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Insights into the molecular interaction between sucrose and α-chymotrypsin

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dc.contributor.author Farhadian S.
dc.contributor.author Shareghi B.
dc.contributor.author Momeni L.
dc.contributor.author Abou-Zied O.
dc.contributor.author Sirotkin V.
dc.contributor.author Tachiya M.
dc.contributor.author Saboury A.
dc.date.accessioned 2019-01-22T20:35:31Z
dc.date.available 2019-01-22T20:35:31Z
dc.date.issued 2018
dc.identifier.issn 0141-8130
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/147858
dc.description.abstract © 2018 Elsevier B.V. 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 protecting the native structural conformation of α-Chy. Sucrose was preferentially excluded from the surface of α-Chy which is explained by the higher tendency of water toward favorable interactions with the functional groups of α-Chy than with sucrose.
dc.relation.ispartofseries International Journal of Biological Macromolecules
dc.subject Circular dichroism
dc.subject Fluorescence spectroscopy
dc.subject Molecular docking and dynamics
dc.subject Sucrose
dc.subject α-Chymotrypsin
dc.title Insights into the molecular interaction between sucrose and α-chymotrypsin
dc.type Article
dc.relation.ispartofseries-volume 114
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 950
dc.source.id SCOPUS01418130-2018-114-SID85045076621

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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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