Detailed Information on Publication Record
2023
Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin
CZUBINSKI, Jaroslaw, Erika LATTOVÁ, Zbyněk ZDRÁHAL and Richard STRASSERBasic information
Original name
Characteristics of N-Glycosylation and Its Impact on the Molecular Behavior of Lupinus angustifolius ?-Conglutin
Authors
CZUBINSKI, Jaroslaw (616 Poland), Erika LATTOVÁ (703 Slovakia, guarantor, belonging to the institution), Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution) and Richard STRASSER (40 Austria)
Edition
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, UNITED STATES, AMER CHEMICAL SOC, 2023, 0021-8561
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
40500 4.5 Other agricultural sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 6.100 in 2022
RIV identification code
RIV/00216224:14740/23:00131565
Organization unit
Central European Institute of Technology
UT WoS
000986537100001
Keywords in English
lupin seed;gamma-conglutin;N-glycosylation;mass spectrometry;post-translational modification;thermal stability
Tags
International impact, Reviewed
Změněno: 2/11/2024 21:14, Ing. Martina Blahová
Abstract
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.
Links
EF16_026/0008446, research and development project |
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90242, large research infrastructures |
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