DOI QR코드

DOI QR Code

Development of Two-Step Temperature Process to Modulate the Physicochemical Properties of β-lactoglobulin Nanoparticles

  • Ha, Ho-Kyung (Department of Animal Bioscience (Institute of Agriculture and Life Science), Gyeongsang National University) ;
  • Nam, Gyeong-Won (Kawoo Commerce Co., Ltd.) ;
  • Khang, Dongwoo (Department of Physiology, School of Medicine, Gachon University) ;
  • Park, Sung Jean (College of Pharmacy, Gachon University) ;
  • Lee, Mee-Ryung (Department of Food and Nutrition, Daegu University) ;
  • Lee, Won-Jae (Department of Animal Bioscience (Institute of Agriculture and Life Science), Gyeongsang National University)
  • Received : 2016.12.20
  • Accepted : 2017.02.01
  • Published : 2017.02.28

Abstract

The development of a new manufacturing process, a two-step temperature treatment, to modulate the physicochemical properties of nanoparticles including the size is critical. This is because its physicochemical properties can be key factors affecting the cellular uptake and the bioavailability of bioactive compounds encapsulated in nanoparticles. The aims of this study were to produce (beta-lactoglobulin) ${\beta}-lg$ nanoparticles and to understand how two-step temperature treatment could affect the formation and physicochemical properties of ${\beta}-lg$ nanoparticles. The morphological and physicochemical properties of ${\beta}-lg$ nanoparticles were determined using atomic force microscopy and a particle size analyzer, respectively. Circular dichroism spectroscopy was used to investigate the secondary structure of ${\beta}-lg$. The surface hydrophobicity and free thiol groups of ${\beta}-lg$ were increased with a decrease in sub-ambient temperature and an increase in mild heat temperature. As sub-ambient temperature was decreased, a decrease in ${\alpha}-helical$ content and an increase in ${\beta}-sheet$ content were observed. The two-step temperature treatment firstly involved a sub-ambient temperature treatment from 5 to $20^{\circ}C$ for 30 min, followed secondly by a mild heat temperature treatment from 55 to $75^{\circ}C$ for 10 min. This resulted in the production of spherically-shaped particles with a size ranging from 61 to 214 nm. Two-way ANOVA exhibited the finding that both sub-ambient and mild heat temperature significantly (p<0.0001) affected the size of nanoparticles. Zeta-potential values of ${\beta}-lg$ nanoparticles were reduced with increasing mild heat temperature. In conclusion, two-step temperature treatment was shown to play an important role in the manufacturing process - both due to its inducement of the conformational changes of ${\beta}-lg$ during nanoparticle formation, and due to its modulation of the physicochemical properties of ${\beta}-lg$ nanoparticles.

