2023
Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin
CZUBINSKI, Jaroslaw, Erika LATTOVÁ, Zbyněk ZDRÁHAL a Richard STRASSERZákladní údaje
Originální název
Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin
Autoři
CZUBINSKI, Jaroslaw (616 Polsko), Erika LATTOVÁ (703 Slovensko, garant, domácí), Zbyněk ZDRÁHAL (203 Česká republika, domácí) a Richard STRASSER (40 Rakousko)
Vydání
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, UNITED STATES, AMER CHEMICAL SOC, 2023, 0021-8561
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
40500 4.5 Other agricultural sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 6.100 v roce 2022
Kód RIV
RIV/00216224:14740/23:00131565
Organizační jednotka
Středoevropský technologický institut
UT WoS
000986537100001
Klíčová slova anglicky
lupin seed;gamma-conglutin;N-glycosylation;mass spectrometry;post-translational modification;thermal stability
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 2. 11. 2024 21:14, Ing. Martina Blahová
Anotace
V originále
a-Conglutin, a lupin seed protein, is an intriguing protein both in terms of the complexity of its molecular structure and a broad spectrum of unique health-promoting properties manifested in animal and human trials. Moreover, this protein is an evolutionary cornerstone whose physiological significance for the plant has not been determined yet. Herein, a comprehensive characterization of a-conglutin glycosylation is presented and includes the identification of the N-glycan-bearing site, the qualitative and quantitative composition of glycan-building saccharides, as well as the effect of oligosaccharide removal on structural and thermal stability. The obtained results indicate the presence of glycans belonging to different classes attached to the Asn98 residue. In addition, the detachment of the oligosaccharide significantly affects secondary structure composition, which disturbs the oligomerization process. The structural changes were also reflected in biophysical parameters, i.e., at a pH value of 4.5, an increase in a-conglutin thermal stability was observed for the deglycosylated monomeric form. Collectively, the presented results provide evidence of the high complexity of the post-translational maturation and suggest the possibility of a functional effect that glycosylation might have on a-conglutin structure integrity.
Návaznosti
EF16_026/0008446, projekt VaV |
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90242, velká výzkumná infrastruktura |
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