Efficient purification of native recombinant proteins using proteases immobilized on cellulose

Dongming Lan; Yan Tai; Yanfei Shen; Fanghua Wang; Bo Yang; Yonghua Wang

doi:10.1016/j.jbiosc.2011.12.003

Efficient purification of native recombinant proteins using proteases immobilized on cellulose

J Biosci Bioeng. 2012 Apr;113(4):542-4. doi: 10.1016/j.jbiosc.2011.12.003. Epub 2012 Jan 23.

Authors

Dongming Lan¹, Yan Tai, Yanfei Shen, Fanghua Wang, Bo Yang, Yonghua Wang

Affiliation

¹ School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, PR China.

PMID: 22265893
DOI: 10.1016/j.jbiosc.2011.12.003

Abstract

Cellulose binding domain (CBD) fusion protease was employed to digest the CBD fusion protein. After cleavage, the tag free target proteins can be separated from the CBD tag and CBD fusion protease which still adsorbed to the cellulose by centrifugation. The green fluorescent protein was efficiently purified using this method.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cellulose / metabolism
Enzymes, Immobilized / metabolism*
Green Fluorescent Proteins / genetics
Green Fluorescent Proteins / isolation & purification
Peptide Hydrolases / metabolism*
Protein Binding
Protein Engineering / methods*
Recombinant Proteins / isolation & purification*

Substances

Enzymes, Immobilized
Recombinant Proteins
Green Fluorescent Proteins
Cellulose
Peptide Hydrolases