STRUCTURAL CHARACTERIZATION AND STORAGE STABILITY OF HEAT-INDUCED LACTOFERRIN-SODIUM CASEINATE COMPLEXES AT DIFFERENT MASS RATIOS

Yaping Sun

doi:10.5937/ffr0-61995

Yaping Sun Cisen pharmaceutical Co., Ltd

DOI: https://doi.org/10.5937/ffr0-61995

Sažetak

Sodium caseinate (NaCas) forms complexes with lactoferrin (LF), yet the structural characteristics and stability of these complexes before and after heating are not well understood. This study demonstrated that lactoferrin and sodium caseinate exhibit weak electrostatic interactions prior to heating. Upon heating at 90 °C for 10 minutes, these interactions were significantly enhanced, resulting in the formation of stable lactoferrin/sodium caseinate complexes at ratios of 2:1 and 1:1. Complexes formed at a 1:2 ratio initially exhibited smaller particle sizes and lower turbidity but subsequently precipitated during storage. Conversely, complexes at 2:1 and 1:1 ratios maintained consistent turbidity and particle size over 20 days, indicating excellent long-term stability. These findings reveal the important role of NaCas in stabilizing LF during heat treatment and storage, providing valuable insights for the development of stable protein-based functional food ingredients.

Reference

Anema, S. G. (2021). Spontaneous interaction between whey protein isolate proteins and lactoferrin: Effect of heat denaturation. International Dairy Journal, 113, 104887. https://doi.org/10.1016/j.idairyj.2020.104887.

Betz, S. F. (1993). Disulfide bonds and the stability of globular proteins. Protein Science, 2, 1551-1558. doi: 10.1002/pro.5560021002.

Bokkhim, H., Bansal, N., Grondahl, L., & Bhandari, B. (2010). Physico-chemical properties of different forms of bovine lactoferrin. Food Chemistry, 141, 3007-3013. https://doi.org/10.1016/j.foodchem.2013.05.139.

De Kruif, C. G., Pedersen, J., Huppertz, T., & Anema, SG. (2013). Coacervates of lactotransferrin and β- or κ-casein: structure determined using SAXS. Langmuir 29, 10483-10490. https://doi.org/10.1021/la402236f.

Gazi, I., Vilalva, I., & Huppertz, T. (2014). Plasmin activity and proteolysis in milk protein ingredients. International Dairy Journal, 38, 208-212. https://doi.org/10.1016/j.idairyj.2013.11.012.

Jenkins, P., & Snowden, M. (1996). Depletion flocculation in colloidal dispersions. Advances in Colloid and Interface Science, 68, 57-96. https://doi.org/10.1016/S0001-8686(96)90046-9.

Jiang, H., Zhang, T., Pan, Y., Yang, H., Xu, X., Han, J., & Liu, W. (2024). Thermal stability and in vitro biological fate of lactoferrin-polysaccharide complexes. Food Research International 182, 114182. https://doi.org/10.1016/j.foodres.2024.114182

Li, Q., & Zhao, Z. (2017). Formation of lactoferrin/sodium caseinate complexes and their adsorption behavior at the air/water interface. Food Chemistry, 232, 697-703. https://doi.org/10.1016/j.foodchem.2017.04.072.

Li, Q., & Zhao, Z. (2018). Interaction between lactoferrin and whey proteins and its influence on the heat-induced gelation of whey proteins. Food Chemistry, 252, 92-98. https://doi.org/10.1016/j.foodchem.2018.01.114.

Li, Q., Lan, H., & Zhao, Z. (2019). Protection effect of sodium alginate against heat-induced structural changes of lactoferrin molecules at neutral pH. LWT-Food Science and Technology, 99, 513-518. https://doi.org/10.1016/j.lwt.2018.10.019.

Sreedhara, A., Flengsrud, R., Langsrud, T., Kaul, P., Prakash, V., Krowarsch, D., & Vegarud, G. E. (2010). Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins. Biometals, 23, 1159-1170. DOI: 10.1007/s10534-010-9366-5.

Stănciuc, N., Aprodu, I., Râpeanu, G., van der Plancken, I., Bahrim, G., Hendrickx, M. (2013). Analysis of the Thermally induced structural changes of bovine lactoferrin. Journal of Agricultural and Food Chemistry, 61, 2234-2243. https://doi.org/ 10.1021/ jf305178s.

Wang, X., & Zhao, Z. (2022). Improved encapsulation capacity of casein micelles with modified structure. Journal of Food Engineering 333, 111138. https://doi.org/10.1016/ j. jfoodeng.2022.111138.

Ward, P. P., Paz, E., & Conneely, O. M. (2005). Multifunctional roles of lactoferrin: A critical overview. Cellular and Molecular Life Sciences, 62, 2540-2548. https://doi.org/10.1007/s00018-005-5369-8

Xu, K., Zhao, Z., Guo, M., & Du, J. (2019). Conjugation between okra polysaccharide and lactoferrin and its inhibition effect on thermal aggregation of lactoferrin at neutral pH. LWT-Food Science and Technology, 107, 125-131. https://doi.org/10.1016/j.lwt. 2019.02.082

Zhao, Z., & Corredig, M. (2016). Serum composition of milk subjected to re-equilibration by dialysis at different temperatures, after pH adjustments. Journal of Dairy Science, 99, 2588-2593. https://doi.org/10.3168/jds.2015-9917.

Zhao, Z., Lan, H., Li, Q., & Wang, L. (2018). Stability of heat-induced lactoferrin-sodium caseinate complexes: effects of pH and ionic strength. Journal of Food Measurement and Characterization, 12, 1896-1903. https://doi.org/10.1007/s11694-018-9803-7.