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Α-Chymotrypsin in water-ethanol mixtures: Effect of preferential interactions

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dc.contributor.author Sirotkin V.
dc.contributor.author Kuchierskaya A.
dc.date.accessioned 2018-04-05T07:08:52Z
dc.date.available 2018-04-05T07:08:52Z
dc.date.issued 2017
dc.identifier.issn 0009-2614
dc.identifier.uri http://dspace.kpfu.ru/xmlui/handle/net/129382
dc.description.abstract © 2017 Elsevier B.V. We investigated preferential interactions of α-chymotrypsin with water–ethanol mixtures at 25 °C. Our approach is based on the analysis of residual enzyme activity and water/alcohol sorption. There are three concentration regimes. α-Chymotrypsin is preferentially hydrated at high water content. The residual enzyme activity is close to 100%. α-Chymotrypsin has a higher affinity for alcohol than for water at intermediate water content. Residual enzyme activity is close to zero in this concentration range. At low water content, ethanol is preferentially excluded from the protein surface. This results in preferential hydration of α-chymotrypsin and significant residual catalytic activity (∼50%) in water-poor ethanol.
dc.relation.ispartofseries Chemical Physics Letters
dc.subject Bovine pancreatic α-chymotrypsin
dc.subject Ethanol
dc.subject Preferential solvation and hydration
dc.subject Protein hydration
dc.subject Protein stabilization
dc.title Α-Chymotrypsin in water-ethanol mixtures: Effect of preferential interactions
dc.type Article
dc.relation.ispartofseries-volume 689
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 156
dc.source.id SCOPUS00092614-2017-689-SID85031731147

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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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