TY  - CONF
AU  - Ivanov, Aleksandar
AU  - Veličković, Luka
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6665
AB  - C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examination of C-phycocyanin interactions with selected vitamins
SP  - 106
EP  - 106
UR  - https://hdl.handle.net/21.15107/rcub_cer_6665
ER  - 

@conference{
author = "Ivanov, Aleksandar and Veličković, Luka and Jovanović, Zorana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examination of C-phycocyanin interactions with selected vitamins",
pages = "106-106",
url = "https://hdl.handle.net/21.15107/rcub_cer_6665"
}

Ivanov, A., Veličković, L., Jovanović, Z., Gligorijević, N., Minić, S.,& Nikolić, M.. (2023). Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665

Ivanov A, Veličković L, Jovanović Z, Gligorijević N, Minić S, Nikolić M. Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665 .

Ivanov, Aleksandar, Veličković, Luka, Jovanović, Zorana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Examination of C-phycocyanin interactions with selected vitamins" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):106-106,
https://hdl.handle.net/21.15107/rcub_cer_6665 .