Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration

α-Lactalbumin is an essential protein with multiple roles in physiological and the nutritional functionalities, such as diabetic prevention, blood pressure stabilization, and cancer cell inhibition. In the present work, polyethersulfone (PES)-based membranes were developed by incorporating Pluronic...

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Autores principales: Nasrul Arahman, Cut Meurah Rosnelly, Yusni Yusni, Afrillia Fahrina, Silmina Silmina, Aulia Chintia Ambarita, Muhammad Roil Bilad, Poernomo Gunawan, Saeid Rajabzadeh, Ryosuke Takagi, Hideto Matsuyama, Muhammad Aziz
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Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:b6ec170b84e8485c8255fba2f18f19b52021-11-11T18:42:11ZUltrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration10.3390/polym132136322073-4360https://doaj.org/article/b6ec170b84e8485c8255fba2f18f19b52021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4360/13/21/3632https://doaj.org/toc/2073-4360α-Lactalbumin is an essential protein with multiple roles in physiological and the nutritional functionalities, such as diabetic prevention, blood pressure stabilization, and cancer cell inhibition. In the present work, polyethersulfone (PES)-based membranes were developed by incorporating Pluronic F127 and carbon nanotubes with single- and multi-walled dimensions (Sw-Cnts and Mw-Cnts) as additives. The resulting membranes were evaluated for use in the filtration of α-lactalbumin protein solution. Four series of membranes, including PES pristine membrane, were fabricated via the phase inversion process. The characteristics of the membrane samples were analyzed in terms of morphology, membrane surface hydrophilicity and roughness, and surface chemistry. The characterization results show that the incorporation of additive increased the surface wettability by reducing the surface water contact angle from 80.4° to 64.1° by adding F127 and Mw-Cnt additives. The highest pure water permeability of 135 L/(m<sup>2</sup>·h·bar) was also exhibited by the PES/F127/Mw-Cnt membrane. The performance of the modified membranes was clearly better than the pristine PSF for α-lactalbumin solution filtration. The permeability of α-lactalbumin solution increased from 9.0 L/(m<sup>2</sup>·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m<sup>2</sup>·h·bar) for membranes loaded with Pluronic F127, Sw-Cnts, and Mw-Cnts, respectively. Those increments corresponded to 17, 22, and 28%. Such increments could be achieved without altering the α-lactalbumin rejections of 80%. Remarkably, the rejection for the membrane loaded with Sw-Cnts even increased to 89%.Nasrul ArahmanCut Meurah RosnellyYusni YusniAfrillia FahrinaSilmina SilminaAulia Chintia AmbaritaMuhammad Roil BiladPoernomo GunawanSaeid RajabzadehRyosuke TakagiHideto MatsuyamaMuhammad AzizMDPI AGarticlepolyethersulfoneα-lactalbuminsingle-walled carbon nanotubemulti-walled carbon nanotubemembrane roughnessOrganic chemistryQD241-441ENPolymers, Vol 13, Iss 3632, p 3632 (2021)
institution DOAJ
collection DOAJ
language EN
topic polyethersulfone
α-lactalbumin
single-walled carbon nanotube
multi-walled carbon nanotube
membrane roughness
Organic chemistry
QD241-441
spellingShingle polyethersulfone
α-lactalbumin
single-walled carbon nanotube
multi-walled carbon nanotube
membrane roughness
Organic chemistry
QD241-441
Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Poernomo Gunawan
Saeid Rajabzadeh
Ryosuke Takagi
Hideto Matsuyama
Muhammad Aziz
Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
description α-Lactalbumin is an essential protein with multiple roles in physiological and the nutritional functionalities, such as diabetic prevention, blood pressure stabilization, and cancer cell inhibition. In the present work, polyethersulfone (PES)-based membranes were developed by incorporating Pluronic F127 and carbon nanotubes with single- and multi-walled dimensions (Sw-Cnts and Mw-Cnts) as additives. The resulting membranes were evaluated for use in the filtration of α-lactalbumin protein solution. Four series of membranes, including PES pristine membrane, were fabricated via the phase inversion process. The characteristics of the membrane samples were analyzed in terms of morphology, membrane surface hydrophilicity and roughness, and surface chemistry. The characterization results show that the incorporation of additive increased the surface wettability by reducing the surface water contact angle from 80.4° to 64.1° by adding F127 and Mw-Cnt additives. The highest pure water permeability of 135 L/(m<sup>2</sup>·h·bar) was also exhibited by the PES/F127/Mw-Cnt membrane. The performance of the modified membranes was clearly better than the pristine PSF for α-lactalbumin solution filtration. The permeability of α-lactalbumin solution increased from 9.0 L/(m<sup>2</sup>·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m<sup>2</sup>·h·bar) for membranes loaded with Pluronic F127, Sw-Cnts, and Mw-Cnts, respectively. Those increments corresponded to 17, 22, and 28%. Such increments could be achieved without altering the α-lactalbumin rejections of 80%. Remarkably, the rejection for the membrane loaded with Sw-Cnts even increased to 89%.
format article
author Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Poernomo Gunawan
Saeid Rajabzadeh
Ryosuke Takagi
Hideto Matsuyama
Muhammad Aziz
author_facet Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Poernomo Gunawan
Saeid Rajabzadeh
Ryosuke Takagi
Hideto Matsuyama
Muhammad Aziz
author_sort Nasrul Arahman
title Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title_short Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title_full Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title_fullStr Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title_full_unstemmed Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title_sort ultrafiltration of α-lactalbumin protein: acquaintance of the filtration performance by membrane structure and surface alteration
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/b6ec170b84e8485c8255fba2f18f19b5
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