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Eco-friendly zinc oxide nanoparticle biosynthesis powered by probiotic bacteria.
Appl Microbiol Biotechnol
January 2025
School of Environmental and Life Sciences, The University of Newcastle, Callaghan, NSW, 2308, Australia.
The rapid advancement of nanotechnology, particularly in the realm of pharmaceutical sciences, has significantly transformed the potential for treating life-threatening diseases. A pivotal aspect of this evolution is the emergence of "green nanotechnology," which emphasizes the environmentally sustainable synthesis of raw materials through biological processes. This review focuses on the biological synthesis and application of zinc oxide (ZnO) nanoparticles (NPs) from probiotic bacteria, particularly those sourced from wastewater.
View Article and Find Full Text PDFProbiotic-based adsorbent mitigates aflatoxin B1 toxicity in Piaractus mesopotamicus: assessing well-being via changes in tissue architecture and digestive enzyme activity.
Vet Res Commun
January 2025
Faculdade de Ciências Agrárias, Universidade Federal da Grande Dourados, Rodovia Dourados - Itahum, km 12, Cidade Universitária, Dourados, MS, Brasil.
Aflatoxin is a mycotoxin produced by fungi of the genus Aspergillus that is present in various foods. Probiotics are well-established products in aquaculture, and due to their effective contribution to the intestine, they can be used as an aflatoxin adsorbent. This study evaluated the effects of aflatoxin B1 (AFB1) on enzymatic activity and intestinal function in Piaractus mesopotamicus (pacu) fingerlings fed diets containing a probiotic-based adsorbent (PBA).
View Article and Find Full Text PDFBioactivities of secondary metabolites of two actinomycetes Streptomyces parvulus GloL3, and Streptomyces lienomycini SK5, endophytes of two Indian medicinal herbs- Globba marantina L. and Selaginella kraussiana (Kunze) A. Braun.
Braz J Microbiol
January 2025
Microbiology and Microbial Biotechnology Laboratory, Department of Botany and Forestry, Vidyasagar University, 721102, Midnapore, West Bengal, India.
Endophytic actinomycetes are potential sources of novel pharmaceutically active metabolites, significantly advancing natural product research. In the present investigation, secondary metabolites from two endophytic actinomycetes, Streptomyces parvulus GloL3, and Streptomyces lienomycini SK5, isolated from medicinal plant taxa, Globba marantina, and Selaginella kraussiana, exhibited broad-spectrum bioactivity. Ethyl Acetate (EA) extract of SK5 showed antimicrobial activity against nine human pathogens, including Methicillin-resistant Staphylococcus aureus (MRSA), Candida tropicalis, and C.
View Article and Find Full Text PDFCharacterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.
Arch Microbiol
January 2025
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, 43400, Malaysia.
Bacteriophages produce endolysins at the end of the lytic cycle, which are crucial for lysing the host cells and releasing virion progeny. This lytic feature allows endolysins to act as effective antimicrobial alternatives when applied exogenously. Staphylococcal endolysins typically possess a modular structure with one or two enzymatically active N-terminal domains (EADs) and a C-terminal cell wall binding domain (CBD).
View Article and Find Full Text PDFHHV-6B ribonucleotide reductase sequesters NF-κB subunit p65 to inhibit innate immune responses.
iScience
February 2025
Division of Clinical Virology, Center for Infectious Diseases, Kobe University Graduate School of Medicine, Kobe, Hyogo, Japan.
Human herpesvirus 6B (HHV-6B) belongs to the genus of the betaherpesvirus subfamily, causing exanthema subitum and encephalitis. Although viral ribonucleotide reductase (RNR) is conserved in betaherpesviruses, it has lost its enzymatic activity. Human cytomegalovirus (HCMV) belongs to the other betaherpesvirus genus, ; its RNR inhibits nuclear factor-kappa B (NF-κB) signaling via interaction with the adaptor molecule RIPK1.
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