Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isolectric focusing slab two-dimensinal gel = 바실러스 유래의 세린 프로티아제의 규명

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Title
Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isolectric focusing slab two-dimensinal gel = 바실러스 유래의 세린 프로티아제의 규명
Author(s)
Nack-Shick Choi; Jong Hyun Choi; Jung-Hoon Yoon; Seung Goo LeeJae Jun Song
Bibliographic Citation
Biotechnology Letters, vol. 31, no. 7, pp. 975-978
Publication Year
2009
Abstract
A protease was purified from Bacillus sp. DJ isolated from Doenjang, a traditional Korean fermented food. Its molecular weight (MW) and isoelectric point (p I) were 18-19 kDa and 6.0-6.5 using 1- or 2-D fibrin zymography, respectively. The protease was optimally active at pH 9 and 55°C. Activity was inhibited by 1 mM PMSF, but not by EDTA, EGTA, aprotinin, or leupeptin, indicating that the protease is a serine protease. By using a new electrophoretic technique, multiple loading of O'Farrell-type isoelectric focusing (IEF) slab gel, the first amino acid residues of the N-terminal sequence of the protease were determined as HPLVLVDPIL, which is 80% identical with serine proteases of the subtilase family.
Keyword
isoelectric focusingMALDI-TOF/MSproteasetwo-dimensional electrophoresiszymography
ISSN
0141-5492
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s10529-009-9962-z
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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