Transcriptomic Analysis Followed by the Isolation of Extracellular Bacteriolytic Proteases from <i>Lysobacter capsici</i> VKM B-2533<sup>T</sup>
The aim of the study was to search for, isolate and characterize new bacteriolytic enzymes that show promising potential for their use in medicine, agriculture and veterinary. Using a transcriptomic analysis, we annotated in <i>Lysobacter capsici</i> VKM B-2533<sup>T</sup> th...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-07-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/24/14/11652 |
| Summary: | The aim of the study was to search for, isolate and characterize new bacteriolytic enzymes that show promising potential for their use in medicine, agriculture and veterinary. Using a transcriptomic analysis, we annotated in <i>Lysobacter capsici</i> VKM B-2533<sup>T</sup> the genes of known bacteriolytic and antifungal enzymes, as well as of antibiotics, whose expression levels increased when cultivated on media conducive to the production of antimicrobial agents. The genes of the secreted putative bacteriolytic proteases were also annotated. Two new bacteriolytic proteases, Serp and Serp3, were isolated and characterized. The maximum bacteriolytic activities of Serp and Serp3 were exhibited at low ionic strength of 10 mM Tris-HCl, and high temperatures of, respectively, 80 °C and 70 °C. The pH optimum for Serp was 8.0; for Serp3, it was slightly acidic, at 6.0. Both enzymes hydrolyzed autoclaved cells of <i>Micrococcus luteus</i> Ac-2230<sup>T</sup>, <i>Proteus vulgaris</i> H-19, <i>Pseudomonas aeruginosa</i> and <i>Staphylococcus aureus</i> 209P. Serp also digested cells of <i>Bacillus cereus</i> 217. Both enzymes hydrolyzed casein and azofibrin. The newly discovered enzymes are promising for developing proteolytic antimicrobial drugs on their basis. |
|---|---|
| ISSN: | 1661-6596 1422-0067 |