Current affinity approaches for purification of recombinant proteins. Issue 1 (1st January 2019)

• Record Type: Journal Article
• Authors: Mahmoodi, Sahar; Pourhassan-Moghaddam, Mohammad; Wood, David W.; Majdi, Hasan; Zarghami, Nosratollah
• Editors: Hatti Kaul, Rajni
• Is Part Of: Cogent biology. Volume 5:Issue 1(2019)
• Publication Date: 2019-01-01
• Subjects: recombinant protein -- affinity purification -- fusion purification; Biology -- Periodicals; Biology; Periodicals; 570.5
• DOI: 10.1080/23312025.2019.1665406
• Languages: English
• ISSNs: 2331-2025

Abstract

Abstract: Recombinant proteins have wide applications in the development of pharmaceutical compounds, industrial applications of enzymes, and basic proteomics research. In this way, efficient production of recombinant proteins with high purity needs efficient purification methods. Various strategies have been devised to improve these proteins purification such as affinity purification and physicochemical purification methods which the affinity purification has some advantages over the others. Affinity strategies especially fusion strategies have been devised as indispensable tools for the massive parallel production, identification and purification of recombinant proteins from the host systems. These strategies facilitate commercial and industrial formulations of recombinant proteins, improve the study of protein interactions at the molecular level, and develop highly sensitive and specific bioassays. Recently, various surface-modified nanoparticles have been widely developed to enhance recovery and purification of recombinant proteins such as Hydrophobic polymer nanoparticles and Oleosin nanoparticles. In this review, we aim to discuss affinity purification technologies and address the principles, advantages, limitations and potential applications of them.