Effects of Hydrophobic Nanospaces on Structures of Lysozyme
Adsorption of lysozyme on carbon nanospaces was studied by measurement of structures and biological activities of the adsorbed lysozyme. Carbon aerogel (CA) was used as the carbon material. Several kinds of CAs with different pore sizes were prepared. Porosities of CAs were characterized by a nitrog...
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SAGE Publishing
2015-01-01
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Series: | Adsorption Science & Technology |
Online Access: | https://doi.org/10.1260/0263-6174.33.1.63 |
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author | Koki Takenaka Tomonori Ohaba Kazuo Takei Kuniko Akama Joaquin Silvestre-Albero Hirofumi Kanoh |
author_facet | Koki Takenaka Tomonori Ohaba Kazuo Takei Kuniko Akama Joaquin Silvestre-Albero Hirofumi Kanoh |
author_sort | Koki Takenaka |
collection | DOAJ |
description | Adsorption of lysozyme on carbon nanospaces was studied by measurement of structures and biological activities of the adsorbed lysozyme. Carbon aerogel (CA) was used as the carbon material. Several kinds of CAs with different pore sizes were prepared. Porosities of CAs were characterized by a nitrogen adsorption measurement at 77 K. Adsorption measurements showed that mesopores with diameters between 15 and 25 nm were the most suitable for lysozyme adsorption. However, because the size of lysozyme is less than 5 nm in length, this adsorption behaviour suggests that lysozyme molecules may associate with one another to form clusters on mesopores of CAs. This is a unique behaviour because it is well-known that lysozyme indicates monolayer adsorption on the flat surface. The X-ray diffraction patterns of lysozyme-adsorbed CA showed a few peaks originating from the structure of lysozyme. The strongest peak of a bulk species of lysozyme was shifted by heating because of changes in its secondary structures. Lysozyme-adsorbed CA showed behaviours different from that of bulk species of lysozyme on heating. The recovery of biological activity of lysozyme denatured by heating was promoted by CA. Thus, hydrophobic mesopores of CA influence the stability of the structure of lysozyme. |
format | Article |
id | doaj-art-f340d2eec80c4a89a701097e5a007e1a |
institution | Kabale University |
issn | 0263-6174 2048-4038 |
language | English |
publishDate | 2015-01-01 |
publisher | SAGE Publishing |
record_format | Article |
series | Adsorption Science & Technology |
spelling | doaj-art-f340d2eec80c4a89a701097e5a007e1a2025-01-03T00:11:56ZengSAGE PublishingAdsorption Science & Technology0263-61742048-40382015-01-013310.1260/0263-6174.33.1.63Effects of Hydrophobic Nanospaces on Structures of LysozymeKoki Takenaka0Tomonori Ohaba1Kazuo Takei2Kuniko Akama3Joaquin Silvestre-Albero4Hirofumi Kanoh5 Graduate School of Science, Chiba University, 1-33 Yayoi-Cho, Inage-Ku, Chiba, Japan Graduate School of Science, Chiba University, 1-33 Yayoi-Cho, Inage-Ku, Chiba, Japan Graduate School of Science, Chiba University, 1-33 Yayoi-Cho, Inage-Ku, Chiba, Japan Center for General Education, Chiba University, 1-33 Yayoi-Cho, Inage-Ku, Chiba, Japan Laboratory for Advanced Materials, University of Alicante, Carretera San Vicente-Alicante, Alicante, Spain Graduate School of Science, Chiba University, 1-33 Yayoi-Cho, Inage-Ku, Chiba, JapanAdsorption of lysozyme on carbon nanospaces was studied by measurement of structures and biological activities of the adsorbed lysozyme. Carbon aerogel (CA) was used as the carbon material. Several kinds of CAs with different pore sizes were prepared. Porosities of CAs were characterized by a nitrogen adsorption measurement at 77 K. Adsorption measurements showed that mesopores with diameters between 15 and 25 nm were the most suitable for lysozyme adsorption. However, because the size of lysozyme is less than 5 nm in length, this adsorption behaviour suggests that lysozyme molecules may associate with one another to form clusters on mesopores of CAs. This is a unique behaviour because it is well-known that lysozyme indicates monolayer adsorption on the flat surface. The X-ray diffraction patterns of lysozyme-adsorbed CA showed a few peaks originating from the structure of lysozyme. The strongest peak of a bulk species of lysozyme was shifted by heating because of changes in its secondary structures. Lysozyme-adsorbed CA showed behaviours different from that of bulk species of lysozyme on heating. The recovery of biological activity of lysozyme denatured by heating was promoted by CA. Thus, hydrophobic mesopores of CA influence the stability of the structure of lysozyme.https://doi.org/10.1260/0263-6174.33.1.63 |
spellingShingle | Koki Takenaka Tomonori Ohaba Kazuo Takei Kuniko Akama Joaquin Silvestre-Albero Hirofumi Kanoh Effects of Hydrophobic Nanospaces on Structures of Lysozyme Adsorption Science & Technology |
title | Effects of Hydrophobic Nanospaces on Structures of Lysozyme |
title_full | Effects of Hydrophobic Nanospaces on Structures of Lysozyme |
title_fullStr | Effects of Hydrophobic Nanospaces on Structures of Lysozyme |
title_full_unstemmed | Effects of Hydrophobic Nanospaces on Structures of Lysozyme |
title_short | Effects of Hydrophobic Nanospaces on Structures of Lysozyme |
title_sort | effects of hydrophobic nanospaces on structures of lysozyme |
url | https://doi.org/10.1260/0263-6174.33.1.63 |
work_keys_str_mv | AT kokitakenaka effectsofhydrophobicnanospacesonstructuresoflysozyme AT tomonoriohaba effectsofhydrophobicnanospacesonstructuresoflysozyme AT kazuotakei effectsofhydrophobicnanospacesonstructuresoflysozyme AT kunikoakama effectsofhydrophobicnanospacesonstructuresoflysozyme AT joaquinsilvestrealbero effectsofhydrophobicnanospacesonstructuresoflysozyme AT hirofumikanoh effectsofhydrophobicnanospacesonstructuresoflysozyme |