Insight into thermally induced structural changes of lupin seed
gamma-conglutin

J 2021

Insight into thermally induced structural changes of lupin seed gamma-conglutin

CZUBINSKI, J.

Základní údaje

Originální název

Insight into thermally induced structural changes of lupin seed gamma-conglutin

Autoři

CZUBINSKI, J. (garant)

Vydání

Food Chemistry, Oxford, UK, Elsevier Science, 2021, 0308-8146

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10400 1.4 Chemical sciences

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 9.231

Kód RIV

RIV/00216224:14740/21:00124446

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.foodchem.2021.129480

UT WoS

000642467500014

Klíčová slova anglicky

Lupin seed; ?-Conglutin; Protein thermostability; Protein structure; Hypoglycemic protein

Štítky

CF BIC, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 3. 2022 12:37, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

A multidimensional analysis aimed to determine the thermal impact on ?-conglutin at the two oligomeric states was carried out. A wide range of biophysical and bioinformatic methods allowed to get insight into a thermal unfolding mechanism. The determined midpoint transition temperature (Tm) values were remarkably different, being 56.5 ?C and 71.1 ?C for ?-conglutin monomer and hexamer, respectively. The unfolding pattern for hexamer molecules included aggregation/precipitation, while monomers tended to form soluble aggregates after heat exposure. Interestingly, differences in the aromatic amino acid residues movements indicate that during thermal treatment of ?-conglutin hexamer red-shift occurred contrary to the monomer in the case of which blueshift was noted. The obtained results provide an essential contribution to expand our knowledge about the molecular characterization of this intriguing lupin seed protein.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

CZUBINSKI, J. Insight into thermally induced structural changes of lupin seed gamma-conglutin. Food Chemistry. Oxford, UK: Elsevier Science, 2021, roč. 354, AUG, s. 129480-129490. ISSN 0308-8146. Dostupné z: https://dx.doi.org/10.1016/j.foodchem.2021.129480.

@article{1842617,
   author = {Czubinski, J.},
   article_location = {Oxford, UK},
   article_number = {AUG},
   doi = {http://dx.doi.org/10.1016/j.foodchem.2021.129480},
   keywords = {Lupin seed; ?-Conglutin; Protein thermostability; Protein structure; Hypoglycemic protein},
   language = {eng},
   issn = {0308-8146},
   journal = {Food Chemistry},
   title = {Insight into thermally induced structural changes of lupin seed gamma-conglutin},
   url = {https://www.sciencedirect.com/science/article/pii/S0308814621004866?via%3Dihub},
   volume = {354},
   year = {2021}
}

TY  - JOUR
ID  - 1842617
AU  - Czubinski, J.
PY  - 2021
TI  - Insight into thermally induced structural changes of lupin seed gamma-conglutin
JF  - Food Chemistry
VL  - 354
IS  - AUG
SP  - 129480
EP  - 129480
PB  - Elsevier Science
SN  - 03088146
KW  - Lupin seed
KW  - ?-Conglutin
KW  - Protein thermostability
KW  - Protein structure
KW  - Hypoglycemic protein
UR  - https://www.sciencedirect.com/science/article/pii/S0308814621004866?via%3Dihub
N2  - A multidimensional analysis aimed to determine the thermal impact on ?-conglutin at the two oligomeric states was carried out. A wide range of biophysical and bioinformatic methods allowed to get insight into a thermal unfolding mechanism. The determined midpoint transition temperature (Tm) values were remarkably different, being 56.5 ?C and 71.1 ?C for ?-conglutin monomer and hexamer, respectively. The unfolding pattern for hexamer molecules included aggregation/precipitation, while monomers tended to form soluble aggregates after heat exposure. Interestingly, differences in the aromatic amino acid residues movements indicate that during thermal treatment of ?-conglutin hexamer red-shift occurred contrary to the monomer in the case of which blueshift was noted. The obtained results provide an essential contribution to expand our knowledge about the molecular characterization of this intriguing lupin seed protein.
ER  -

CZUBINSKI, J. Insight into thermally induced structural changes of lupin seed gamma-conglutin. \textit{Food Chemistry}. Oxford, UK: Elsevier Science, 2021, roč.~354, AUG, s.~129480-129490. ISSN~0308-8146. Dostupné z: https://dx.doi.org/10.1016/j.foodchem.2021.129480.

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