Mycoprotein is an alternative protein produced through fungal fermentation. However, it typically relies on refined glucose syrup derived from starch, which can be costly and unsustainable. This study investigates the potential of soybean processing by-products (okara and soy whey) as alternative substrates for producing mycoprotein using Aspergillus oryzae. A. oryzae was cultured for 7 days at 30 °C in diluted okara (1:50) and soy whey (1:1) with or without agitation (100 rpm). Soy whey produced higher biomass yields (369.2–408.8 mg dry biomass/g dry substrate), but had a lower biomass concentration (0.783–0.867 g dry weight/L). Conversely, okara produced a higher biomass concentration (2.02 g dry weight/L) with a yield of 114.7 mg dry biomass/g dry substrate. However, biomass formation in okara was only observed in static conditions, as agitation caused biomass to entangle with soy pulp, hampering its production. Additionally, okara tended to release protein into the media, while soy whey accumulated protein within the biomass, reaching up to 53% w/w protein content. The results of this study provide a promising approach to addressing both soybean processing waste reduction and food security concerns.

Pediococcus acidilactici has gained research and commercial interest due to its outstanding probiotic properties, yet its survival during storage and consumption requires improvement. This study aims to enhance P. acidilactici survival using spray drying encapsulation. Different inlet air temperatures (120 °C, 150 °C, and 170 °C) and whey protein isolate (WPI):gum arabic (GA) ratios (1:1, 3:1, 1:3) were tested. Cell viability was significantly (p < 0.05) affected by the inlet temperature but not the WPI:GA ratio. Increasing the inlet temperature to 170 °C significantly decreased P. acidilactici viability by 1.36 log cycles, from 8.61 log CFU/g to 7.25 log CFU/g. The inlet temperature of 150 °C resulted in a powder yield (63.12%) higher than at 120 °C (58.97%), as well as significantly (p < 0.05) lower moisture content (5.71%) and water activity (a_w 0.21). Viable cell counts in all encapsulated P. acidilactici were maintained at 5.24–6.75 log CFU/g after gastrointestinal tract (GIT) simulation, with WPI:GA of 3:1 and inlet temperature 150 °C having the smallest log reduction (0.3 log cycles). All samples containing different WPI:GA ratios maintained sufficient viability (>7 log CFU/g) during the first three weeks of storage at 25 °C. These results could provide insights for further developing P. acidilactici as commercial probiotic products.

This study delves into the production and antimicrobial characteristics of cell-free supernatants from Pediococcus acidilactici (CFSs-Pa). Antimicrobial activity was initially observed in CFS-Pa harvested after 12 h of incubation and increased up to the late stationary phase at 48 h. The increase in antimicrobial activity did not align with total protein content, pointing to other factors linked to the accumulation of organic acids, particularly lactic acid. The SDS-PAGE analysis also indicated that the expected proteinaceous compound (pediocin) was not observed in CFS-Pa. Further investigations suggested that the antimicrobial properties of CFS-Pa were exclusively due to organic acids. The MIC values confirmed potent antimicrobial activity, particularly at a 10% dilution of CFS-Pa in MRS broth. The time–kill assays demonstrated bactericidal activity against EHEC, Listeria monocytogenes, and Staphylococcus aureus by 12 h, 18 h, and 24 h using a 10% dilution of CFS-Pa. Additionally, CFS-Pa exhibited dose-dependent antioxidant activity, requiring a 70% (v/v) concentration to inhibit DPPH scavenging activity by 50%. All the experimental results suggested potential applications of CFS-Pa in food preservation. An attempt to incorporate CFS-Pa into bacterial cellulose (BC) for edible food packaging demonstrated promising antimicrobial results, particularly against L. monocytogenes and S. aureus, with room for optimization.

Patients with burn injuries are at high risk of bacterial infection due to the loss of the skin barrier, often leading to complications that contribute to increasing death tolls from burn injuries. The formation of biofilms in bacteria increases its survival rate, especially in the rise of antibiotic resistance cases, which ineffectively combats biofilm production. This research explores the use of two types of cationic antimicrobial peptides, LL-37 and CATH2, commonly originating from humans and chickens, respectively, as a form of host defense in preventing the formation of biofilms by one of the most common pathogenic bacterial strains in severe burn wounds, Pseudomonas aeruginosa, through inhibition in its LPS region. In silico analyses were performed using AlphaFold, GLYCAM-Web, YASARA, and AutoDock Vina. It was found that the CATH-2 model has the strongest binding affinity towards the three types of LPS—alginate, Pel, and Psl—scoring between -5.5 and -6.0 kcal/mol, as opposed to the score range of -4.1 to -6.0 for LL-37. However, the LL-37 model is considered more precise than the CATH-2 model overall, meaning the in silico results of the former are likely more accurate in real life than the latter. These results suggest the utilization of the two peptides as treatments in severe burn cases. In future developments, the application of genetically engineered plasmid-inserted Staphylococcus epidermidis, a commensal bacterium commonly found on human skin, to produce peptides may be considered.

Malaria is an infectious disease caused by Plasmodium spp., a protist whose infection is spread by Anopheles mosquito as a vector. A potential method to counter the infection is through paratransgenesis, a promising genetic control approach. This study proposed a new approach by using a transgene carried in a modified Ti plasmid hosted in Asaia bacterium to carry out two purposes: sensing the presence of Plasmodium protein biomarkers and transferring the toxin transgene to the parasite upon detection, thereby killing it without harming the Asaia carrier. The biosensor mechanism was created by repurposing a TonB dependent iron-uptake transport pathway to transcribe the vir genes of Agrobacterium tumefaciens that facilitate the gene transfer. The aim of this in silico project was to serve as a preliminary study on the likelihood of success of the aforementioned biosensor mechanism. This study utilized Alphafold and RCSB (Research Collaboratory for Structural Bioinformatic Protein Data Bank). As for the research tools: PyMOL, ClusPro website, and PRODIGY (PROtein binDIng enerGY prediction) server was used for data preparation, protein-protein docking and binding affinity analysis respectively. The results were assessed with t-test to analyze the significance of the binding affinity, in comparison to other studies that employed similar methods. The result showed Plasmodium protein GGCS (Gamma-glutamylcysteine synthetase) having the highest binding affinity with FecA (Fe(3+) dicitrate transport protein A). The preliminary data suggested that introducing the toxin transgene may be possible through vir gene transcription from the TonB pathway.