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@article{2367497,
author = {Czubinski, Jaroslaw and Kubíčková, Monika and Szpotkowski, Kamil and Komárek, Jan},
article_location = {Oxford},
article_number = {A},
doi = {http://dx.doi.org/10.1016/j.foodhyd.2023.109386},
keywords = {gamma-Conglutin; Lupin seed; Oligomerisation; Protein structure; Protein size and molecular weight; Nutraceutical protein},
language = {eng},
issn = {0268-005X},
journal = {Food Hydrocolloids},
title = {pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action},
url = {https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub},
volume = {147},
year = {2024}
}
TY - JOUR
ID - 2367497
AU - Czubinski, Jaroslaw - Kubíčková, Monika - Szpotkowski, Kamil - Komárek, Jan
PY - 2024
TI - pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action
JF - Food Hydrocolloids
VL - 147
IS - A
SP - 1-12
EP - 1-12
PB - Elsevier Science
SN - 0268005X
KW - gamma-Conglutin
KW - Lupin seed
KW - Oligomerisation
KW - Protein structure
KW - Protein size and molecular weight
KW - Nutraceutical protein
UR - https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub
N2 - Despite extensive research carried out on lupin seed gamma-conglutin neither its mechanism of action as a hypoglycaemic nutraceutical compound nor its physiological role for the plant has been unveil. This article revealed a pH-dependent reversible association/dissociation equilibrium involving monomer, dimer and hexamer of Lupinus angustifolius gamma-conglutin. The interaction between different oligomeric forms of this protein is reversible, and spectroscopic studies showed that the intact structure of gamma-conglutin was preserved under the tested environmental conditions tested (pH 4.5-7.5). The obtained results prove that the hexameric form was preferred under basic conditions and was stabilised by a number of bonds formed upon association of individual protomers. The simultaneous occurrence of several oligomeric forms at a given pH value was shown, and their share was strongly driven by protein concentration. The main changes in oligomerisation of gamma-conglutin take place in a pH range of 4.5-6.0, correlating with the pKa(R) values of the amino acid residues of His (6.0), Glu (4.1), and Asp (3.9). Moreover, a structural model of the protein in hexamer assembly was obtained based on small-angle X-ray scattering (SAXS) and negative staining cryo-electron microscopy (cryo-EM) analyses. The presented study provides essential knowledge about the colloidal dynamics and stability of gamma-conglutin in solution, improving our understanding of fundamental environmental factors that could affect the health-promoting activity of this lupin seed protein.
ER -
CZUBINSKI, Jaroslaw, Monika KUBÍČKOVÁ, Kamil SZPOTKOWSKI and Jan KOMÁREK. pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action. \textit{Food Hydrocolloids}. Oxford: Elsevier Science, 2024, vol.~147, A, p.~1-12. ISSN~0268-005X. Available from: https://dx.doi.org/10.1016/j.foodhyd.2023.109386.
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