Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system

Adsorption and interactions of Bovine Serum Albumin (BSA) with Double Walled Carbon Nanotubes (DWNT) prepared by catalytic chemical vapor deposition (CCVD) synthesis were studied. Adsorption kinetics and equilibrium were investigated by means of in situ UV-spectroscopy. The extent of adsorption at different temperatures was determined at the end of a 420-min adsorption period. The adsorption equilibrium experiments were performed using various amounts of nanotubes at pH 4 and 40 °C, and the adsorption parameters were evaluated comparing the experimental data with models such as the Freundlich and Langmuir isotherms. The maximum protein adsorption capacity (Q0) of DWNT was determined as 1221 mg·g- 1. The effect of temperature on the adsorption rate experiments was investigated for constant amount of adsorbent at pH 4. Adsorption kinetics followed the pseudo-first-order rate. Zeta potential measurements were performed with respect to solution pH for understanding the protein-surface interactions. The interactions between positively charged BSA molecules with negatively charged DWNT at pH 4 were found to be electrostatic attractions. Thermodynamic parameters, ?H0 and ?S0 were found as 9.40 kJ·mol- 1 and 321.5 J·mol- 1 K- 1, respectively. ?H0 value indicated that BSA adsorption on DWNT was a physisorption process. © 2017 Elsevier B.V.

Yazar Kopac T.
Bozgeyik K.
Flahaut E.
Yayın Türü Article
Tek Biçim Adres https://hdl.handle.net/20.500.12628/4143
Tek Biçim Adres 10.1016/j.molliq.2017.12.100
Konu Başlıkları Adsorption
Bovine serum albumin
Double walled carbon nanotubes
Koleksiyonlar Araştırma Çıktıları | WoS | Scopus | TR-Dizin | PubMed | SOBİAD
Scopus İndeksli Yayınlar Koleksiyonu
WoS İndeksli Yayınlar Koleksiyonu
Dergi Adı Journal of Molecular Liquids
Dergi Cilt Bilgisi 252
Sayfalar 1 - 8
Yayın Yılı 2018
Eser Adı
[dc.title]
Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system
Yazar
[dc.contributor.author]
Kopac T.
Yazar
[dc.contributor.author]
Bozgeyik K.
Yazar
[dc.contributor.author]
Flahaut E.
Yayın Yılı
[dc.date.issued]
2018
Yayıncı
[dc.publisher]
Elsevier B.V.
Yayın Türü
[dc.type]
article
Özet
[dc.description.abstract]
Adsorption and interactions of Bovine Serum Albumin (BSA) with Double Walled Carbon Nanotubes (DWNT) prepared by catalytic chemical vapor deposition (CCVD) synthesis were studied. Adsorption kinetics and equilibrium were investigated by means of in situ UV-spectroscopy. The extent of adsorption at different temperatures was determined at the end of a 420-min adsorption period. The adsorption equilibrium experiments were performed using various amounts of nanotubes at pH 4 and 40 °C, and the adsorption parameters were evaluated comparing the experimental data with models such as the Freundlich and Langmuir isotherms. The maximum protein adsorption capacity (Q0) of DWNT was determined as 1221 mg·g- 1. The effect of temperature on the adsorption rate experiments was investigated for constant amount of adsorbent at pH 4. Adsorption kinetics followed the pseudo-first-order rate. Zeta potential measurements were performed with respect to solution pH for understanding the protein-surface interactions. The interactions between positively charged BSA molecules with negatively charged DWNT at pH 4 were found to be electrostatic attractions. Thermodynamic parameters, ?H0 and ?S0 were found as 9.40 kJ·mol- 1 and 321.5 J·mol- 1 K- 1, respectively. ?H0 value indicated that BSA adsorption on DWNT was a physisorption process. © 2017 Elsevier B.V.
Kayıt Giriş Tarihi
[dc.date.accessioned]
2019-12-23
Açık Erişim Tarihi
[dc.date.available]
2019-12-23
Yayın Dili
[dc.language.iso]
eng
Konu Başlıkları
[dc.subject]
Adsorption
Konu Başlıkları
[dc.subject]
Bovine serum albumin
Konu Başlıkları
[dc.subject]
Double walled carbon nanotubes
Haklar
[dc.rights]
info:eu-repo/semantics/closedAccess
ISSN
[dc.identifier.issn]
0167-7322
İlk Sayfa Sayısı
[dc.identifier.startpage]
1
Son Sayfa Sayısı
[dc.identifier.endpage]
8
Dergi Adı
[dc.relation.journal]
Journal of Molecular Liquids
Dergi Cilt Bilgisi
[dc.identifier.volume]
252
Tek Biçim Adres
[dc.identifier.uri]
https://dx.doi.org/10.1016/j.molliq.2017.12.100
Tek Biçim Adres
[dc.identifier.uri]
https://hdl.handle.net/20.500.12628/4143
Görüntülenme Sayısı ( Şehir )
Görüntülenme Sayısı ( Ülke )
Görüntülenme Sayısı ( Zaman Dağılımı )
Görüntülenme
12
09.12.2022 tarihinden bu yana
İndirme
1
09.12.2022 tarihinden bu yana
Son Erişim Tarihi
10 Şubat 2024 00:22
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Tıklayınız
adsorption Adsorption interactions determined parameters charged performed experiments kinetics equilibrium investigated Thermodynamic respect measurements potential pseudo-first-order followed adsorbent amount constant kJ·mol- J·mol- solution Elsevier understanding indicated electrostatic physisorption temperature process negatively molecules positively between protein-surface
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