In silico design of high-affinity ligands for the immobilization of inulinase
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- 作者：M.G. Holyavkaa ; marinaholyavka@yahoo.com" class="auth_mail" title="E-mail the corresponding author ; M.S. Kondratyevb ; ma-ko@bk.ru" class="auth_mail" title="E-mail the corresponding author ; A.A. Samchenkob ; sam4enkoaa@mail.ru" class="auth_mail" title="E-mail the corresponding author ; A.V. Kabanovb ; kabanov@mail.ru" class="auth_mail" title="E-mail the corresponding author ; V.M. Komarovb ; komarov@icb.psn.ru" class="auth_mail" title="E-mail the corresponding author ; V.G. Artyukhova ; artyukhov@bio.vsu.ru" class="auth_mail" title="E-mail the corresponding author
- 关键词：Computer modeling ; Inulinase ; Immobilization ; Ligand ; Docking
- 刊名：Computers in Biology and Medicine
- 出版年：2016
- 出版时间：1 April 2016
- 年：2016
- 卷：71
- 期：Complete
- 页码：198-204
- 全文大小：2424 K
文摘
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For the immobilization matrices we revealed the binding site with the inulinase.
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Ion exchange resins and fibers were experimentally tested.
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The maximal affinity to the inulinase was possessed by the matrix of KU-2.
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Affinities were in good agreement with catalytic activity of immobilized inulinase.
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Correlation factors are −0.84 (for yeast inulinase) and −0.81 (for plant inulinase).