Production, Partial Purification and Based SDS-PAGE Profiles of Caseinolytic Enzyme in two Bacillus Strains Isolated from Fermented Cassava leaves "Ntoba mbodi" in Congo Brazzaville

Faly, Soloka Mabika Armel; Moyen, Rachel; Nguimbi, Etienne; Ahombo, Gabriel; Ampa, Raoul; Kayath, Aimé Christian; Vouidibio, Alain; Morabandza, Cyr Jonas; Kobawila, Simon Charles

doi:10.22207/jpam.11.1.11

Cited by 2 publications

(3 citation statements)

References 19 publications

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“…The role of the SecYEG translocon in protein secretion is well established, including descriptions of B. subtilis . The Bacillus genus is one of the more commercially interesting bacterial groups, generally recognized as safe, having the potential to produce cellulase [ 34 ], amylase [ 17 ], and proteases [ 18 ]. Studies of members of the Bacillus genus continue to surprise the scientific community.…”

Section: Discussionmentioning

confidence: 99%

“…The ability of the isolates to produce proteases was based on their ability to degrade casein in skim milk. The methodology carried out was previously described [ 18 ].…”

Section: Methodsmentioning

confidence: 99%

“…Although mutants have been described in the literature regarding SecYEG components [ 10 , 14 – 16 ], we use a different approach based on protein-protein interactions for the SecA proteins of the SecYEG system, TasA and TapA [ 12 ]. They are involved in the formation of biofilms and secretion of AmyE and AprE, which represent, respectively, amylase [ 17 ] and proteases [ 18 – 22 ]. For this work, recombinant proteins were fused with targeted proteins.…”

Section: Introductionmentioning

confidence: 99%

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Involvement of the Bacillus SecYEG Pathway in Biosurfactant Production and Biofilm Formation

Okouakoua,

Kayath,

Mokemiabeka

et al. 2024

International Journal of Microbiology

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With Bacillus species, about 30% of extracellular proteins are translocated through the cytoplasmic membrane, coordinated by the Sec translocase. This system mainly consists of the cytoplasmic ATPase SecA and the membrane-embedded SecYEG channel. The purpose of this work was to investigate the effects of the SecYEG export system on the production of industrial biomolecules, such as biosurfactants, proteases, amylases, and cellulases. Fifty-two isolates of Bacillus species were obtained from traditional fermented foods and then characterized using molecular microbiology methods. The isolates secreted exoenzymes that included cellulases, amylases, and proteases. We present evidence that a biosurfactant-like molecule requires the SecA ATPase and the SecYEG membrane channel for its secretion. In addition, we showed that biomolecules involved in biofilm formation required the SecYEG pathway. This work presents a novel seven-target fragment multiplex PCR assay capable of identification at the species level of Bacillus through a unique SecDF chromosomal gene. The bacterial membrane protein SecDF allowed the discrimination of Bacillus subtilis, B. licheniformis, B. amyloliquefaciens, and B. sonorensis. SecA was able to interact with AprE, AmyE, and TasA. The Rose Bengal inhibitor of SecA crucially affected the interaction of AprE, AmyE, TapA, and TasA with recombinant Gst-SecA. The Rose Bengal prevented Bacillus species from secreting and producing proteases, cellulases, amylases, and biosurfactant-like molecules. It also inhibited the formation of biofilm cell communities. The data support, for the first time, that the SecYEG translocon mediates the secretion of a biosurfactant-like molecule.

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Section: Discussionmentioning

confidence: 99%

“…The ability of the isolates to produce proteases was based on their ability to degrade casein in skim milk. The methodology carried out was previously described [ 18 ].…”

Section: Methodsmentioning

confidence: 99%