Optimizing alginate immobilization of food-derived C-phycocyanin: structural and functional characterization

Nikola Gligorijević; Nikola Svrzić; Biljana Dojčinović; Dalibor Stanković; Sophie Combet; Simeon Minić; Milan Nikolić

doi:10.2298/JSC241025012G

PDF (723 kB)

Published: Jan 29, 2025

DOI: https://doi.org/10.2298/JSC241025012G

Keywords:

C-phycocyanin alginate immobilization stability mercury ions spirulina

Nikola Gligorijević

University of Belgrade - Institute for Chemistry, Technology and Metallurgy, Studentski trg 12-16, Belgrade

https://orcid.org/0000-0002-8691-2486

Nikola Svrzić

Department of Biochemistry, University of Belgrade – Faculty of Chemistry, Studentski trg 12-16, Belgrade, Serbia

https://orcid.org/0009-0001-7386-2918

Biljana Dojčinović

Department of Chemistry, University of Belgrade – Institute of Chemistry, Technology and Metallurgy, National Institute of the Republic of Serbia, Studentski trg 12-16, Belgrade

https://orcid.org/0000-0003-1479-8060

Dalibor Stanković

Department of Analytical Chemistry, University of Belgrade – Faculty of Chemistry, Studentski trg 12-16, Belgrade

https://orcid.org/0000-0001-7465-1373

Sophie Combet

Laboratoire Léon-Brillouin (LLB), UMR12 CEA, CNRS, Université Paris-Saclay, CEA-Saclay, F-91191 Gif-sur-Yvette CEDEX, Gif-sur-Yvette

https://orcid.org/0000-0002-8672-4514

Simeon Minić

Center of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade – Faculty of Chemistry, Studentski trg 12-16, Belgrade

Milan Nikolić

Center of Excellence for Molecular Food Sciences and Department of Biochemistry, University of Belgrade – Faculty of Chemistry, Studentski trg 12-16, Belgrade

https://orcid.org/0000-0003-0932-889X

Abstract

C-phycocyanin (C-PC) represents a significant component of the cyanobacteria Arthrospira platensis (Spirulina) biomass. Beyond its nutritional value, this protein exhibits numerous beneficial biological activities. A covalently attached chromophore, phycocyanobilin, gives C-PC a blue color, enabling its use as a natural food colorant. Additionally, phycocyanobilin exhibits various bioactive properties, including metal-binding activities. A key drawback to the broader industrial application of C-PC is its poor stability. Alternative food formulations using natural polymers as carriers and active components have recently gained considerable scientific attention. This paper describes optimized conditions for C-PC immobilization using alginate. The structural stabilization of immobilized C-PC was analyzed under high temperature (60°C) and high pressure (450 MPa). The storage stability of immobilized C-PC in dried alginate beads was tested by keeping the samples at 4°C for one month. The potential application of immobilized C-PC for the removal of mercury ions was also investigated. Alginate immobilization proved effective in stabilizing C-PC, significantly preserving its structure during prolonged storage, thermal treatment, and high-pressure exposure. Under the tested conditions, 97% of Hg²⁺ ions were removed by immobilized C-PC. Overall, this study optimized the procedure for enhancing C-PC stability through alginate immobilization and broadened its potential applications in food and bioremediation industries.

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

How to Cite

[1]

N. Gligorijević, “Optimizing alginate immobilization of food-derived C-phycocyanin: structural and functional characterization”, J. Serb. Chem. Soc., Jan. 2025.

Issue

Accepted Manuscripts

Section

Biochemistry & Biotechnology

This work is licensed under a Creative Commons Attribution 4.0 International License.

Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution license 4.0 that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.

