2, relaxation in meat—an approach in the determination of water-holding capacity. Meat Science, 60(3), 279.

    Article  Google Scholar 

  • Beveridge, T., et al. (1974). Determination of SH- and SS-groups in some food proteins using Ellman’s reagent. Journal of Food Science, 39(1), 49–51.

    Article  CAS  Google Scholar 

  • Bianchi-Hall, C. M., et al. (1993). Diversity of seed storage protein patterns in wild peanut (Arachis, Fabaceae) species. Plant Systematics and Evolution, 186(1–2), 1–15.

    Article  CAS  Google Scholar 

  • Boye, J. I., Alli, I., & Ismail, A. A. (1996). Interactions involved in the gelation of bovine serum albumin. Journal of Agricultural and Food Chemistry., 44(4), 996–1004.

    Article  CAS  Google Scholar 

  • Caessens, P. W., et al. (1999). The adsorption-induced secondary structure of beta-casein and of distinct parts of its sequence in relation to foam and emulsion properties. Biochimica et Biophysica Acta, 1430(1), 73.

    Article  CAS  Google Scholar 

  • Cataldo, F. (2003). On the action of ozone on proteins. Polymer Degradation & Stability, 82(1), 105–114.

    Article  CAS  Google Scholar 

  • Daussant, J., et al. (1969). Immunochemical studies on arachis hypogaea proteins with particular reference to the reserve proteins. I. Characterization, distribution, and properties of α-arachin and α-conarachin. Plant Physiology, 44(4), 471.

    Article  CAS  Google Scholar 

  • Davies, M. J. (2005). The oxidative environment and protein damage. Biochimica et Biophysica Acta, 1703, 93.

    Article  CAS  Google Scholar 

  • Dong, S., 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.

    Article  CAS  Google Scholar 

  • Donovan, J. W., & Beardslee, R. A. (1975). Heat stabilization produced by protein-protein association. A differential scanning calorimetric study of the heat denaturation of the trypsin-soybean trypsin inhibitor and trypsin-ovomucoid complexes. Journal of Biological Chemistry, 250(6).

  • Durand, A., et al. (2003). Particle sizes and stability of the bovine, cereal and grain milks. Food Hydrocolloids, 17(5), 671–678.

    Article  CAS  Google Scholar 

  • Eaton, P. (2006). Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radical Biology and Medicine, 40(11), 1889–1899.

    Article  CAS  Google Scholar 

  • Ellman, G. D. (1959). Tissue sulfhydryl groups. Archives Biochemistry Biophysics, 82, 70–72.

    Article  CAS  Google Scholar 

  • Gianferri, R., et al. (2007). A low-resolution and high-resolution nuclear magnetic resonance integrated approach to investigate the physical structure and metabolic profile of Mozzarella di Bufala Campana cheese. International Dairy Journal, 17, 167–176.

    Article  CAS  Google Scholar 

  • Haris, P. I., & Severcan, F. (1999). FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. Journal of Molecular Catalysis B Enzymatic, 7, 207–221.

    Article  CAS  Google Scholar 

  • 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. J. Agric Food Chemistry, 46, 2671–2677.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Hoying, L., et al. (2008). Study of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry. Food Research Internationa, 41(7), 720–729.

    Article  Google Scholar 

  • J. M. Berg, J. L. Tymoczko and L. (2001). Stryer, Biochemistry, W. H. Freeman and Company. New York, p. 84.

  • Kim, J. E., et al. (2014). Microbial decontamination of red pepper powder by cold plasma. Food Microbiology, 38, 128.

    Article  CAS  Google Scholar 

  • Kim, S., et al. (2004). Characterization of zein modified with a mild cross-linking agent. Industrial Crops and Products, 20(3), 291–300.

    Article  CAS  Google Scholar 

  • Kocher, P. N., & Foegeding, E. A. (1993). Microcentrifuge-based method for measuring water-holding of protein gels. Journal of Food Science, 58, 1040–1046.

    Article  CAS  Google Scholar 

  • Kong, B., & Xiong, Y. L. (2006). Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action. Journal of Agricultural and Food Chemistry, 54(16), 6059–6068.

    Article  CAS  Google Scholar 

  • Kurganov, B. I., et al. (1997). Analysis of differential scanning calorimetry data for proteins. Criteria of validity of one-step mechanism of irreversible protein denaturation. Biophysical Chemistry, 69(2–3), 125–135.

    Article  CAS  Google Scholar 

  • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.

    Article  CAS  Google Scholar 

  • 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(8), 594–601.

    Google Scholar 

  • Lu, M., et al. (2002). Differential scanning calorimetric and circular dichroistic studies on plant antifreeze proteins. Journal of Thermal Analysis and Calorimetry, 67(3), 689–698.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Wiśniewska, M., et al. (2013). Effect of solution pH on the stability of mixed silica-alumina suspension in the presence of polyacrylic acid (PAA) with different molecular weights. Central European Journal of Chemistry, 11, 101–110.