Keywords

References

  1. Alizadeh-Pasdar, N. and Li-Chan, E. C. (2000) Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. J. Agric. Food Chem. 48, 328-334. https://doi.org/10.1021/jf990393p
  2. Birnbaum, D., Kosmala, J., Henthorn, D., and Brannon-Peppas, L. (2000) Controlled release of beta-estradiol from PLGA microparticles: The effect of organic phase solvent on encapsulation and release. J. Controlled Release 65, 375-387. https://doi.org/10.1016/S0168-3659(99)00219-9
  3. Bruschi, M. L., Cardoso, M. L. C., Lucchesi, M. B., and Gremiao, M. P. D. (2003) Gelatin microparticles containing propolis obtained by spray-drying technique: Preparation and characterization. Int. J. Pharm. 264, 45-55. https://doi.org/10.1016/S0378-5173(03)00386-7
  4. Bryant, C. M. and McClements, D. J. (2000) Influence of NaCl and $CaCl_2$ on cold-set gelation of heat-denatured whey protein. J. Food Sci. 65, 801-804. https://doi.org/10.1111/j.1365-2621.2000.tb13590.x
  5. Chen, L., Remondetto, G. E., and Subirade, M. (2006) Food protein-based materials as nutraceutical delivery systems. Trends Food Sci. Technol. 17, 272-283. https://doi.org/10.1016/j.tifs.2005.12.011
  6. Chen, L. and Subirade, M. (2005) Chitosan/${\beta}$-lactoglobulin core-shell nanoparticles as nutraceutical carriers. Biomaterials 26, 6041-6053. https://doi.org/10.1016/j.biomaterials.2005.03.011
  7. Davidovic, M., Mattea, C., Qvist, J., and Halle, B. (2009) Protein cold denaturation as seen from the solvent. J. Am.Chem. Soc. 131, 1025-1036. https://doi.org/10.1021/ja8056419
  8. Duchene, D. and Ponchel, G. (1997). Bioadhesion of solid oral dosage forms, why and how? Eur. J. Pharm. Biopharm. 44, 15-23. https://doi.org/10.1016/S0939-6411(97)00097-0
  9. Gracia-Julia, A., Rene, M., Cortes-Munoz, M., Picart, L., Lopez-Pedemonte, T., Chevalier, D., and Dumay, E. (2008) Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments. Food Hydrocolloid. 22, 1014-1032. https://doi.org/10.1016/j.foodhyd.2007.05.017
  10. Ha, H. K., Kim, J. W., Lee, M. R., Jun, W., and Lee, W. J. (2015) Cellular uptake and cytotoxicity of ${\beta}$-lactoglobulin nanoparticles: The effects of particle size and surface charge. Asian-Aust. J. Anim. Sci. 28, 420-427. https://doi.org/10.5713/ajas.14.0761
  11. Ha, H. K., Kim, J. W., Lee, M. R., and Lee, W. J. (2013) Formation and characterization of quercetin-loaded chitosan oligosaccharide/${\beta}$-lactogloublin nanoparticle. Food Res. Int. 52, 82-90. https://doi.org/10.1016/j.foodres.2013.02.021
  12. Haug, I. J., Skar, H. M., Vegarud, G. E., Langsrud, T., and Draget, K. I. (2009) Electrostatic effects on ${\beta}$-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocoll. 23, 2287-2293. https://doi.org/10.1016/j.foodhyd.2009.06.006
  13. Hoffmann, M. A. M. and van Mil, P. J. J. M. (1997) Heat-induced aggregation of ${\beta}$-lactoglobulin: Role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 45, 2942-2948. https://doi.org/10.1021/jf960789q
  14. Hoffmann, M. A. M. and van Mil, P. J. J. M. (1999) Heat-induced aggregation of ${\beta}$-lactoglobulin as a function of pH. J. Agric. Food. Chem. 47, 1898-1905. https://doi.org/10.1021/jf980886e
  15. Hongsprabhas, P. and Barbut, S. (1996) $Ca^{2+}$-induced gelation of whey protein isolate: Effects of pre-heating. Food Res. Int. 29, 135-139. https://doi.org/10.1016/0963-9969(96)00011-7
  16. Iametti, S. Gregori, B. D. E., Vecchio, G., and Bonomi, F. (1996) Modifications occur at different structural levels during the heat denaturation of ${\beta}$-lactoglobulin. Eur. J. Biochem. 237, 106-112. https://doi.org/10.1111/j.1432-1033.1996.0106n.x
  17. Leclerc, P. L., Remondetto, G. E., Ramassamy, C., and Subirade, M. (2005) Whey protein nanospheres as drug carriers for oral administration. In Conference on bioencapsulation, Kingston, pp. 24-26.
