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Published on: February 15, 2012
[Activity of the SrfAC-A domain from Bacillus subtilis fmbj]
Lixia Liu1, Zhaoxin Lu, Fengxia Lv
1College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. hzdaxia@126.com
Objective:
We studied the A domain of surfactin synthase in vitro to obtain new surfactin analogues.
Methods:
We cloned the srfAC-A gene from Bacillus subtilis fmbj by PCR, and constructed a recombinant expression vector named pET-23a-srfAC-A. Furthermore, the SrfAC-A domain was expressed in E. coli BL21 (DE3) and purified by Ni-NTA agarose column. Then the activity of srfAC-A domain was detected.
Results:
The srfAC-A domain had specificity towards Ile, but almost no activity to other amino acids.
Conclusion:
The independent A domain from surfactin synthase had selectivity to specific amino acids in vitro.
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