Journal of Ocean University of China

, Volume 18, Issue 4, pp 953–961 | Cite as

Preparation, Characteristics, and Formation Mechanism of Oyster Peptide-Zinc Nanoparticles

  • Hai HuangEmail author
  • Man Fu
  • Meihua Chen


Oyster peptide-zinc nanoparticles (OPZNPs) (28–108 nm) were prepared in the presence of 0.5%–0.9% zinc sulfate at pH 6.0–11.0. The obtained nanoparticles exhibited uniform size distribution and spherical shapes. Nanoparticle characteristics, such as size, surface charge, and hydrophobicity, could be adjusted by controlling zinc sulfate concentration and environmental pH. Increasing pH value or decreasing zinc sulfate concentration tended to reduce nanoparticle size and increase nanoparticle surface charge and hydrophobicity. OPZNPs presented good stability at near-neutral pH and could be stored for at least 20 days at 4°C. The results of the peptide conformation study and nanoparticle dissociation test proved that zinc ions and carboxyl groups are the key factors that affect OPZNP formation. The intermolecular combinations of carboxyl groups via zinc bridging facilitated the aggregation of oyster peptides. Nanoparticle formation was accompanied by aggregate association and conformational changes. These changes included increments in β-sheets, especially intermolecular β-sheets, at the expense of α-helixes. Overall, this work provided a green alternative route for the synthesis of OPZNPs.

Key words

oyster peptide zinc nanoparticles characteristics mechanism conformation changes 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.



This work was financially supported by the National Natural Science Foundation of China (No. 31860442) and the Natural Science Foundation of Guangxi Province, China (No.2016GXNSFAA380067).