References

L. Zhang, W. Liao, Y. Huang, Y. Wen, Y. Chu, C. Zhao, Food Prod. Process. Nutr. 4 (2022) 23 (https://doi.org/10.1186/s43014-022-00103-2)

V. Prete, A. C. Abate, P. Di Pietro, M. De Lucia, C. Vecchione, A. Carrizzo, Nutrients 16 (2024) 642 (https://doi.org/10.3390/nu16050642)

P. Grover, A. Bhatnagar, N. Kumari, A. Narayan Bhatt, D. Kumar Nishad, J. Purkayastha, Saudi J. Biol. Sci. 28 (2021) 1853 (https://doi.org/10.1016/j.sjbs.2020.12.037)

M. A. Domínguez-Martín, P. V. Sauer, H. Kirst, M. Sutter, D. Bína, B. J. Greber, E. Nogales, T. Polívka, C. A. Kerfeld, Nature 609 (2022) 835 (https://doi.org/10.1038/s41586-022-05156-4)

J. Dagnino-Leone, C. P. Figueroa, M. L. Castañeda, A. D. Youlton, A. Vallejos-Almirall, A. Agurto-Muñoz, J. Pavón Pérez, C. Agurto-Muñoz, Comput. Struct. Biotechnol. J. 20 (2022) 1506 (https://doi.org/10.1016/j.csbj.2022.02.016)

T. Minato, T. Teramoto, N. Adachi, N. K. Hung, K. Yamada, M. Kawasaki, M. Akutsu, T. Moriya, T. Senda, S. Ogo, Y. Kakuta, K.-S. Yoon, Commun. Biol. 4 (2021) 1238 (https://doi.org/10.1038/s42003-021-02767-x)

A. M. Saxena, J. Mol. Biol. 200 (1988) 579 (https://doi.org/10.1016/0022-2836(88)90544-X)

X.-Q. Wang, L.-N. Li, W.-R. Chang, J.-P. Zhang, L.-L. Gui, B.-J. Guo, D.-C. Liang, Acta Crystallogr. Sect. D Biol. Crystallogr. 57 (2001) 784 (https://doi.org/10.1107/S0907444901004528)

T. Watermann, H. Elgabarty, D. Sebastiani, Phys. Chem. Chem. Phys. 16 (2014) 6146 (https://doi.org/10.1039/C3CP54307B)

F. Pagels, A. C. Guedes, H. M. Amaro, A. Kijjoa, V. Vasconcelos, Biotechnol. Adv. 37 (2019) 422 (https://doi.org/10.1016/j.biotechadv.2019.02.010)

Y. Hou, M. Yan, Q. Wang, Y. Wang, Y. Xu, Y. Wang, H. Li, H. Wang, Food Anal. Methods 10 (2017) 1931 (https://doi.org/10.1007/s12161-016-0759-0)

M. Carocho, P. Morales, I. C. F. R. Ferreira, Trends Food Sci. Technol. 45 (2015) 284 (https://doi.org/10.1016/j.tifs.2015.06.007)

M. I. Landim Neves, E. K. Silva, M. A. A. Meireles, Trends Food Sci. Technol. 112 (2021) 163 (https://doi.org/10.1016/j.tifs.2021.03.023)

D. Pez Jaeschke, I. Rocha Teixeira, L. Damasceno Ferreira Marczak, G. Domeneghini Mercali, Food Res. Int. 143 (2021) 110314 (https://doi.org/10.1016/j.foodres.2021.110314)

R. Chaiklahan, N. Chirasuwan, B. Bunnag, Process Biochem. 47 (2012) 659 (https://doi.org/10.1016/j.procbio.2012.01.010)

S. Minić, N. Gligorijević, L. Veličković, M. Nikolić, Int. J. Mol. Sci. 25 (2024) 7187 (https://doi.org/10.3390/ijms25137187)

H. Wang, Z. Ouyang, L. Hu, Y. Cheng, J. Zhu, L. Ma, Y. Zhang, Food Chem. 397 (2022) 133725 (https://doi.org/10.1016/j.foodchem.2022.133725)

B.-W. Qiao, X.-T. Liu, C.-X. Wang, S. Song, C.-Q. Ai, Y.-H. Fu, Front. Nutr. 9 (2022) 890942 (https://doi.org/10.3389/fnut.2022.890942)

A. Londoño-Moreno, Z. Mundo-Franco, M. Franco-Colin, C. Buitrago-Arias, M. L. Arenas-Ocampo, A. R. Jiménez-Aparicio, E. Cano-Europa, B. H. Camacho-Díaz, Foods 12 (2023) 3272 (https://doi.org/10.3390/foods12173272)

