Biopolymer monolith for protein purification

Yoshiko Miura, Hirokazu Seto, Makoto Shibuya, Yu Hoshino

Research output: Contribution to journalArticle

Abstract

Porous glycopolymers, "glycomonoliths", were prepared by radical polymerization based on polymerization-induced phase separation with an acrylamide derivative of α-mannose, acrylamide and cross-linker in order to investigate protein adsorption and separation. The porous structure was induced by a porogenic alcohol. The pore diameter and surface area were controlled by the type of alcohol. The protein adsorption was measured in both batch and continuous flow systems. The glycomonoliths showed specific interaction with the sugar recognition protein of concanavalin A, and non-specific interaction to other proteins was negligible. The amount of protein adsorption to the materials was determined by the sugar density and the composition of the glycomonoliths. Fundamental knowledge regarding the glycomonoliths for protein separation was obtained.

Original languageEnglish
Pages (from-to)154-167
Number of pages14
JournalFaraday Discussions
Volume219
DOIs
Publication statusPublished - Jan 1 2019

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Biopolymers
biopolymers
purification
Purification
proteins
Proteins
Acrylamide
sugars
Adsorption
Sugars
adsorption
alcohols
polymerization
Alcohols
Mannose
Concanavalin A
Free radical polymerization
Phase separation
Polymerization
interactions

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry

Cite this

Biopolymer monolith for protein purification. / Miura, Yoshiko; Seto, Hirokazu; Shibuya, Makoto; Hoshino, Yu.

In: Faraday Discussions, Vol. 219, 01.01.2019, p. 154-167.

Research output: Contribution to journalArticle

Miura, Yoshiko ; Seto, Hirokazu ; Shibuya, Makoto ; Hoshino, Yu. / Biopolymer monolith for protein purification. In: Faraday Discussions. 2019 ; Vol. 219. pp. 154-167.
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