Improvement of protein binding capacity of acrylic-acid-grafted fibers by polymer root-to-brush shift

Yuka Matsuzaki; Takeshi Itabashi; Shigeko Kawai-Noma; Daisuke Umeno; Kyoichi Saito

doi:10.1016/j.radphyschem.2018.12.022

Improvement of protein binding capacity of acrylic-acid-grafted fibers by polymer root-to-brush shift

Yuka Matsuzaki, Takeshi Itabashi, Shigeko Kawai-Noma, Daisuke Umeno, Kyoichi Saito^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

A weak acid cation exchange fiber used for large-scale antibody purification was prepared by radiation-induced graft polymerization of acrylic acid (AA) onto a commercially available nylon-6 fiber. The AA-grafted fiber was post-treated by conditioning in NaOH aqueous solution at 298 K followed by immersion in water at 353 K to increase the protein binding capacity of the cation exchange fiber. A 2 g/L lysozyme solution buffered at pH 6.0 flowed through a column charged with a treated or untreated AA-grafted fiber at a space velocity of 20 h ⁻¹ . The 10% dynamic binding capacity of the column charged with the former fiber of 200 mg/mL-column was 5.9-fold that of the column charged with the latter fiber, and 2.3-fold that (88 mg/mL-column) of a column charged with CM Sepharose™ Fast Flow (GE Healthcare).

Original language	English
Pages (from-to)	131-136
Number of pages	6
Journal	Radiation Physics and Chemistry
Volume	158
DOIs	https://doi.org/10.1016/j.radphyschem.2018.12.022
Publication status	Published - 2019 May
Externally published	Yes

Keywords

Acrylic-acid-grafted fiber
Conditioning with alkaline solution
Immersion in hot water
Protein-binding capacity
Radiation-induced graft polymerization

ASJC Scopus subject areas

Radiation

Access to Document

10.1016/j.radphyschem.2018.12.022

Cite this

@article{d597f2e984b94692a82a392b5d7ce5f0,

title = "Improvement of protein binding capacity of acrylic-acid-grafted fibers by polymer root-to-brush shift",

abstract = " A weak acid cation exchange fiber used for large-scale antibody purification was prepared by radiation-induced graft polymerization of acrylic acid (AA) onto a commercially available nylon-6 fiber. The AA-grafted fiber was post-treated by conditioning in NaOH aqueous solution at 298 K followed by immersion in water at 353 K to increase the protein binding capacity of the cation exchange fiber. A 2 g/L lysozyme solution buffered at pH 6.0 flowed through a column charged with a treated or untreated AA-grafted fiber at a space velocity of 20 h −1 . The 10% dynamic binding capacity of the column charged with the former fiber of 200 mg/mL-column was 5.9-fold that of the column charged with the latter fiber, and 2.3-fold that (88 mg/mL-column) of a column charged with CM Sepharose{\texttrademark} Fast Flow (GE Healthcare). ",

keywords = "Acrylic-acid-grafted fiber, Conditioning with alkaline solution, Immersion in hot water, Protein-binding capacity, Radiation-induced graft polymerization",

author = "Yuka Matsuzaki and Takeshi Itabashi and Shigeko Kawai-Noma and Daisuke Umeno and Kyoichi Saito",

note = "Publisher Copyright: {\textcopyright} 2019 Elsevier Ltd",

year = "2019",

month = may,

doi = "10.1016/j.radphyschem.2018.12.022",

language = "English",

volume = "158",

pages = "131--136",

journal = "Radiation Physics and Chemistry",

issn = "0969-806X",

publisher = "Elsevier Limited",

}

TY - JOUR

T1 - Improvement of protein binding capacity of acrylic-acid-grafted fibers by polymer root-to-brush shift

AU - Matsuzaki, Yuka

AU - Itabashi, Takeshi

AU - Kawai-Noma, Shigeko

AU - Umeno, Daisuke

AU - Saito, Kyoichi

PY - 2019/5

Y1 - 2019/5

N2 - A weak acid cation exchange fiber used for large-scale antibody purification was prepared by radiation-induced graft polymerization of acrylic acid (AA) onto a commercially available nylon-6 fiber. The AA-grafted fiber was post-treated by conditioning in NaOH aqueous solution at 298 K followed by immersion in water at 353 K to increase the protein binding capacity of the cation exchange fiber. A 2 g/L lysozyme solution buffered at pH 6.0 flowed through a column charged with a treated or untreated AA-grafted fiber at a space velocity of 20 h −1 . The 10% dynamic binding capacity of the column charged with the former fiber of 200 mg/mL-column was 5.9-fold that of the column charged with the latter fiber, and 2.3-fold that (88 mg/mL-column) of a column charged with CM Sepharose™ Fast Flow (GE Healthcare).

AB - A weak acid cation exchange fiber used for large-scale antibody purification was prepared by radiation-induced graft polymerization of acrylic acid (AA) onto a commercially available nylon-6 fiber. The AA-grafted fiber was post-treated by conditioning in NaOH aqueous solution at 298 K followed by immersion in water at 353 K to increase the protein binding capacity of the cation exchange fiber. A 2 g/L lysozyme solution buffered at pH 6.0 flowed through a column charged with a treated or untreated AA-grafted fiber at a space velocity of 20 h −1 . The 10% dynamic binding capacity of the column charged with the former fiber of 200 mg/mL-column was 5.9-fold that of the column charged with the latter fiber, and 2.3-fold that (88 mg/mL-column) of a column charged with CM Sepharose™ Fast Flow (GE Healthcare).

KW - Acrylic-acid-grafted fiber

KW - Conditioning with alkaline solution

KW - Immersion in hot water

KW - Protein-binding capacity

KW - Radiation-induced graft polymerization

UR - http://www.scopus.com/inward/record.url?scp=85061672675&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85061672675&partnerID=8YFLogxK

U2 - 10.1016/j.radphyschem.2018.12.022

DO - 10.1016/j.radphyschem.2018.12.022

M3 - Article

AN - SCOPUS:85061672675

SN - 0969-806X

VL - 158

SP - 131

EP - 136

JO - Radiation Physics and Chemistry

JF - Radiation Physics and Chemistry

ER -

Improvement of protein binding capacity of acrylic-acid-grafted fibers by polymer root-to-brush shift

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this