| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2018 |
| Язык | английский |
|
Сироткин Владимир Александрович, автор
|
| Библиографическое описание на языке оригинала |
Farhadian, S. Insights into the molecular interaction between sucrose and a-chymotrypsin. [Text]/ S. Farhadian, B. Shareghi, L. Momeni, O. K.Abou-Zied, V.A. Sirotkin, M. Tachiya, A.A. Saboury // International Journal of Biological Macromolecules. - 2018. - Vol. 114. - P.950-960. |
| Аннотация |
One of the most important purposes of enzyme engineering is to increase the thermal and kinetic stability of enzymes, which is an important factor for using enzymes in industry. The purpose of the present study is to achieve a higher thermal stability of α-chymotrypsin (α-Chy) by modification of the solvent environment. The influence of sucrose was investigated using thermal denaturation analysis, fluorescence spectroscopy, circular dichroism, molecular docking and molecular dynamics (MD) simulations. The results point to the effect of sucrose in enhancing the α-Chy stability. Fluorescence spectroscopy revealed one binding site that is dominated by static quenching. Molecular docking and MD simulation results indicate that hydrogen bonding and van der Waals forces play a major role in stabilizing the complex. Tm of this complex was enhanced due to the higher H-bond formation and the lower surface hydrophobicity after sucrose modification. The results show the ability of sucrose in prot |
| Ключевые слова |
chymotrypsin, sucrose, enzyme engineering, thermal denaturation analysis, fluorescence spectroscopy, circular dichroism, molecular docking, molecular dynamics simulations |
| Название журнала |
International Journal of Biological Macromolecules
|
| URL |
https://www.sciencedirect.com/science/article/pii/S0141813018300990 |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=179420 |
Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Сироткин Владимир Александрович |
ru_RU |
| dc.date.accessioned |
2018-01-01T00:00:00Z |
ru_RU |
| dc.date.available |
2018-01-01T00:00:00Z |
ru_RU |
| dc.date.issued |
2018 |
ru_RU |
| dc.identifier.citation |
Farhadian, S. Insights into the molecular interaction between sucrose and a-chymotrypsin. [Text]/ S. Farhadian, B. Shareghi, L. Momeni, O. K.Abou-Zied, V.A. Sirotkin, M. Tachiya, A.A. Saboury // International Journal of Biological Macromolecules. - 2018. - Vol. 114. - P.950-960. |
ru_RU |
| dc.identifier.uri |
https://repository.kpfu.ru/?p_id=179420 |
ru_RU |
| dc.description.abstract |
International Journal of Biological Macromolecules |
ru_RU |
| dc.description.abstract |
One of the most important purposes of enzyme engineering is to increase the thermal and kinetic stability of enzymes, which is an important factor for using enzymes in industry. The purpose of the present study is to achieve a higher thermal stability of α-chymotrypsin (α-Chy) by modification of the solvent environment. The influence of sucrose was investigated using thermal denaturation analysis, fluorescence spectroscopy, circular dichroism, molecular docking and molecular dynamics (MD) simulations. The results point to the effect of sucrose in enhancing the α-Chy stability. Fluorescence spectroscopy revealed one binding site that is dominated by static quenching. Molecular docking and MD simulation results indicate that hydrogen bonding and van der Waals forces play a major role in stabilizing the complex. Tm of this complex was enhanced due to the higher H-bond formation and the lower surface hydrophobicity after sucrose modification. The results show the ability of sucrose in prot |
ru_RU |
| dc.language.iso |
ru |
ru_RU |
| dc.subject |
chymotrypsin |
ru_RU |
| dc.subject |
sucrose |
ru_RU |
| dc.subject |
enzyme engineering |
ru_RU |
| dc.subject |
thermal denaturation analysis |
ru_RU |
| dc.subject |
fluorescence spectroscopy |
ru_RU |
| dc.subject |
circular dichroism |
ru_RU |
| dc.subject |
molecular docking |
ru_RU |
| dc.subject |
molecular dynamics simulations |
ru_RU |
| dc.title |
Insights into the molecular interaction between sucrose and a-chymotrypsin |
ru_RU |
| dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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