  18. Lee, M. R., Choi, H. N., Ha, H. K., and Lee, W. J. (2013) Production and characterization of ${\beta}$-lactoglobulin/alginate nano-emulsion containing coenzyme $Q_{10}$: Impact of heat treatment and alginate concentrate. Korean J. Food Sci. An. 33, 67-74. https://doi.org/10.5851/kosfa.2013.33.1.67
  19. Li, H., Hardin, C. C., and Foegeding, E. A. (1994) NMR studies of thermal denaturation and cation-mediated aggregation of ${\beta}$-lactoglobulin. J. Agric. Food Chem. 42, 2411-2420. https://doi.org/10.1021/jf00047a010
  20. Mauguet, M. C., legrand, J., Brujes, L., Carnelle, G., Larre, C., and Popineau, Y. (2002) Gliadin matrices for microencapsulation processes by simple coacervation method. J. Microencapsulation 19, 377-384. https://doi.org/10.1080/02652040110105346
  21. Monahan, F. J., German, J. B., and Kinsella, J. E. (1995) Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 43, 46-52. https://doi.org/10.1021/jf00049a010
  22. Muthu, M. S. and Wilson, B. (2012) Challenges posed by the scale-up of nanomedicines. Nanomed. 7, 307-309. https://doi.org/10.2217/nnm.12.3
  23. Némethy, G. and Scheraga, H. A. (1962) The structure of water and hydrophobic binding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. J. Phys. Chem. 66, 1773-1789. https://doi.org/10.1021/j100816a004
  24. Parris, N., Purcell, J. M., and Ptashkin, S. M. (1991) Thermal denaturation of whey proteins in skim milk. J. Agric. Food Chem. 39, 2167-2170. https://doi.org/10.1021/jf00012a013
  25. Patel, A. R. and Velikov, K. P. (2011) Colloidal delivery systems in foods: A general comparison with oral drug delivery. LWT-Food Sci. Technol. 44, 1958-1964. https://doi.org/10.1016/j.lwt.2011.04.005
  26. Prabakaran, S. and Damodaran, S. (1997) Thermal unfolding of ${\beta}$-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 45, 4303-4308. https://doi.org/10.1021/jf970269a
  27. Relkin, P. (1998) Reversibility of heat-induced conformational changes and surface exposed hydrophobic clusters of ${\beta}$-lactoglobulin: Their role in heat-induced sol-gel state transition. Int. J. Biol. Macromol. 22, 59-66. https://doi.org/10.1016/S0141-8130(97)00089-5
  28. Taulier, N. and Chalikian, T. V. (2001). Characterization of pH-induced transitions of ${\beta}$-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies. J. Mol. Biol. 314, 873-889. https://doi.org/10.1006/jmbi.2001.5188
  29. Vetri, V. and Militello, V. (2005) Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin. Biophys. Chem. 113, 83-91. https://doi.org/10.1016/j.bpc.2004.07.042
  30. Win, K. Y. and Feng, S.-S. (2005) Effects of particle size and surface coating on cellular uptake of polymeric nanoparticles for oral delivery of anticancer drugs. Biomaterials 26, 2713-2722. https://doi.org/10.1016/j.biomaterials.2004.07.050
  31. Yang, J. T., Wu, C. C., and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
  32. Zangi, R. (2011) Driving force for hydrophobic interaction at different length scales. J. Phys. Chem. B. 115, 2303-2311. https://doi.org/10.1021/jp1090284
  33. Zhang, J., Chen, X. G., Peng, W. B., and Liu, C. S. (2008) Up-take of oleoyl-chitosan nanoparticles by A549 cells. Nanomed. 4, 208-214. https://doi.org/10.1016/j.nano.2008.03.006
  34. Zimet, P. and Livney, Y. D. (2009) Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for $\omega$-3 polyunsaturated fatty acids. Food Hydrocolloid. 23, 1120-1126. https://doi.org/10.1016/j.foodhyd.2008.10.008

Cited by

  1. 식품 소재를 이용한 나노전달체의 제조 및 유식품 적용에 관한 고찰 vol.36, pp.4, 2017, https://doi.org/10.22424/jmsb.2018.36.4.187
  2. Manufacture and Physicochemical Properties of Chitosan Oligosaccharide/A2 β-Casein Nano-Delivery System Entrapped with Resveratrol vol.39, pp.5, 2017, https://doi.org/10.5851/kosfa.2019.e74
  3. Development and Characterization of Whey Protein-Based Nano-Delivery Systems: A Review vol.24, pp.18, 2017, https://doi.org/10.3390/molecules24183254