Overexpression, purification and characterization of a recombinant secretary catalase from Bacillus subtilis
Document Type
Article
Publication Title
Biotechnology Letters
ISSN
0141-5492
Volume
30
Issue
1
DOI
10.1007/s10529-007-9510-7
First Page
181
Last Page
186
Publication Date
1-1-2008
Abstract
A recombinant Bacillus subtilis strain (KN25) was generated for the large-scale preparation of catalase. The B. subtilis katA gene encoding for catalase was cloned into the shuttle vector PRB374, downstream of the constitutively active vegII promoter, followed by transformation of the B. subtilis strain WB600 with the plasmid. The transformant strain, KN25 secretes high levels (3,500 U/ml) of catalase, which facilitates its purification. Three simple purification steps yielded nearly homogeneous catalase, with approximately 70% recovery. The purified recombinant catalase has a specific activity of 34,600 U/mg under optimal conditions, and is more resistant to acidic conditions than bovine liver catalase.
Recommended Citation
Shi, X.,
Feng, M.,
Zhao, Y.,
Guo, X.,
&
Zhou, P.
(2008).
Overexpression, purification and characterization of a recombinant secretary catalase from Bacillus subtilis.
Biotechnology Letters, 30(1), 181–186.
DOI: 10.1007/s10529-007-9510-7
https://scholarlycommons.pacific.edu/phs-facarticles/292
