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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: Arahman, Nasrul, Rosnelly, Cut Meurah, Yusni, Yusni, Fahrina, Afrillia, Silmina, Silmina, Ambarita, Aulia Chintia, Bilad, Muhammad Roil, Gunawan, Poernomo, Rajabzadeh, Saeid, Takagi, Ryosuke, Matsuyama, Hideto, Aziz, Muhammad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8587019/
https://www.ncbi.nlm.nih.gov/pubmed/34771192
http://dx.doi.org/10.3390/polym13213632
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author Arahman, Nasrul
Rosnelly, Cut Meurah
Yusni, Yusni
Fahrina, Afrillia
Silmina, Silmina
Ambarita, Aulia Chintia
Bilad, Muhammad Roil
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
Aziz, Muhammad
author_facet Arahman, Nasrul
Rosnelly, Cut Meurah
Yusni, Yusni
Fahrina, Afrillia
Silmina, Silmina
Ambarita, Aulia Chintia
Bilad, Muhammad Roil
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
Aziz, Muhammad
author_sort Arahman, Nasrul
collection PubMed
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(2)·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(2)·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m(2)·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%.
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spelling pubmed-85870192021-11-13 Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration Arahman, Nasrul Rosnelly, Cut Meurah Yusni, Yusni Fahrina, Afrillia Silmina, Silmina Ambarita, Aulia Chintia Bilad, Muhammad Roil Gunawan, Poernomo Rajabzadeh, Saeid Takagi, Ryosuke Matsuyama, Hideto Aziz, Muhammad Polymers (Basel) Article 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(2)·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(2)·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m(2)·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%. MDPI 2021-10-21 /pmc/articles/PMC8587019/ /pubmed/34771192 http://dx.doi.org/10.3390/polym13213632 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Arahman, Nasrul
Rosnelly, Cut Meurah
Yusni, Yusni
Fahrina, Afrillia
Silmina, Silmina
Ambarita, Aulia Chintia
Bilad, Muhammad Roil
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
Aziz, Muhammad
Ultrafiltration of α-Lactalbumin Protein: Acquaintance of the Filtration Performance by Membrane Structure and Surface Alteration
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8587019/
https://www.ncbi.nlm.nih.gov/pubmed/34771192
http://dx.doi.org/10.3390/polym13213632
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