TY  - CONF
AU  - Minić, Simeon
AU  - Annighöfer, Burkhard
AU  - Brûlet, Annie
AU  - Combet, Sophie
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6438
AB  - High pressure (HP) is particularly suited to study protein folding/unfolding, revealing subtle structural rearrangements not accessible by other types of denaturation. HP also has many industrial-scale advantages over heat treatments, including “greener” processing and preservation of nutritional values, colors, and flavors of foods. We have combined in situ HP with small-angle (X-ray and neutron) scattering (SAS) and spectrophotometry to follow the structure in solution of proteins of interest for the food industry. SAS is an essential technique for obtaining structural, but low-resolution, information about proteins, when conventional high-resolution structural biology methods are not possible. I will illustrate this approach with two studies on proteins of food interest: (i) bovine β-lactoglobulin (BLG), a whey protein with a high propensity to bind to various bioactive molecules. We probed by SANS1 and absorbance the effects on pressure stability and reversibility of BLG of the binding of retinol (vitamin A), resveratrol (polyphenol), and biliverdin (linear tetrapyrrole chromophore) to different sites on the protein2, 3. (ii) C-phycocyanin (CPC), a phycobiliprotein from cyanobacteria, to which tetrapyrrole chromophores are covalently attached and which can be used as a natural blue dye in the food industry. We studied by SAXS and absorbance HP-induced CPC unfolding and reversibility from two oligomeric states of the protein as a function of pH.
Acknowledgements
LLB, SOLEIL, and I2BC facilities are acknowledged for beamtime and proteomic expertise. This work was also supported by ANSO Project No. ANSOCR-PP-2021- 01.
References
1. Annighöfer B, et al. High pressure cell to investigate protein unfolding up to 600 MPa by small-angle neutron scattering. Rev Sci Instr 2019;90:025106.
2. Minic S, et al. Effect of ligands on HP-induced unfolding and oligomerization of β-lactoglobulin. Biophysical J 2020;119:2262-74.
3. Minic S, et al. Structure of proteins under pressure: covalent binding effects of biliverdin on beta-lactoglobulin. Biophysical J 2022;121:2514-25.
PB  - Belgrade : Serbian Biochemical Society
C3  - "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia
T1  - Stability of food proteins at high pressure conditions
SP  - 59
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6438
ER  - 

@conference{
author = "Minić, Simeon and Annighöfer, Burkhard and Brûlet, Annie and Combet, Sophie",
year = "2023",
abstract = "High pressure (HP) is particularly suited to study protein folding/unfolding, revealing subtle structural rearrangements not accessible by other types of denaturation. HP also has many industrial-scale advantages over heat treatments, including “greener” processing and preservation of nutritional values, colors, and flavors of foods. We have combined in situ HP with small-angle (X-ray and neutron) scattering (SAS) and spectrophotometry to follow the structure in solution of proteins of interest for the food industry. SAS is an essential technique for obtaining structural, but low-resolution, information about proteins, when conventional high-resolution structural biology methods are not possible. I will illustrate this approach with two studies on proteins of food interest: (i) bovine β-lactoglobulin (BLG), a whey protein with a high propensity to bind to various bioactive molecules. We probed by SANS1 and absorbance the effects on pressure stability and reversibility of BLG of the binding of retinol (vitamin A), resveratrol (polyphenol), and biliverdin (linear tetrapyrrole chromophore) to different sites on the protein2, 3. (ii) C-phycocyanin (CPC), a phycobiliprotein from cyanobacteria, to which tetrapyrrole chromophores are covalently attached and which can be used as a natural blue dye in the food industry. We studied by SAXS and absorbance HP-induced CPC unfolding and reversibility from two oligomeric states of the protein as a function of pH.
Acknowledgements
LLB, SOLEIL, and I2BC facilities are acknowledged for beamtime and proteomic expertise. This work was also supported by ANSO Project No. ANSOCR-PP-2021- 01.
References
1. Annighöfer B, et al. High pressure cell to investigate protein unfolding up to 600 MPa by small-angle neutron scattering. Rev Sci Instr 2019;90:025106.
2. Minic S, et al. Effect of ligands on HP-induced unfolding and oligomerization of β-lactoglobulin. Biophysical J 2020;119:2262-74.
3. Minic S, et al. Structure of proteins under pressure: covalent binding effects of biliverdin on beta-lactoglobulin. Biophysical J 2022;121:2514-25.",
publisher = "Belgrade : Serbian Biochemical Society",
journal = ""Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia",
title = "Stability of food proteins at high pressure conditions",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6438"
}

Minić, S., Annighöfer, B., Brûlet, A.,& Combet, S.. (2023). Stability of food proteins at high pressure conditions. in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia
Belgrade : Serbian Biochemical Society., 59-59.
https://hdl.handle.net/21.15107/rcub_cherry_6438

Minić S, Annighöfer B, Brûlet A, Combet S. Stability of food proteins at high pressure conditions. in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia. 2023;:59-59.
https://hdl.handle.net/21.15107/rcub_cherry_6438 .

Minić, Simeon, Annighöfer, Burkhard, Brûlet, Annie, Combet, Sophie, "Stability of food proteins at high pressure conditions" in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia (2023):59-59,
https://hdl.handle.net/21.15107/rcub_cherry_6438 .