21:I[432972,["/_next/static/chunks/bb923814e1f4d2e9.js","/_next/static/chunks/dd3ee9f5b7716ca6.js","/_next/static/chunks/4204a0ae82542ca8.js","/_next/static/chunks/1270dead247da766.js","/_next/static/chunks/6e1aa89a642f40be.js","/_next/static/chunks/2d7aa753e81324a8.js","/_next/static/chunks/8ffd0b71567920d8.js","/_next/static/chunks/67ea6dfd21f16c5f.js","/_next/static/chunks/24eb4379f68013fd.js","/_next/static/chunks/b8cd775ffdf935bd.js","/_next/static/chunks/983103cd9eb7b428.js","/_next/static/chunks/263f2cdcb9aa2341.js","/_next/static/chunks/294b9525248c8e5f.js"],"default"] 22:T47c,Bovine lactoferrin N-lobe plays an important key in the nonimmunological defense system. In this work, the most suitable promoter P_veg was selected and the fragment coding bovine lactoferrin N-lobe was optimized according to codon bias of Bacillus. The recombinant plasmid pMA0911-P_veg-mBLF-N was introduced into Baicillus subtilis 168 to create B. subtilis/pMA0911-P_veg-mBLF-N. The bovine lactoferrin N-lobe was highly expressed at 28 °C for 15 h. Its purified protein was obtained with 16.5 mg/L and a purity of 93.6% using ammonium sulfate precipitation, Ni-NTA, and molecular exclusion. About 200 ng/mL purified bovine lactoferrin N-lobe completely inhibited cell-growth of Escherichia coli JM109 (DE3), 70.3% of Pseudomonas aeruginosa CGMCC 1.6740, and 41.5% of Staphylococcus aureus CGMCC 1.282. To our knowledge, this is the first report about active expression, purification, and characterization of bovine lactoferrin N-lobe in safe bacterium B. subtilis, which opens an available application way in the biomedical and food industries.23:T431,The expression and purification of melittin (MET) in microbials are difficult because of its antibacterial activities. In this work, MET was fused with a glutathione-S-transferase (GST) tag and expressed in Escherichia coli to overcome its lethality to host cells. The fusion protein GST-MET was highly expressed and then purified by glutathione sepharose high-performance affinity chromatography, digested with prescission protease, and further purified by Superdex Peptide 10/300 GL chromatography. Finally, 3.5 mg/L recombinant melittin (rMET) with a purity of >90% was obtained; its antibacterial activities against Gram-positive Bacillus pumilus and Staphylococcus pasteuri were similar to those of commercial MET. A circular dichroism spectroscopic assay showed that the rMET peptide secondary structure was similar to those of the commercial form. To our knowledge, this is the report of the preparation of active pure rMET with no tags. The successful expression and purification of rMET will enable large-scale, industrial biosynthesis of MET.

#	Concept	H-Index	Publications	Citations
1	Engineering	1	1	10
2	Medicine	1	1	10
3	Biochemistry	1	1	10
4	Metabolism	1	1	10
5	Microbiology	1	1	10

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