Background:
Bacteriocins (Bac1, Bac2, and Bac3) from Weissella confusa MBF8-1, weissellicin-
MBF, have been reported as potential alternative substances as well as complements to the existing
antibiotics against many antimicrobial-resistant pathogens. Previously, the genes encoded in the
large plasmid, pWcMBF8-1, and the spermicidal activity of their synthetic peptides, originally discovered
Indonesia, have been studied. Three synthetic bacteriocins peptides of this weissellicin-MBF have
been reported for their potential activities, i.e. antibacterial and spermicidal.
Objective:
The aim of this study was to construct the recombinant Bacteriocin (r-Bac) genes, as well as
to investigate the gene expressions and their functional analysis.
Method:
Here, the recombinant Bacteriocin (r-Bac) genes were constructed and the recombinant peptides
(r-Bac1, r-Bac2, and r-Bac3) in B. subtilis DB403 cells were produced on a large scale. After purification,
using the His-tag affinity column, their potential bioactivities were measured as well as their
antibacterial minimum inhibitory concentrations against Leuconostoc mesenteroides and Micrococcus
luteus, were determined.
Results:
Pure His-tag-recombinant Bac1, Bac2, and Bac3 were obtained and they could inhibit the
growth of L. mesenteroides and M. luteus.
Conclusion:
The recombinant bacteriocin could be obtained although with weak activity in inhibiting
gram-positive bacterial growth.
Coenzyme- and His-tag-induced crystallization of octopine dehydrogenase