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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Main Authors: Nasrul Arahman, Cut Meurah Rosnelly, Yusni Yusni, Afrillia Fahrina, Silmina Silmina, Aulia Chintia Ambarita, Muhammad Roil Bilad, Gunawan, Poernomo, Rajabzadeh, Saeid, Takagi, Ryosuke, Matsuyama, Hideto, Muhammad Aziz
Other Authors: School of Chemical and Biomedical Engineering
Format: Article
Language:English
Published: 2021
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Online Access:https://hdl.handle.net/10356/153451
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spelling sg-ntu-dr.10356-1534512023-12-29T06:45:22Z Ultrafiltration of α-lactalbumin protein : acquaintance of the filtration performance by membrane structure and surface alteration Nasrul Arahman Cut Meurah Rosnelly Yusni Yusni Afrillia Fahrina Silmina Silmina Aulia Chintia Ambarita Muhammad Roil Bilad Gunawan, Poernomo Rajabzadeh, Saeid Takagi, Ryosuke Matsuyama, Hideto Muhammad Aziz School of Chemical and Biomedical Engineering Universitas Syiah Kuala, Indonesia Universitas Syiah Kuala, Indonesia Universiti Brunei Darussalam Kobe University, Japan The University of Tokyo, Japan Engineering::Chemical engineering::Polymers and polymer manufacture Engineering::Chemical engineering::Processes and operations Polyethersulfone α-Lactalbumin Carbon Nanotubes Membrane Separation 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/(m2·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/(m2·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m2·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%. Published version This research was funded by the Indonesian Ministry of Education, Culture, Research, and Technology with grant contract number 46/UN11.2.1/PT.01.03/DRPM/2021 (Penelitian Dasar) 2021-12-03T05:57:37Z 2021-12-03T05:57:37Z 2021 Journal Article Nasrul Arahman, Cut Meurah Rosnelly, Yusni Yusni, Afrillia Fahrina, Silmina Silmina, Aulia Chintia Ambarita, Muhammad Roil Bilad, Gunawan, P., Rajabzadeh, S., Takagi, R., Matsuyama, H. & Muhammad Aziz (2021). Ultrafiltration of α-lactalbumin protein : acquaintance of the filtration performance by membrane structure and surface alteration. Polymers, 13(21), 3632-. https://dx.doi.org/10.3390/polym13213632 2073-4360 https://hdl.handle.net/10356/153451 10.3390/polym13213632 34771192 2-s2.0-85117891813 21 13 3632 en Polymers © 2021 by the authors. 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/). application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Chemical engineering::Polymers and polymer manufacture
Engineering::Chemical engineering::Processes and operations
Polyethersulfone
α-Lactalbumin
Carbon Nanotubes
Membrane Separation
spellingShingle Engineering::Chemical engineering::Polymers and polymer manufacture
Engineering::Chemical engineering::Processes and operations
Polyethersulfone
α-Lactalbumin
Carbon Nanotubes
Membrane Separation
Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
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/(m2·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/(m2·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m2·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%.
author2 School of Chemical and Biomedical Engineering
author_facet School of Chemical and Biomedical Engineering
Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
Muhammad Aziz
format Article
author Nasrul Arahman
Cut Meurah Rosnelly
Yusni Yusni
Afrillia Fahrina
Silmina Silmina
Aulia Chintia Ambarita
Muhammad Roil Bilad
Gunawan, Poernomo
Rajabzadeh, Saeid
Takagi, Ryosuke
Matsuyama, Hideto
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
publishDate 2021
url https://hdl.handle.net/10356/153451
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