Hemolytic activity

Codon optimization enhances the expression of porcine β-defensin-2 in Escherichia coli

C. Y. Gao, Xu, T. T., Zhao, Q. J., and Li, C. L., Codon optimization enhances the expression of porcine β-defensin-2 in Escherichia coli, vol. 14, pp. 4978-4988, 2015.

Porcine β-defensin-2 (pBD2) is a cationic antimicrobial peptide that has therapeutic potential. The amount of pBD2 in nature is limited, and the expression of pBD2 in Escherichia coli is low, probably because a different gene codon is used by prokaryotic organisms to that used by eukaryotes. Codon preference optimization is one of the ways to increase heterologous expression of pBD2. To achieve high expression of pBD2, the pBD2 gene was redesigned according to the preferred codon in E. coli without altering the amino acid sequence.

Isolation and molecular characterization of a novel strain of Bacillus with antifungal activity from the sorghum rhizosphere

S. C. Martinez-Absalon, Orozco-Mosqueda, Mdel C., Martinez-Pacheco, M. M., Farias-Rodriguez, R., Govindappa, M., and Santoyo, G., Isolation and molecular characterization of a novel strain of Bacillus with antifungal activity from the sorghum rhizosphere, vol. 11, pp. 2665-2673, 2012.

We looked for bacterial strains with antifungal activity in the sorghum rhizosphere. A prescreening procedure to search for hemolytic activity among the isolated strains allowed us to detect good fungitoxic activity in a bacterial isolate that we named UM96. This bacterial isolate showed strong growth inhibition in bioassays against the pathogens Diaporthe phaseolorum, Colletotrichum acutatum, Rhizoctonia solani, and Fusarium oxysporum.

Subscribe to Hemolytic activity