Selective Adsorption and Separation of Proteins by Ligand-Modified Nanofiber Fabric.

Song Liu,Yasuhito Mukai

doi:10.3390/polym13142313

Abstract

Electrospun polyvinyl alcohol (PVA) nanofiber fabric was modified by Cibacron Blue F3GA (CB) to enhance the affinity of the fabric. Batch experiments were performed to study the nanofiber fabric’s bovine hemoglobin (BHb) adsorption capacity at different protein concentrations before and after modification. The maximum BHb adsorption capacity of the modified nanofiber fabric was 686 mg/g, which was much larger than the 58 mg/g of the original fabric. After that, the effect of feed concentration and permeation rate on the dynamic adsorption behaviors for BHb of the nanofiber fabric was investigated. The pH impact on BHb and bovine serum albumin (BSA) adsorption was examined by static adsorption experiments of single protein solutions. The selective separation experiments of the BHb–BSA binary solution were carried out at the optimal pH value, and a high selectivity factor of 5.45 for BHb was achieved. Finally, the reusability of the nanofiber fabric was examined using three adsorption–elution cycle tests. This research demonstrated the potential of the CB-modified PVA nanofiber fabric in protein adsorption and selective separation.

Highlights

Proteins are biological macromolecules that maintain the integrity of the cell structure and function [1]
Morphologies of the polyvinyl alcohol (PVA) nanofiber fabrics before and after Cibacron Blue F3GA (CB) modification were observed by scanning electron microscopy (SEM, S4300, Hitachi High-Technologies Corporation, Tokyo, Japan), operating at 15 kV
CB-modified PVA nanofiber fabrics were fabricated via immobilization of CB molecules on the nanofiber surface

Summary

Introduction

Proteins are biological macromolecules that maintain the integrity of the cell structure and function [1]. The cells of living organisms consist of different kinds of proteins, each of which has a different structure and function [3,4,5]. Proteins generally exist in complex mixed forms in tissues and cells, and various types of cells contain thousands of different proteins. As proteins vary in size, charge and water solubility, it is challenging to obtain target proteins from mixtures [6,7]. The overall goal of protein isolation and purification is to increase the purity of the product and to maintain the isolated protein’s biological activity. It is desirable to achieve high production efficiency and high product quality while reducing the cost of the isolation process

Methods

Results

Conclusion