Adsorptive properties of milk proteins onto novel porous zirconia
Source abstract
Abstract
In this study, porous zirconia (PZ) was synthesised by sol–gel process and evaluated for the adsorption of milk proteins such as β-casein and β-lactoglobulin. The particles manifested an extremely good adsorption affinity for β-casein, with very short adsorption times. In addition, increasing of the adsorption times afforded aggregation of the β-casein-adsorbed particles. Adsorption–desorption experiments, carried out by immersing the PZ in HEPES buffer solution containing 2 M sodium chloride, revealed that only a small amount of adsorbed β-casein was leached from the particles, which suggests that the protein was tightly adsorbed. Taken together, the results obtained suggest that the strong adsorption affinity and specific adsorption behaviour of PZ for the phosphate group render it a promising candidate for the development of phosphoprotein adsorbents.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Proteins in Food Systems · Protein Hydrolysis and Bioactive Peptides
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Materials Chemistry Course, Graduate School of Engineering, Aichi Institute of Technology
National Institute of Advanced Industrial Science and Technology
References (22)
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1. 1) O. Svensson, A. Kurut and M. Skepö, Food Hydrocolloid., 36, 332–338 (2014).
2. 2) K. R. Kristiansen, J. Otte, R. Ipsen and K. B. Qvist, Int. Dairy J., 8, 113–118 (1998).
3. 3) R. Wüstneck, J. Krägel, R. Miller, V. B. Fainerman, P. J. Wilde, D. K. Sarker and D. C. Clark, Food Hydrocolloid., 10, 395–405 (1996).
4. 4) L. K. Creamer, D. A. D. Parry and G. N. Malcolm, Arch. Biochem. Biophys., 227, 98–105 (1983).
5. 5) J. Nawrocki, M. P. Rigney, A. M. Cormick and P. W. Carr, J. Chromatogr. A, 657, 229–282 (1993).
6. 6) J. Zhao, S. S. Ge, L. Liu, Q. Shao, X. Mai, C. X. Zhao, L. Hao, T. Wu, Z. Yu and Z. Guo, Ind. Eng. Chem. Res., 57, 231–241 (2018).
7. 7) W. A. Schafer and P. W. Carr, J. Chromatogr. A, 587, 137–147 (1991).
8. 8) M. Haneda, K. Takamura, Y. Doi, N. Bion and L. Vivier, J. Mater. Sci., 52, 5835–5845 (2017).
9. 9) M. S. Wong and J. Y. Ying, Chem. Mater., 10, 2067–2077 (1998).
10. 10) D. Spielbauer, G. A. H. Mekhemer, T. Riemer, M. I. Zaki and H. Knözinger, J. Phys. Chem. B, 101, 4681–4688 (1997).
11. 11) R. Chitrakar, S. Tezuka, A. Sonoda, K. Sakane, K. Ooi and T. Hirotsu, J. Colloid Interf. Sci., 297, 426–433 (2006).
12. 12) Y. Su, H. Cui, Q. Li, S. Gao and J. K. Shang, Water Res., 47, 5018–5026 (2013).
13. 13) K. S. Karpisz, M. Wisniewska and D. Mysliwiec, J. Ind. Eng. Chem., 32, 113–119 (2015).
14. 14) Y. Masuda, S. Kugimiya and K. Kato, J. Asian Ceram. Soc., 2, 11–19 (2014).
15. 15) C. Liu, Y. Guo, Q. Hong, C. Rao, H. Zhang, Y. Dong, L. Huang, X. Lu and N. Bao, Langmuir, 32, 3995–4003 (2016).10.1021/acs.langmuir.5b04496 ↗
16. 16) A. Ebadi, J. S. S. Mohammadzadeh and A. Khudiev, Adsorption, 15, 65–73 (2009).10.1007/s10450-009-9151-3 ↗
17. 17) M. Kruk and M. Jaroniec, Chem. Mater., 13, 3169–3183 (2001).
18. 18) M. M. Bradford, Anal. Biochem., 72, 248–254 (1976).
19. 19) A. Majedi, A. Abbasi and F. Davar, J. Sol-Gel Sci. Techn., 77, 542–552 (2016).
20. 20) B. Ksapabutr, E. Gulari and S. Wongkasemjit, Powder Technol., 148, 11–14 (2004).
21. 21) H. Cui, Q. Li, S. Gao and J. K. Shang, J. Ind. Eng. Chem., 18, 1418–1427 (2012).
22. 22) H. Chen and C. X. Ding, Surf. Coat. Tech., 150, 31–36 (2002).