Two-step purification of elastin-like polypeptide-fusion superoxide dismutase via hydrophobicity and thermoresponsiveness.

ABSTRACT:

Introduction

Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to oxygen and hydrogen peroxide, serving as a key antioxidant enzyme with important therapeutic and industrial applications. However, the purification of recombinant SOD remains challenging due to low expression levels and the complexity of traditional purification methods, which involve time-consuming and multi-step chromatography. Elastin-like polypeptides (ELPs) offer a promising alternative due to their hydrophobic and thermoresponsive properties, which can be leveraged for non-chromatographic purification.

Methods

A fusion protein of human SOD and an ELP tag (hSOD-ELP) was produced. The purification strategy consisted of two sequential steps. First, foam separation was employed, exp

SUBMITTER: Wang W 

PROVIDER: S-EPMC12592124 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature