Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F23%3A00131565" target="_blank" >RIV/00216224:14740/23:00131565 - isvavai.cz</a>

Výsledek na webu

<a href="https://pubs.acs.org/doi/epdf/10.1021/acs.jafc.3c00727" target="_blank" >https://pubs.acs.org/doi/epdf/10.1021/acs.jafc.3c00727</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.jafc.3c00727" target="_blank" >10.1021/acs.jafc.3c00727</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

40500 - Other agricultural sciences

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

ISSN

0021-8561

e-ISSN

1520-5118

Svazek periodika

71

Číslo periodika v rámci svazku

19

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

7359-7369

Kód UT WoS článku

000986537100001

EID výsledku v databázi Scopus

2-s2.0-85159738458