Serine bacteriolytic protease L1 of Lysobacter sp. XL1 complexed with protease inhibitor AEBSF: features of interaction

Kudryakova, Irina V.; Габдулхаков, А.Г.; Tishchenko, Svetlana; Afoshin, Alexey S.; Vasilyeva, Natalia V.

doi:10.1016/j.procbio.2019.02.013

Cited by 3 publications

(1 citation statement)

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“…Our main works investigate such enzymes in Lysobacter sp. XL1 [ 11 , 12 , 13 , 14 , 15 , 16 , 17 ]. Our recent research has been related to the study of antimicrobial potential in L. capsici VKM B-2533 T [ 6 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

The First Homologous Expression System for the β-Lytic Protease of Lysobacter capsici VKM B-2533T, a Promising Antimicrobial Agent

Kudryakova

Afoshin

Leontyevskaya

et al. 2022

IJMS

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A successful homologous expression system based on Lysobacter capsici VKM B-2533T and the plasmid pBBR1-MCS5 was first developed for a promising bacteriolytic enzyme of this bacterium, β-lytic protease (Blp). In the expression strains, blp gene expression under the regulation of the GroEL(A) and T5 promoters increased by 247- and 667-fold, respectively, as compared with the wild-type strain. After the cultivation of the expression strains L. capsici PGroEL(A)-blp and L. capsici PT5-blp, the Blp yield increased by 6.7- and 8.5-fold, respectively, with respect to the wild-type strain. The cultivation of the expression strain L. capsici PT5-blp was successfully scaled up. Under fermentation conditions the yield of the enzyme increased by 1.6-fold. The developed homologous system was used to express the gene of the bacteriolytic serine protease (Serp) of L. capsici VKM B-2533T. The expression of the serp gene in L. capsici PT5-serp increased by 585-fold. The developed homologous system for the gene expression of bacteriolytic Lysobacter enzymes is potentially biotechnologically valuable, and is promising for creating highly efficient expression strains.

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