  1. Allaoua, A., and Wang, Z., 2001. Effect of succinylation on the physicochemical properties of soy protein hydrolysate. Food Research International, 34: 507–514.CrossRefGoogle Scholar
  2. Bandekar, J., 1992. Amide modes and protein conformation. Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology, 1120 (2): 123–143.CrossRefGoogle Scholar
  3. Barth, A., and Zscherp, C., 2002. What vibrations tell us about proteins. Quarterly Reviews of Biophysics, 35: 369–430.CrossRefGoogle Scholar
  4. Byler, D. M., and Susi, H., 1986. Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers, 25: 469–487.CrossRefGoogle Scholar
  5. Chen, D., Liu, Z., Huang, W., Zhao, Y., Dong, S., and Zeng, M., 2013. Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate. Journal of Functional Foods, 5: 689–697.CrossRefGoogle Scholar
  6. Corrêa, D. H. A., and Ramos, C. H. I., 2009. The use of circular dichroism spectroscopy to study protein folding, form and function. African Journal of Biochemistry Research, 3: 164–173.Google Scholar
  7. Dragicevic-Curic, N., Gräfe, S., Gitter, B., Winter, S., and Fahr, A., 2010. Surface charged temoporfin-loaded flexible vesicles: In vitro skin penetration studies and stability. International Journal of Pharmaceutics, 384 (1–2): 100–108.CrossRefGoogle Scholar
  8. Food and Agriculture Organization of the United Nations (FAO), 2014. The state of food and agriculture 2013: Food systems for better nutrition. FAO, Roman.Google Scholar
  9. Galloway, J. M., and Staniland, S. S., 2012. Protein and peptide biotemplated metal and metal oxide nanoparticles and their patterning onto surfaces. Journal of Materials Chemistry, 22: 12423–12434.CrossRefGoogle Scholar
  10. Gao, H., Chen, H., Chen, W., Tao, F., Zheng, Y., Jiang, Y., and Ruan, H., 2008. Effect of nanometer pearl powder on calcium absorption and utilization in rats. Food Chemistry, 109: 493–498.CrossRefGoogle Scholar
  11. Hilty, F. M., Arnold, M., Hilbe, M., Teleki, A., Knijnenburg, J. T., Ehrensperger, F., Hurrell, R. F., Pratsinis, S. E., Langhans, W., and Zimmermann, M. B., 2010. Iron from nanocompounds containing iron and zinc is highly bioavailable in rats without tissue accumulation. Nature Nanotechnology, 5: 374–380.CrossRefGoogle Scholar
  12. Huang, H., Li, B., Liu, Z., Mu, X., Nie, R., and Zeng, M., 2014. Effectiveness of carp egg phosphopeptide on inhibiting the formation of insoluble Ca salts in vitro and enhancing Ca bioavailability in vivo. Food Science and Technology Research, 20: 385–392.CrossRefGoogle Scholar
  13. Huang, H., Li, B., and Zeng, M., 2016a. Nanoparticles formation of carp eggs peptides induced by Ca2+ and pH values. Science and Technology of Food Industry, 37 (18): 100–105 (in Chinese with English abstract).Google Scholar
  14. Huang, H., Li, B., and Zeng, M., 2016b. Mechanism of binding Ca2+ and the effect of inhibiting calcium phosphate crystal formation of phosphopeptide. Science and Technology of Food Industry, 37 (19): 62–66, 74 (in Chinese with English abstract).Google Scholar
  15. Huang, H., Li, B., and Zeng, M., 2016c. Preparation and stability of peptide-calcium complex of carp egg. Food Science and Technology, 41 (9): 246–251 (in Chinese with English abstract).Google Scholar
  16. Huang, H., Li, N., Su, J., Mo, X., and Li, X., 2018. Effect of collagen peptide on formation and stability of oyster peptidezinc nanoparticles. Food Science and Technology, 43 (5): 308–312 (in Chinese with English abstract).Google Scholar
  17. Huang, H., Mo, X., Su, J., and Su, B., 2018. Enzymatic preparation of oyster hydrolysate with peptide-zinc nanoparticle formation activity. Food Industry, 39 (5): 156–159 (in Chinese with English abstract).Google Scholar
  18. Jahn, M. R., Nawroth, T., Fütterer, S., Wolfrum, U., Kolb, U., and Langguth, P., 2012. Iron oxide/hydroxide nanoparticles with negatively charged shells show increased uptake in Caco-2 cells. Molecular Pharmaceutics, 9: 1628–1637.CrossRefGoogle Scholar
  19. Kong, J., and Yu, S., 2007. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica (Shanghai), 39: 549–559.CrossRefGoogle Scholar
  20. Lamprecht, A., Saumet, J. L., Roux, J., and Benoit, J. P., 2004. Lipid nanocarriers as drug delivery system for ibuprofen in pain treatment. International Journal of Pharmaceutics, 278: 407–414.CrossRefGoogle Scholar
