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language |
eng
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Author | |
Description | Circular dichroism spectroscopy revealed that the thermal stability of chicken egg white lysozyme in an aqueous buffer solution is significantly lowered by the addition of 6-O-α-D-glucosyl-β-cyclodextrin (G1-β-CD), whereas it is raised by the addition of methyl α-D-glucopyranoside. The α- and γ-cyclodextrin also lowered the thermal stability, although the effects were less prominent than that of G1-β-CD. Fluorescence spectroscopy suggested that cyclodextrins include the side chains of tryptophan residues within their internal cavities to lower the thermal stability of lysozyme. The fluorescence intensity of a sample, re-cooled to 25℃ after thermal denaturation at 75℃ in the presence of G1-β-CD, was stronger than that observed for native lysozyme. The fact that the fluorescence intensity of the re-cooling sample was stronger than that of the native one indicates that G1-β-CD persists in binding to the side chains of tryptophan residues of the re-cooled lysozyme.
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Subject | chicken egg white lysozyme
circular dichroism spectroscopy
cyclodextrin
fluorescence spectroscopy
inclusion
thermal stability
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Journal Title |
Journal of molecular structure
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Volume | 782
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Issue | 1
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Start Page | 60
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End Page | 66
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ISSN | 00222860
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Published Date | 2006-01-09
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DOI | |
DOI Date | 2013-04-01
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NCID | AA00702852
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Publisher | Elsevier
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DCMI | text
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NII Type |
Journal Article
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Format |
PDF
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Rights | Copyright c 2005 Elsevier B.V. All rights reserved.
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Text Version |
著者版
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OAI-PMH Set |
Faculty of Life and Environmental Science
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