    Article  Google Scholar 

  • Molina, E., et al. (2002). Soy protein pressure-induced gels. Food Hydrocolloids 16:625–632.

  • Monteiro, et al. (1994). Effect of proteases on arachin, conarachin I, and conarachin II from peanut (Arachis hypogaea L.) Journal of Agricultural and Food Chemistry, 42, 268–273.

    Article  Google Scholar 

  • Ochoa-Rivas, A., et al. (2016). 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, 1–13.

  • Mu, L., et al. (2010). Effect of ultrasonic treatment on the graft reaction between soy protein isolate and gum acacia and on the physicochemical properties of conjugates. Journal of Agricultural & Food Chemistry, 58(7), 4494.

    Article  CAS  Google Scholar 

  • Oehmigen, K., et al. (2010). The role of acidification for antimicrobial activity of atmospheric pressure plasma in liquids. Plasma Processes and Polymers, 7(3–4), 250–257.

    Article  CAS  Google Scholar 

  • Offer, G., & Knight, P. (1988). Structural basis of water-holding in meat. 1. General principles and water uptake in meat processing. Developments in Meat Science.

  • Raemy, A. (2003). Behavior of foods studied by thermal analysis: introduction. Journal of Thermal Analysis and Calorimetry, 71(1), 273–278.

    Article  CAS  Google Scholar 

  • Relkin, P. (1994). Differential scanning calorimetry: a useful tool for studying protein denaturation. Thermochimica Acta, 246(2), 371–386.

    Article  CAS  Google Scholar 

  • Segat, A., et al. (2014). Effects of ozone processing on chemical, structural and functional properties of whey protein isolate. Food Research International, 66, 365–372.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Thorarinsdottir, K. A., et al. (2002). Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry. Food Chemistry, 77, 377–385.

    Article  CAS  Google Scholar 

  • Traylor, M. J., et al. (2011). Long-term antibacterial efficacy of air plasma-activated water. Journal of Physics D: Applied Physics, 44(47), 472001.

    Article  Google Scholar 

  • Wang, S. F., and Smith, D. M. (1994). Poultry muscle proteins and heat-induced gelation. Poultry Science Reviews.

  • Wang, Z., et al. (2014). Relationship between secondary structure and surface hydrophobicity of soybean protein isolate subjected to heat treatment. Journal of Chemistry, 2014(5), 1–10.

    Google Scholar 

  • Wisniewska, M. (2010). Influences of polyacrylic acid adsorption and temperature on the alumina suspension stability. Powder Technology, 198(2), 258–266.

    Article  CAS  Google Scholar 

  • Wu, H., et al. (2009). Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Research International, 42(3), 343–348.

    Article  CAS  Google Scholar 

  • Yamada, T., et al. (1979). Isolation and some properties of arachin subunits. Agricultural and Biological Chemistry, 43, 2563.

    CAS  Google Scholar 

  • Yang, H., et al. (2015). Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy. Nature Protocols, 10, 382–396.

    Article  CAS  Google Scholar 

  • Yu, J. M., et al. (2007). Peanut protein concentrate: production and functional properties as affected by processing. Food Chemistry, 103(1), 121–129.

    Article  CAS  Google Scholar 

  • Zhang, Q. T., et al. (2014). Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate. Food & Bioproducts Processing, 92(1), 30–37.

    Article  CAS  Google Scholar 

  • Zhao, G. L., et al. (2011). Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry, 127(4), 1438–1443.

    Article  CAS  Google Scholar 

Download references

Funding

This research was financially supported by the National Science Foundation of China (Grant Nos. 31271974 and 31501503) and Tianjin Food Safety and Low Carbon Manufacturing Collaborative Innovation Center.

Author information

Authors and Affiliations

  1. Key Laboratory of Food Nutrition and Safety, Ministry of Education, Tianjin University of Science and Technology, Tianjin, 300457, China

    Hui Ji, Shuang Dong, Yuntong Li, Guiyun Chen & Ye Chen

  2. Linyi University, Linyi, 276005, China

    Hui Ji & Ling Li

  3. Chinese Medicine Hospital in Linyi City, Linyi, 276002, China

    Fei Han

  4. College of Food Engineering and Biotechnology, Tianjin University of Science and Technology, Tianjin, 300457, China

    Ye Chen

Authors
  1. Hui Ji
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Shuang Dong
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Fei Han
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Yuntong Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Guiyun Chen
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Ling Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Ye Chen
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Ye Chen.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Ji, H., Dong, S., Han, F. et al. Effects of Dielectric Barrier Discharge (DBD) Cold Plasma Treatment on Physicochemical and Functional Properties of Peanut Protein. Food Bioprocess Technol 11, 344–354 (2018). https://doi.org/10.1007/s11947-017-2015-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-017-2015-z

Keywords

Search

Navigation