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

Kód výsledku v IS VaVaI

RIV/00216224:14740/21:00124446 - isvavai.cz

Výsledek na webu

https://www.sciencedirect.com/science/article/pii/S0308814621004866?via%3Dihub

DOI - Digital Object Identifier

10.1016/j.foodchem.2021.129480

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10400 - Chemical sciences

Projekt

—

Návaznosti

—

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Food Chemistry

ISSN

0308-8146

e-ISSN

—

Svazek periodika

354

Číslo periodika v rámci svazku

AUG

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

129480

Kód UT WoS článku

000642467500014

EID výsledku v databázi Scopus

2-s2.0-85102879167