A preparative purification process for recombinant hepatitis B core antigen using online capture by expanded bed adsorption followed by size-exclusion chromatography.

Abstract:

:Hepatitis B core antigen (HBcAg) is an important serological marker used in the diagnosis of hepatitis B virus (HBV) infections. In the current study, a fast and efficient preparative purification protocol for truncated HBcAg from Escherichia coli disruptate was developed. The recombinant HBcAg was first captured by anion exchange expanded bed adsorption chromatography integrated with a cell disruption process. This online capture process has shortened the process time and eliminated the "hold-up" period that may be detrimental to the quality of target protein. The eluted product from the expanded bed adsorption chromatography was subsequently purified using size-exclusion chromatography. The results showed that this novel purification protocol achieved a recovery yield of 45.1% with a product purity of 88.2%, which corresponds to a purification factor of 4.5. The recovered HBcAg is still biologically active as shown by ELISA test.

journal_name

J Microbiol Biotechnol

authors

Ho CW,Tan WS,Chong FC,Ling TC,Tey BT

doi

10.4014/jmb.0804.254

subject

Has Abstract

pub_date

2009-04-01 00:00:00

pages

416-23

issue

4

eissn

1017-7825

issn

1738-8872

pii

8255

journal_volume

19

pub_type

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