Among the trace elements, selenium (Se) has great demand as a health supplement. Compared to its other forms, selenium nanoparticles have minor toxicity, superior reactivity, and excellent bioavailability. The present study was conducted to produce selenium nanoparticles (SeNPs) via a biosynthetic approach using probiotic Bacillus subtilis BSN313 in an economical and easy manner. The BSN313 exhibited a gradual increase in Se reduction and production of SeNPs up to 5–200 µg/mL of its environmental Se. However, the capability was decreased beyond that concentration. The capacity for extracellular SeNP production was evidenced by the emergence of red color, then confirmed by a microscopic approach. Produced SeNPs were purified, freeze-dried, and subsequently characterized systematically using UV–Vis spectroscopy, FTIR, Zetasizer, SEM–EDS, and TEM techniques. SEM–EDS analysis proved the presence of selenium as the foremost constituent of SeNPs. With an average particle size of 530 nm, SeNPs were shown to have a −26.9 (mV) zeta potential and −2.11 µm cm/Vs electrophoretic mobility in water. SeNPs produced during both the 24 and 48 h incubation periods showed good antioxidant activity in terms of DPPH and ABST scavenging action at a concentration of 150 µg/mL with no significant differences (p > 0.05). Moreover, 200 µg/mL of SeNPs showed antibacterial reactivity against Escherichia coli ATCC 8739, Staphylococcus aureus ATCC 9027, and Pseudomonas aeruginosa ATCC 25923. In the future, this work will be helpful to produce biogenic SeNPs using probiotic Bacillus subtilis BSN313 as biofactories, with the potential for safe use in biomedical and nutritional applications.

Biosurfactants are a functionally and structurally heterogeneous group of biomolecules produced by multiple filamentous fungi, yeast, and bacteria, and characterized by their distinct surface and emulsifying ability. The genus Bacillus is well studied for biosurfactant production as it produces various types of lipopeptides, for example, lichenysins, bacillomycin, fengycins, and surfactins. Bacillus lipopeptides possess a broad spectrum of biological activities such as antimicrobial, antitumor, immunosuppressant, and antidiabetic, in addition to their use in skincare. Moreover, Bacillus lipopeptides are also involved in various food products to increase the antimicrobial, surfactant, and emulsification impact. From the previously published articles, it can be concluded that biosurfactants have strong potential to be used in food, healthcare, and agriculture. In this review article, we discuss the versatile functions of lipopeptide Bacillus species with particular emphasis on the biological activities and their applications in food.

The present study describes the production of biosurfactant from isolate B. licheniformis Ali5. Seven different, previously-reported minimal media were screened for biosurfactant production, and two selected media were further optimized for carbon source. Further, various fermentation conditions such as (pH 2–12, temperature 20–50 °C, agitation speed 100–300 rpm, NaCl (0–30 g·L⁻¹) were investigated. The partially purified biosurfactant was characterized by Fourier transform infrared spectroscopy (FTIR) and matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy (MALDI-TOF MS) and found a lipopeptide mixture, similar to lichenysin-A. Biosurfactant reduced surface tension from 72.0 to 26.21 ± 0.3 and interfacial tension by 0.26 ± 0.1 mN·m⁻¹ respectively, biosurfactant yield under optimized conditions was 1 g·L⁻¹, with critical micelle concentration (CMC) of 21 mg·L⁻¹ with high emulsification activity of (E24) 66.4 ± 1.4% against crude oil. Biosurfactant was found to be stable over extreme conditions. It also altered the wettability of hydrophobic surface by changing the contact angle from 49.76° to 16.97°. Biosurfactant efficiently removed (70-79%) motor oil from sand, with an efficiency of more than 2 fold as compared without biosurfactant (36–38%). It gave 32% additional oil recovery over residual oil saturation upon application to a sand-packed column. These results are indicative of potential application of biosurfactant in wettability alteration and ex-situ microbial enhanced oil recovery.

In the present study, lysozyme was purified by the following multi-step methodology: salt (ammonium sulfate) precipitation, dialysis, and ultrafiltration. The lysozyme potential was measured by enzymatic activity after each purification step. However, after ultrafiltration, the resulting material was considered extra purified. It was concentrated in an ultrafiltration centrifuge tube, and the resulting protein/lysozyme was used to determine its bactericidal potential against five bacterial strains, including three gram-positive (Bacillus subtilis 168, Micrococcus luteus, and Bacillus cereus) and two gram-negative (Salmonella typhimurium and Pseudomonas aeruginosa) strains. The results of ZOI and MIC/MBC showed that lysozyme had a higher antimicrobial activity against gram-positive than gram-negative bacterial strains. The results of the antibacterial activity of lysozyme were compared with those of ciprofloxacin (antibiotic). For this purpose, two indices were applied in the present study: antimicrobial index (AMI) and percent activity index (PAI). It was found that the purified lysozyme had a higher antibacterial activity against Bacillus cereus (AMI/PAI; 1.01/101) and Bacillus subtilis 168 (AMI/PAI; 1.03/103), compared to the antibiotic (ciprofloxacin) used in this study. Atomic force microscopy (AFM) was used to determine the bactericidal action of the lysozyme on the bacterial cell. The purified protein was further processed by gel column chromatography and the eluate was collected, its enzymatic activity was 21.93 U/mL, while the eluate was processed by native-PAGE. By this analysis, the un-denatured protein with enzymatic activity of 40.9 U/mL was obtained. This step shows that the protein (lysozyme) has an even higher enzymatic potential. To determine the specific peptides (in lysozyme) that may cause the bactericidal potential and cell lytic/enzymatic activity, the isolated protein (lysozyme) was further processed by the SDS-PAGE technique. SDS-PAGE analysis revealed different bands with sizes of 34 kDa, 24 kDa, and 10 kDa, respectively. To determine the chemical composition of the peptides, the bands (from SDS-PAGE) were cut, enzymatically digested, desalted, and analyzed by LC-MS (liquid chromatography-mass spectrometry). LC-MS analysis showed that the purified lysozyme had the following composition: the number of proteins in the sample was 56, the number of peptides was 124, and the number of PSMs (peptide spectrum matches) was 309. Among them, two peptides related to lysozyme and bactericidal activities were identified as: A0A1Q9G213 (N-acetylmuramoyl-L-alanine amidase) and A0A1Q9FRD3 (D-alanyl-D-alanine carboxypeptidase). The corresponding protein sequence and nucleic acid sequence were determined by comparison with the database.

Naturally occurring monoglyceride esters of fatty acids have been associated with a broad spectrum of antimicrobial activities. We used an automated turbidimetric method to measure the MIC... HIGHLIGHTS The antimicrobial activity of monoglycerides depends on the length of their carbon chains. The MICs of monocaprin against S. aureus and E. coli were 0.32 and 2.5 mg/mL, respectively. Mon...