КФУ. Карточка публикации. Binding studies of crocin to b-Lactoglobulin and its impacts on both components

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BINDING STUDIES OF CROCIN TO B-LACTOGLOBULIN AND ITS IMPACTS ON BOTH COMPONENTS

Форма представления

Статьи в зарубежных журналах и сборниках

Год публикации

2020

Язык

английский

Авторы, сотрудники КФУ

Сироткин Владимир Александрович, автор

Библиографическое описание на языке оригинала

Allahdad Z., Khammari A., Karami L., Khasemi A., Sirotkin V.A., Haertle T., Saboury A.A. Binding studies of crocin to b-Lactoglobulin and its impacts on both components. // Food Hydrocolloids. - 2020. - Vol.108, - Art. № 106003.

Аннотация

Light susceptibility of crocin and high degree of unsaturation limit its application in food systems. This study aimed to investigate the impact of molecular binding of crocin to β-lactoglobulin (β-LG) on crocin stability as well as the conformational stability of β-LG. The overall binding affinity was estimated about 1.74 × 103 M−1 through following UV spectral changes of β-LG at different concentrations of crocin. A 1:1 binding stoichiometry for the complex of crocin and β-LG was recognized using Job's method. The results of molecular docking and molecular dynamic simulation indicated that in addition to a single hydrogen bond with an oxygen linker attached to polyene chain, hydrophobic interactions play the major role in binding of crocin's polyene chain to β-LG surface. Three-dimensional emission and CD spectra showed conformational alterations in both tertiary and secondary structure of β-LG varying with crocin concentration. Depending on the temperature, crocin showed a dual effect on the thermodynamic stability of β-LG. Crocin destabilized β-LG up to room temperature, but stabilized at higher temperatures. The CD spectra of crocin in the Soret region and simulation results proved the bending of polyene chain and changes in the angle between sugar groups and polyene chain in combination with the protein. β-LG complexation enhanced the chemical stability of crocin by 20% during a 30-day storage, while its degradation was accelerated under UV irradiation. According to the results, it is predicted crocin functionalities to be affected by β-LG association and vice versa.

Ключевые слова

Lactoglobulin, Ligand, Crocin, Ligand binding, Binding constant, Circular dichroism spectroscopy

Название журнала

Food Hydrocolloids

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85085319926&doi=10.1016%2fj.foodhyd.2020.106003&partnerID=40&md5=5dee5ae83b4bebdb2d3da5be07ae461c

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https://repository.kpfu.ru/?p_id=235109

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Сироткин Владимир Александрович	ru_RU
dc.date.accessioned	2020-01-01T00:00:00Z	ru_RU
dc.date.available	2020-01-01T00:00:00Z	ru_RU
dc.date.issued	2020	ru_RU
dc.identifier.citation	Allahdad Z., Khammari A., Karami L., Khasemi A., Sirotkin V.A., Haertle T., Saboury A.A. Binding studies of crocin to b-Lactoglobulin and its impacts on both components. // Food Hydrocolloids. - 2020. - Vol.108, - Art. № 106003.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/?p_id=235109	ru_RU
dc.description.abstract	Food Hydrocolloids	ru_RU
dc.description.abstract	Light susceptibility of crocin and high degree of unsaturation limit its application in food systems. This study aimed to investigate the impact of molecular binding of crocin to β-lactoglobulin (β-LG) on crocin stability as well as the conformational stability of β-LG. The overall binding affinity was estimated about 1.74 × 103 M−1 through following UV spectral changes of β-LG at different concentrations of crocin. A 1:1 binding stoichiometry for the complex of crocin and β-LG was recognized using Job's method. The results of molecular docking and molecular dynamic simulation indicated that in addition to a single hydrogen bond with an oxygen linker attached to polyene chain, hydrophobic interactions play the major role in binding of crocin's polyene chain to β-LG surface. Three-dimensional emission and CD spectra showed conformational alterations in both tertiary and secondary structure of β-LG varying with crocin concentration. Depending on the temperature, crocin showed a dual effect on the thermodynamic stability of β-LG. Crocin destabilized β-LG up to room temperature, but stabilized at higher temperatures. The CD spectra of crocin in the Soret region and simulation results proved the bending of polyene chain and changes in the angle between sugar groups and polyene chain in combination with the protein. β-LG complexation enhanced the chemical stability of crocin by 20% during a 30-day storage, while its degradation was accelerated under UV irradiation. According to the results, it is predicted crocin functionalities to be affected by β-LG association and vice versa.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Lactoglobulin	ru_RU
dc.subject	Ligand	ru_RU
dc.subject	Crocin	ru_RU
dc.subject	Ligand binding	ru_RU
dc.subject	Binding constant	ru_RU
dc.subject	Circular dichroism spectroscopy	ru_RU
dc.title	Binding studies of crocin to b-Lactoglobulin and its impacts on both components	ru_RU
dc.type	Статьи в зарубежных журналах и сборниках	ru_RU