M. Yan, B. Liu, X. Jiao, S. Qin, Food Bioprod. Process. 92 (2014) 89 (https://doi.org/10.1016/j.fbp.2013.07.008)

D. Rajmohan, D. Bellmer, Int. J. Food Sci. 2019 (2019) Article ID 7101279 (https://doi.org/10.1155/2019/7101279)

H. N. Pradeep, C. A. Nayak, J. Food Sci. Technol. 56 (2019) 4526 (https://doi.org/10.1007/s13197-019-03955-8)

W. Pan-utai, S. Iamtham, J. King Saud Univ. - Sci. 31 (2019) 1535 (https://doi.org/10.1016/j.jksus.2018.05.026)

Hadiyanto, M. Suzery, D. Setyawan, D. Majid, H. Sutanto, IOP Conf. Ser. Earth Environ. Sci. 55 (2017) 012030 (https://doi.org/10.1088/1755-1315/55/1/012030)

J. Radović, D. Popović, T. Ćurčić, L. Veličković, S. Lević, V. Pavlović, S. Minić, M. Nikolić, N. Gligorijević, Algal Res. 80 (2024) 103543 (https://doi.org/10.1016/j.algal.2024.103543)

M. R. Nikolic, S. Minic, M. Macvanin, D. Stanic-Vucinic, T. Cirkovic Velickovic, Analytical Protocols in Phycobiliproteins Analysis, in E. Jacob-Lopes, M. Isabel Queiroz, L. Queiroz Zepka (Eds.), Pigment. from Microalgae Handb., Springer Cham, Cham, Germany, 2020, pp. 179 (https://doi.org/10.1007/978-3-030-50971-2_8)

R. Lauceri, G. Chini Zittelli, G. Torzillo, Algal Res. 44 (2019) 101685 (https://doi.org/10.1016/j.algal.2019.101685)

G. Patil, K. S. M. S. Raghavarao, Biochem. Eng. J. 34 (2007) 156 (https://doi.org/10.1016/j.bej.2006.11.026)

H.-L. Wu, G.-H. Wang, W.-Z. Xiang, T. Li, H. He, Int. J. Food Prop. 19 (2016) 2349 (https://doi.org/10.1080/10942912.2015.1038564)

C. Chen, I. Liu, R. MacColl, D. S. Berns, Biopolymers 22 (1983) 1223 (https://doi.org/10.1002/bip.360220414)

M. Faieta, L. Neri, G. Sacchetti, A. Di Michele, P. Pittia, Food Res. Int. 132 (2020) 109093 (https://doi.org/10.1016/j.foodres.2020.109093)

G. Martelli, C. Folli, L. Visai, M. Daglia, D. Ferrari, Process Biochem. 49 (2014) 154 (https://doi.org/10.1016/j.procbio.2013.10.008)

L. Jespersen, L. D. Strømdahl, K. Olsen, L. H. Skibsted, Eur. Food Res. Technol. 220 (2005) 261 (https://doi.org/10.1007/s00217-004-1062-7)

H. Scheer, W. Kufer, Zeitschrift Für Naturforsch. C 32 (1977) 513 (https://doi.org/10.1515/znc-1977-7-806)

S. Minic, L. Velickovic, B. Annighöfer, A. Thureau, N. Gligorijevic, Z. Jovanovic, A. Brûlet, S. Combet, Protein Sci. 33 (2024) e5145 (https://doi.org/10.1002/pro.5145)

Y. Li, Z. Zhang, M. Paciulli, A. Abbaspourrad, J. Food Sci. 85 (2020) 727 (https://doi.org/10.1111/1750-3841.14842)

Z. Zhang, S. Cho, Y. Dadmohammadi, Y. Li, A. Abbaspourrad, Food Hydrocoll. 110 (2021) 106055 (https://doi.org/10.1016/j.foodhyd.2020.106055)

H. Shkolnikov Lozober, Z. Okun, G. Parvari, A. Shpigelman, Antioxidants 12 (2023) 568 (https://doi.org/10.3390/antiox12030568)

S. T. Moe, K. I. Draget, G. Skjåk-Bræk, O. Simdsrød, Carbohydr Polym. 19 (1992) 279 (https://doi.org/10.1016/0144-8617(92)90081-Z)

N. A. A. Qasem, R. H. Mohammed, D. U. Lawal, Npj Clean Water 4 (2021) 36 (https://doi.org/10.1038/s41545-021-00127-0).

Article Sidebar

Main Article Content

Abstract

Downloads

Metrics

Article Details

References

Most read articles by the same author(s)