CZUBINSKI, J. Insight into thermally induced structural changes of lupin seed gamma-conglutin. Food Chemistry. Oxford, UK: Elsevier Science, 2021, vol. 354, AUG, p. 129480-129490. ISSN 0308-8146. Available from: https://dx.doi.org/10.1016/j.foodchem.2021.129480.
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Basic information
Original name Insight into thermally induced structural changes of lupin seed gamma-conglutin
Authors CZUBINSKI, J. (guarantor).
Edition Food Chemistry, Oxford, UK, Elsevier Science, 2021, 0308-8146.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10400 1.4 Chemical sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 9.231
RIV identification code RIV/00216224:14740/21:00124446
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1016/j.foodchem.2021.129480
UT WoS 000642467500014
Keywords in English Lupin seed; ?-Conglutin; Protein thermostability; Protein structure; Hypoglycemic protein
Tags CF BIC, ne MU, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 23/3/2022 12:37.
Abstract
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.
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