  21. Lefèvre, T., and Subirade, M., 1999. Structural and interaction properties of β-lactoglobulin as studied by FTIR spectroscopy. International Journal of Food Science and Technology, 34: 419–428.CrossRefGoogle Scholar
  22. Lefèvre, T., and Subirade, M., 2000. Molecular differences in the formation and structure of fine-stranded and particulate beta-lactoglobulin gels. Biopolymers, 54: 578–586.CrossRefGoogle Scholar
  23. Liu, G., Li, J., Shi, K., Wang, S., Chen, J., and Liu, Y., 2009. Composition, secondary structure, and self-assembly of oat protein isolate. Journal of Agricultural and Food Chemistry, 57: 4552–4558.CrossRefGoogle Scholar
  24. Liu, Y., Lu, J., Chen, L., Wang, H., Gu, R., and Cai, M., 2016. Preparation of oyster peptide-zinc chelates. Science and Technology of Food Industry, 37 (8): 257–261 (in Chinese).Google Scholar
  25. Lodhia, J., Mandarano, G., Ferris, N. J., Eu, P., and Cowell, S. F., 2010. Development and use of iron oxide nanoparticles (Part 1): Synthesis of iron oxide nanoparticles for MRI. Biomedicine Image Interventions Journal, 6: 1–11.Google Scholar
  26. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193: 265–275.Google Scholar
  27. Lukowski, G., Müller, R. H., Miiller, B. W., and Dittgen, M., 1992. Acrylic acid copolymer nanoparticles for drug delivery: I. characterization of the surface properties relevant for in vivo organ distribution. International Journal of Pharmaceutics, 84: 23–31.CrossRefGoogle Scholar
  28. Majumder, D. D., Banerjee, R., and Ulrichs, C. H., 2007. Nanomaterials: Science of bottom-up and top-down. IETE Technical Review, 24: 9–25.Google Scholar
  29. Outten, C. E., and O’Halloran, T. V., 2011. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science, 292: 2488–2492.CrossRefGoogle Scholar
  30. Pereira, D. I. A., Mergler, B. I., Faria, N., Bruggraber, S. F. A., Aslam, M. F., Poots, L. K., Prassmayer, L., Lönnerdal, B., Brown, A. P., and Powell, J. J., 2013. Caco-2 cell acquisition of dietary iron(III) invokes a nanoparticulate endocytic pathway. PLoS One, 8: e81250.CrossRefGoogle Scholar
  31. Roduner, E., 2006. Size matters: Why nanomaterials are different. Chemical Society Reviews, 35: 583–592.CrossRefGoogle Scholar
  32. Sundar, S., Kundu, J., and Kundu, S., 2010. Biopolymeric nanoparticles. Science and Technology of Advanced Materials, 11: 1–13.CrossRefGoogle Scholar
  33. Tan, Y. N., Lee, J. Y., and Wang, D. I., 2010. Uncovering the design rules for peptide synthesis of metal nanoparticles. Journal of American Chemical Society, 132: 5677–5686.CrossRefGoogle Scholar
  34. Von Grebmer, K., Saltzman, A., Birol, E., Wiesman, D., Prasai, N., Yin, S., Yohannes, Y., Menon, P., Thompson, J., and Sonntag, A., 2014. 2014 Global Hunger Index: The Challenge of Hidden Hunger. International Food Policy Research Institute, Washington D. C., 56pp.Google Scholar
  35. Wallace, B. A., and Janes, R. W., 2003. Circular dichroism and synchrotron radiation circular dichroism spectroscopy: Tools for drug discovery. Biochemical Society Transactions, 31: 631–633.CrossRefGoogle Scholar
  36. Wang, C., Wang, C., Li, B., and Li, H., 2014. Zn(II) chelating with peptides found in sesame protein hydrolysates: Identification of the binding sites of complexes. Food Chemistry, 165: 594–602.CrossRefGoogle Scholar
  37. Wu, H., Liu, Z., Dong, S., Zhao, Y., Huang, H., and Zeng, M., 2013. Formation of ferric oxyhydroxide nanoparticles mediated by peptides in anchovy (Engraulis japonicus) muscle protein hydrolysate. Journal of Agricultural and Food Chemistry, 61: 219–224.CrossRefGoogle Scholar
  38. Wu, H., Zhu, S., Zeng, M., Liu, Z., Dong, S., Zhao, Y., Huang, H., and Lo, Y. M., 2014. Enhancement of non-heme iron absorption by anchovy (Engraulis japonicus) muscle protein hydrolysate involves a nano-particle-mediated mechanism. Journal of Agricultural and Food Chemistry, 62: 8632–8639.CrossRefGoogle Scholar
  39. Zhang, J., Liang, L., Tian, Z., Chen, L., and Subirade, M., 2012. Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study. Food Chemistry, 133: 390–399.CrossRefGoogle Scholar

Copyright information

© Ocean University of China, Science Press and Springer-Verlag GmbH Germany 2019

Authors and Affiliations

  1. 1.Guangxi Colleges and Universities Key Laboratory of Development and High-Value Utilization of Beibu Gulf Seafood ResourceQinzhouChina
  2. 2.College of Food EngineeringBeibu Gulf UniversityQinzhouChina

Personalised recommendations